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Coagulation factor IX (EC 3.4.21.22) (Christmas factor) (Plasma thromboplastin component) (PTC) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain]

 FA9_HUMAN               Reviewed;         461 AA.
P00740; A8K9N4; F2RM36; Q5FBE1; Q5JYJ8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
25-OCT-2017, entry version 237.
RecName: Full=Coagulation factor IX {ECO:0000303|PubMed:3857619};
EC=3.4.21.22 {ECO:0000269|PubMed:12444082, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0000269|PubMed:2592373};
AltName: Full=Christmas factor;
AltName: Full=Plasma thromboplastin component;
Short=PTC;
Contains:
RecName: Full=Coagulation factor IXa light chain;
Contains:
RecName: Full=Coagulation factor IXa heavy chain;
Flags: Precursor;
Name=F9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=6959130; DOI=10.1073/pnas.79.21.6461;
Kurachi K., Davie E.W.;
"Isolation and characterization of a cDNA coding for human factor
IX.";
Proc. Natl. Acad. Sci. U.S.A. 79:6461-6464(1982).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=6687940; DOI=10.1093/nar/11.8.2325;
Jaye M., de la Salle H., Schamber F., Balland A., Kohli V.,
Findeli A., Tolstoshev P., Lecocq J.-P.;
"Isolation of a human anti-haemophilic factor IX cDNA clone using a
unique 52-base synthetic oligonucleotide probe deduced from the amino
acid sequence of bovine factor IX.";
Nucleic Acids Res. 11:2325-2335(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-194.
PubMed=6329734;
Anson D.S., Choo K.H., Rees D.J.G., Giannelli F., Gould K.G.,
Huddleston J.A., Brownlee G.G.;
"The gene structure of human anti-haemophilic factor IX.";
EMBO J. 3:1053-1060(1984).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-194.
PubMed=2994716; DOI=10.1021/bi00335a049;
Yoshitake S., Schach B.G., Foster D.C., Davie E.W., Kurachi K.;
"Nucleotide sequence of the gene for human factor IX (antihemophilic
factor B).";
Biochemistry 24:3736-3750(1985).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-194, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND PARTIAL PROTEIN SEQUENCE.
PubMed=3857619; DOI=10.1073/pnas.82.9.2847;
McGraw R.A., Davis L.M., Noyes C.M., Lundblad R.L., Roberts H.R.,
Graham J.B., Stafford D.W.;
"Evidence for a prevalent dimorphism in the activation peptide of
human coagulation factor IX.";
Proc. Natl. Acad. Sci. U.S.A. 82:2847-2851(1985).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
TISSUE=Liver;
Sata S., Yonemitsu Y., Nakagawa K., Sueishi K.;
"Alternative splicing variant of Homo sapiens coagulation factor IX
lacking EGF like domain.";
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-461.
SeattleSNPs variation discovery resource;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Nguyen D.T., Nguyen P.V., Nong H.V.;
"Homo sapiens coagulation factor IX (F9), mRNA.";
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-84, VARIANT HEMB GLN-43,
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PROTEOLYTIC
CLEAVAGE.
PubMed=8295821;
de la Salle C., Charmantier J.L., Ravanat C., Ohlmann P.,
Hartmann M.L., Schuhler S., Bischoff R., Ebel C., Roecklin D.,
Balland A.;
"The Arg-4 mutant factor IX Strasbourg 2 shows a delayed activation by
factor XIa.";
Nouv. Rev. Fr. Hematol. 35:473-480(1993).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 36-326 (ISOFORM 1).
TISSUE=Liver;
PubMed=6089357; DOI=10.1007/BF01534851;
Jagadeeswaran P., Lavelle D.E., Kaul R., Mohandas T., Warren S.T.;
"Isolation and characterization of human factor IX cDNA:
identification of Taq I polymorphism and regional assignment.";
Somat. Cell Mol. Genet. 10:465-473(1984).
[15]
PROTEIN SEQUENCE OF 47-461, VARIANT HEMB TRP-226, FUNCTION, CATALYTIC
ACTIVITY, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, SUBUNIT, AND
TISSUE SPECIFICITY.
PubMed=2592373;
Suehiro K., Kawabata S., Miyata T., Takeya H., Takamatsu J., Ogata K.,
Kamiya T., Saito H., Niho Y., Iwanaga S.;
"Blood clotting factor IX BM Nagoya. Substitution of arginine 180 by
tryptophan and its activation by alpha-chymotrypsin and rat mast cell
chymase.";
J. Biol. Chem. 264:21257-21265(1989).
[16]
PROTEIN SEQUENCE OF 47-52, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
CHARACTERIZATION OF VARIANTS HEMB GLN-43; LEU-43 AND TRP-43,
CALCIUM-BINDING, AND PROTEOLYTIC CLEAVAGE.
PubMed=9169594; DOI=10.1042/bj3230629;
Wojcik E.G., Van Den Berg M., Poort S.R., Bertina R.M.;
"Modification of the N-terminus of human factor IX by defective
propeptide cleavage or acetylation results in a destabilized calcium-
induced conformation: effects on phospholipid binding and activation
by factor XIa.";
Biochem. J. 323:629-636(1997).
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 290-359.
PubMed=3340835; DOI=10.1126/science.3340835;
Stoflet E.S., Koeberl D.D., Sarkar G., Sommer S.S.;
"Genomic amplification with transcript sequencing.";
Science 239:491-494(1988).
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-461.
PubMed=8236150;
de la Salle C., Charmantier J.L., Baas M.-J., Schwartz A.,
Wiesel M.L., Grunebaum L., Cazenave J.-P.;
"A deletion located in the 3' non translated part of the factor IX
gene responsible for mild haemophilia B.";
Thromb. Haemost. 70:370-371(1993).
[19]
HYDROXYLATION AT ASP-110.
PubMed=6688526; DOI=10.1016/0006-291X(83)90961-0;
McMullen B.A., Fujikawa K., Kisiel W.;
"The occurrence of beta-hydroxyaspartic acid in the vitamin K-
dependent blood coagulation zymogens.";
Biochem. Biophys. Res. Commun. 115:8-14(1983).
[20]
PROTEOLYTIC PROCESSING, AND ACTIVE SITE.
PubMed=659613; DOI=10.1172/JCI109073;
di Scipio R.G., Kurachi K., Davie E.W.;
"Activation of human factor IX (Christmas factor).";
J. Clin. Invest. 61:1528-1538(1978).
[21]
CALCIUM-BINDING, AND DOMAIN.
PubMed=6425296;
Morita T., Isaacs B.S., Esmon C.T., Johnson A.E.;
"Derivatives of blood coagulation factor IX contain a high affinity
Ca2+-binding site that lacks gamma-carboxyglutamic acid.";
J. Biol. Chem. 259:5698-5704(1984).
[22]
ERRATUM.
Morita T., Isaacs B.S., Esmon C.T., Johnson A.E.;
J. Biol. Chem. 260:2583-2583(1985).
[23]
STRUCTURE OF CARBOHYDRATE ON SER-99.
PubMed=2511201;
Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T., Takao T.,
Shimonishi Y., Iwanaga S.;
"Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-
Glc) O-glycosidically linked to a serine residue in the first
epidermal growth factor-like domain of human factors VII and IX and
protein Z and bovine protein Z.";
J. Biol. Chem. 264:20320-20325(1989).
[24]
STRUCTURE OF CARBOHYDRATE ON SER-99.
PubMed=2129367;
Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.;
"A new trisaccharide sugar chain linked to a serine residue in the
first EGF-like domain of clotting factors VII and IX and protein Z.";
Adv. Exp. Med. Biol. 281:121-131(1990).
[25]
FUNCTION, AND PROTEOLYTIC CLEAVAGE.
PubMed=1730085;
Rawala-Sheikh R., Ahmad S.S., Monroe D.M., Roberts H.R., Walsh P.N.;
"Role of gamma-carboxyglutamic acid residues in the binding of factor
IXa to platelets and in factor-X activation.";
Blood 79:398-405(1992).
[26]
STRUCTURE OF CARBOHYDRATE ON SER-107.
PubMed=1517205;
Nishimura H., Takao T., Hase S., Shimonishi Y., Iwanaga S.;
"Human factor IX has a tetrasaccharide O-glycosidically linked to
serine 61 through the fucose residue.";
J. Biol. Chem. 267:17520-17525(1992).
[27]
GLYCOSYLATION AT THR-205 AND THR-215.
PubMed=8172892; DOI=10.1021/bi00183a021;
Agarwala K.L., Kawabata S., Takao T., Murata H., Shimonishi Y.,
Nishimura H., Iwanaga S.;
"Activation peptide of human factor IX has oligosaccharides O-
glycosidically linked to threonine residues at 159 and 169.";
Biochemistry 33:5167-5171(1994).
[28]
PHOSPHORYLATION AT SER-114.
Harris R.J., Papac D.I., Truong L., Smith K.J.;
"Partial phosphorylation of serine-68 in EGF-1 of human factor IX.";
(In) Proceedings of XIth international conference on methods in
protein structure analysis, pp.50-50, Annecy (1996).
[29]
SULFATION AT TYR-201, AND PHOSPHORYLATION AT SER-204.
PubMed=11133752; DOI=10.1182/blood.V97.1.130;
Arruda V.R., Hagstrom J.N., Deitch J., Heiman-Patterson T.,
Camire R.M., Chu K., Fields P.A., Herzog R.W., Couto L.B.,
Larson P.J., High K.A.;
"Posttranslational modifications of recombinant myotube-synthesized
human factor IX.";
Blood 97:130-138(2001).
[30]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-305; LYS-311; TYR-312 AND
TYR-391.
PubMed=12444082; DOI=10.1074/jbc.M210722200;
Sichler K., Kopetzki E., Huber R., Bode W., Hopfner K.P.,
Brandstetter H.;
"Physiological fIXa activation involves a cooperative conformational
rearrangement of the 99-loop.";
J. Biol. Chem. 278:4121-4126(2003).
[31]
GLYCOSYLATION AT SER-99.
PubMed=21949356; DOI=10.1073/pnas.1109696108;
Takeuchi H., Fernandez-Valdivia R.C., Caswell D.S., Nita-Lazar A.,
Rana N.A., Garner T.P., Weldeghiorghis T.K., Macnaughtan M.A.,
Jafar-Nejad H., Haltiwanger R.S.;
"Rumi functions as both a protein O-glucosyltransferase and a protein
O-xylosyltransferase.";
Proc. Natl. Acad. Sci. U.S.A. 108:16600-16605(2011).
[32]
GLYCOSYLATION AT THR-85; SER-99; SER-107; THR-205; THR-215 AND
THR-225, PHOSPHORYLATION AT SER-204 AND THR-205, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=25456591; DOI=10.1016/j.chroma.2014.10.046;
Huang L.J., Lin J.H., Tsai J.H., Chu Y.Y., Chen Y.W., Chen S.L.,
Chen S.H.;
"Identification of protein O-glycosylation site and corresponding
glycans using liquid chromatography-tandem mass spectrometry via
mapping accurate mass and retention time shift.";
J. Chromatogr. A 1371:136-145(2014).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[34]
STRUCTURE BY NMR OF 47-93.
PubMed=7713897; DOI=10.1074/jbc.270.14.7980;
Freedman S.J., Furie B.C., Furie B., Baleja J.D.;
"Structure of the metal-free gamma-carboxyglutamic acid-rich membrane
binding region of factor IX by two-dimensional NMR spectroscopy.";
J. Biol. Chem. 270:7980-7987(1995).
[35]
STRUCTURE BY NMR OF 47-93.
PubMed=7547952; DOI=10.1021/bi00038a005;
Freedman S.J., Furie B.C., Furie B., Baleja J.D.;
"Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich
domain of factor IX.";
Biochemistry 34:12126-12137(1995).
[36]
STRUCTURE BY NMR OF 47-93.
PubMed=8663165; DOI=10.1074/jbc.271.27.16227;
Freedman S.J., Blostein M.D., Baleja J.D., Jacobs M., Furie B.C.,
Furie B.;
"Identification of the phospholipid binding site in the vitamin K-
dependent blood coagulation protein factor IX.";
J. Biol. Chem. 271:16227-16236(1996).
[37]
STRUCTURE BY NMR OF 47-93.
PubMed=9047312; DOI=10.1021/bi962250r;
Li L., Darden T.A., Freedman S.J., Furie B.C., Furie B., Baleja J.D.,
Smith H., Hiskey R.G., Pedersen L.G.;
"Refinement of the NMR solution structure of the gamma-carboxyglutamic
acid domain of coagulation factor IX using molecular dynamics
simulation with initial Ca2+ positions determined by a genetic
algorithm.";
Biochemistry 36:2132-2138(1997).
[38]
STRUCTURE BY NMR OF 91-133.
PubMed=1854745; DOI=10.1021/bi00244a006;
Huang L.H., Cheng H., Pardi A., Tam J.P., Sweeney W.V.;
"Sequence-specific 1H NMR assignments, secondary structure, and
location of the calcium binding site in the first epidermal growth
factor like domain of blood coagulation factor IX.";
Biochemistry 30:7402-7409(1991).
[39]
STRUCTURE BY NMR OF 92-130, AND DISULFIDE BOND.
PubMed=1304885; DOI=10.1002/pro.5560010109;
Baron M., Norman D.G., Harvey T.S., Handford P.A., Mayhew M.,
Tse A.G.D., Brownlee G.G., Campbell I.D.C.;
"The three-dimensional structure of the first EGF-like module of human
factor IX: comparison with EGF and TGF-alpha.";
Protein Sci. 1:81-90(1992).
[40]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 92-130 IN COMPLEX WITH
CALCIUM, AND DISULFIDE BOND.
PubMed=7606779; DOI=10.1016/0092-8674(95)90059-4;
Rao Z., Handford P., Mayhew M., Knott V., Brownlee G.G., Stuart D.;
"The structure of a Ca(2+)-binding epidermal growth factor-like
domain: its role in protein-protein interactions.";
Cell 82:131-141(1995).
[41]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 133-461 IN COMPLEX WITH
CALCIUM.
PubMed=10467148; DOI=10.1016/S0969-2126(99)80125-7;
Hopfner K.-P., Lang A., Karcher A., Sichler K., Kopetzki E.,
Brandstetter H., Huber R., Bode W., Engh R.A.;
"Coagulation factor IXa: the relaxed conformation of Tyr99 blocks
substrate binding.";
Structure 7:989-996(1999).
[42]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 47-91 IN COMPLEX WITH
CALCIUM.
PubMed=14722079; DOI=10.1074/jbc.M314011200;
Huang M., Furie B.C., Furie B.;
"Crystal structure of the calcium-stabilized human factor IX Gla
domain bound to a conformation-specific anti-factor IX antibody.";
J. Biol. Chem. 279:14338-14346(2004).
[43]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 133-191 AND 227-461 OF
MUTANTS PHE-305/THR-311/ALA-365/THR-391 IN COMPLEX WITH CALCIUM AND
SYNTHETIC INHIBITOR, ACTIVE SITE, DISULFIDE BOND, SUBUNIT, AND
PROTEOLYTIC CLEAVAGE.
PubMed=20004170; DOI=10.1016/j.str.2009.10.011;
Zogg T., Brandstetter H.;
"Structural basis of the cofactor- and substrate-assisted activation
of human coagulation factor IXa.";
Structure 17:1669-1678(2009).
[44]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 133-461 IN COMPLEX WITH
CALCIUM, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DISULFIDE BOND.
PubMed=20121198; DOI=10.1021/jm901475e;
Wang S., Beck R., Blench T., Burd A., Buxton S., Malic M., Ayele T.,
Shaikh S., Chahwala S., Chander C., Holland R., Merette S., Zhao L.,
Blackney M., Watts A.;
"Studies of benzothiophene template as potent factor IXa (FIXa)
inhibitors in thrombosis.";
J. Med. Chem. 53:1465-1472(2010).
[45]
X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 133-188 AND 227-461 IN
COMPLEX WITH CALCIUM, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
DISULFIDE BOND.
PubMed=20121197; DOI=10.1021/jm901476x;
Wang S., Beck R., Burd A., Blench T., Marlin F., Ayele T., Buxton S.,
Dagostin C., Malic M., Joshi R., Barry J., Sajad M., Cheung C.,
Shaikh S., Chahwala S., Chander C., Baumgartner C., Holthoff H.P.,
Murray E., Blackney M., Giddings A.;
"Structure based drug design: development of potent and selective
factor IXa (FIXa) inhibitors.";
J. Med. Chem. 53:1473-1482(2010).
[46]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 131-188 AND 227-461 IN
COMPLEX WITH SERPINC1 AND CALCIUM, DISULFIDE BOND, PROTEOLYTIC
CLEAVAGE, AND SUBUNIT.
PubMed=20080729; DOI=10.1073/pnas.0910144107;
Johnson D.J., Langdown J., Huntington J.A.;
"Molecular basis of factor IXa recognition by heparin-activated
antithrombin revealed by a 1.7-A structure of the ternary complex.";
Proc. Natl. Acad. Sci. U.S.A. 107:645-650(2010).
[47]
MOLECULAR PATHOLOGY OF HEMB B.
PubMed=2743975;
Green P.M., Bentley D.R., Mibashan R.S., Nilsson I.M., Giannelli F.;
"Molecular pathology of haemophilia B.";
EMBO J. 8:1067-1072(1989).
[48]
REVIEW ON HEMB VARIANTS.
PubMed=1634040;
Sommer S.S.;
"Assessing the underlying pattern of human germline mutations: lessons
from the factor IX gene.";
FASEB J. 6:2767-2774(1992).
[49]
REVIEW ON HEMB VARIANTS.
PubMed=8392713; DOI=10.1093/nar/21.13.3075;
Giannelli F., Green P.M., High K.A., Sommer S., Poon M.-C., Ludwig M.,
Schwaab R., Reitsma P.H., Goossens M., Yoshioka A., Brownlee G.G.;
"Haemophilia B: database of point mutations and short additions and
deletions -- fourth edition, 1993.";
Nucleic Acids Res. 21:3075-3087(1993).
[50]
VARIANT HEMB HIS-191.
PubMed=6603618; DOI=10.1073/pnas.80.14.4200;
Noyes C.M., Griffith M.J., Roberts H.R., Lundblad R.L.;
"Identification of the molecular defect in factor IX Chapel Hill:
substitution of histidine for arginine at position 145.";
Proc. Natl. Acad. Sci. U.S.A. 80:4200-4202(1983).
[51]
VARIANT HEMB GLN-43, AND CHARACTERIZATION OF VARIANT HEMB GLN-43.
PubMed=3009023; DOI=10.1016/0092-8674(86)90319-3;
Bentley A.K., Rees D.J., Rizza C., Brownlee G.G.;
"Defective propeptide processing of blood clotting factor IX caused by
mutation of arginine to glutamine at position -4.";
Cell 45:343-348(1986).
[52]
VARIANT HEMB GLY-93.
PubMed=3790720;
Davis L.M., McGraw R.A., Ware J.L., Roberts H.R., Stafford D.W.;
"Factor IXAlabama: a point mutation in a clotting protein results in
hemophilia B.";
Blood 69:140-143(1987).
[53]
VARIANT HEMB THR-443.
PubMed=3401602;
Ware J., Davis L., Frazier D., Bajaj S.P., Stafford D.W.;
"Genetic defect responsible for the dysfunctional protein: factor IX
(Long Beach).";
Blood 72:820-822(1988).
[54]
VARIANT HEMB VAL-436.
PubMed=3243764;
Sugimoto M., Miyata T., Kawabata S., Yoshioka A., Fukui H.,
Takahashi H., Iwanaga S.;
"Blood clotting factor IX Niigata: substitution of alanine-390 by
valine in the catalytic domain.";
J. Biochem. 104:878-880(1988).
[55]
VARIANT HEMB GLN-226.
PubMed=2713493;
Monroe D.M., McCord D.M., Huang M.N., High K.A., Lundblad R.L.,
Kasper C.K., Roberts H.R.;
"Functional consequences of an arginine180 to glutamine mutation in
factor IX Hilo.";
Blood 73:1540-1544(1989).
[56]
VARIANT HEMB ARG-442.
PubMed=2714791; DOI=10.1016/0888-7543(89)90330-3;
Attree O., Vidaud D., Vidaud M., Amselem S., Lavergne J.-M.,
Goossens M.;
"Mutations in the catalytic domain of human coagulation factor IX:
rapid characterization by direct genomic sequencing of DNA fragments
displaying an altered melting behavior.";
Genomics 4:266-272(1989).
[57]
VARIANTS HEMB GLN-75; ASP-79; TRP-268; THR-279; SER-306; MET-342;
ARG-357 AND ARG-453, AND VARIANT PHE-7.
PubMed=2773937;
Koeberl D.D., Bottema C.D., Buerstedde J.-M., Sommer S.S.;
"Functionally important regions of the factor IX gene have a low rate
of polymorphism and a high rate of mutation in the dinucleotide CpG.";
Am. J. Hum. Genet. 45:448-457(1989).
[58]
VARIANT HEMB CYS-191.
PubMed=2775660; DOI=10.1111/j.1365-2141.1989.tb04323.x;
Liddell M.B., Peake I.R., Taylor S.A., Lillicrap D.P., Giddings J.C.,
Bloom A.L.;
"Factor IX Cardiff: a variant factor IX protein that shows abnormal
activation is caused by an arginine to cysteine substitution at
position 145.";
Br. J. Haematol. 72:556-560(1989).
[59]
VARIANT HEMB PHE-228.
PubMed=2753873;
Sakai T., Yoshioka A., Yamamoto K., Niinomi K., Fujimura Y., Fukui H.,
Miyata T., Iwanaga S.;
"Blood clotting factor IX Kashihara: amino acid substitution of
valine-182 by phenylalanine.";
J. Biochem. 105:756-759(1989).
[60]
VARIANT HEMB GLN-43.
PubMed=2738071;
Ware J., Diuguid D.L., Liebman H.A., Rabiet M.J., Kasper C.K.,
Furie B.C., Furie B., Stafford D.W.;
"Factor IX San Dimas. Substitution of glutamine for Arg-4 in the
propeptide leads to incomplete gamma-carboxylation and altered
phospholipid binding properties.";
J. Biol. Chem. 264:11401-11406(1989).
[61]
VARIANTS HEMB LYS-73; SER-106 AND GLN-294.
PubMed=2472424; DOI=10.1172/JCI114130;
Chen S.H., Thompson A.R., Zhang M., Scott C.R.;
"Three point mutations in the factor IX genes of five hemophilia B
patients. Identification strategy using localization by altered
epitopes in their hemophilic proteins.";
J. Clin. Invest. 84:113-118(1989).
[62]
VARIANT HEMB VAL-73.
PubMed=2339358;
Wang N.S., Zhang M., Thompson A.R., Chen S.H.;
"Factor IX Chongqing: a new mutation in the calcium-binding domain of
factor IX resulting in severe hemophilia B.";
Thromb. Haemost. 63:24-26(1990).
[63]
VARIANT HEMB LEU-228.
PubMed=2372509; DOI=10.1111/j.1365-2141.1990.tb02652.x;
Taylor S.A., Liddell M.B., Peake I.R., Bloom A.L., Lillicrap D.P.;
"A mutation adjacent to the beta cleavage site of factor IX (valine
182 to leucine) results in mild haemophilia Bm.";
Br. J. Haematol. 75:217-221(1990).
[64]
VARIANTS HEMB GLN-226; TRP-226; PHE-227 AND THR-414.
PubMed=2162822;
Bertina R.M., van der Linden I.K., Mannucci P.M., Reinalda-Poot H.H.,
Cupers R., Poort S.R., Reitsma P.H.;
"Mutations in hemophilia Bm occur at the Arg180-Val activation site or
in the catalytic domain of factor IX.";
J. Biol. Chem. 265:10876-10883(1990).
[65]
VARIANT HEMB GLU-357.
PubMed=1958666; DOI=10.1021/bi00111a014;
Miyata T., Sakai T., Sugimoto M., Naka H., Yamamoto K., Yoshioka A.,
Fukui H., Mitsui K., Kamiya K., Umeyama H., Iwanaga S.;
"Factor IX Amagasaki: a new mutation in the catalytic domain resulting
in the loss of both coagulant and esterase activities.";
Biochemistry 30:11286-11291(1991).
[66]
VARIANT HEMB THR-443.
PubMed=1902289; DOI=10.1093/nar/19.5.1165;
Sarkar G., Cassady J.D., Pyeritz R.E., Gilchrist G.S., Sommer S.S.;
"Isoleucine-397 is changed to threonine in two females with hemophilia
B.";
Nucleic Acids Res. 19:1165-1165(1991).
[67]
VARIANTS HEMB VAL-291; GLN-294; HIS-410; GLY-411 AND ILE-411.
PubMed=1346975;
Ludwig M., Sabharwal A.K., Brackmann H.H., Olek K., Smith K.J.,
Birktoft J.J., Bajaj S.P.;
"Hemophilia B caused by five different nondeletion mutations in the
protease domain of factor IX.";
Blood 79:1225-1232(1992).
[68]
VARIANT HEMB SER-252.
PubMed=1615485;
Taylor S.A., Duffin J., Cameron C., Teitel J., Garvey B.,
Lillicrap D.P.;
"Characterization of the original Christmas disease mutation (cysteine
206-->serine): from clinical recognition to molecular pathogenesis.";
Thromb. Haemost. 67:63-65(1992).
[69]
VARIANTS HEMB ARG-253; GLN-294; GLN-379; PRO-426 AND ILE-TYR-THR-445
INS.
PubMed=8257988; DOI=10.1002/humu.1380020506;
David D., Rosa H.A.V., Pemberton S., Diniz M.J., Campos M.,
Lavinha J.;
"Single-strand conformation polymorphism (SSCP) analysis of the
molecular pathology of hemophilia B.";
Hum. Mutat. 2:355-361(1993).
[70]
VARIANTS HEMB HIS-191; GLY-226; THR-279; GLN-379; GLU-419 AND GLN-449.
PubMed=8076946; DOI=10.1007/BF00208285;
Aguilar-Martinez P., Romey M.-C., Schved J.-F., Gris J.-C.,
Demaille J., Claustres M.;
"Factor IX gene mutations causing haemophilia B: comparison of SSC
screening versus systematic DNA sequencing and diagnostic
applications.";
Hum. Genet. 94:287-290(1994).
[71]
VARIANT HEMB GLU-419.
PubMed=8199596; DOI=10.1002/humu.1380030211;
Aguilar-Martinez P., Romey M.-C., Gris J.-C., Schved J.-F.,
Demaille J., Claustres M.;
"A novel mutation (Val-373 to Glu) in the catalytic domain of factor
IX, resulting in moderately/severe hemophilia B in a southern French
patient.";
Hum. Mutat. 3:156-158(1994).
[72]
VARIANTS HEMB GLN-294 AND ARG-413.
PubMed=7981722; DOI=10.1002/humu.1380040214;
Caglayan S.H., Vielhaber E., Guersel T., Aktuglu G., Sommer S.S.;
"Identification of mutations in four hemophilia B patients of Turkish
origin, including a novel deletion of base 6411.";
Hum. Mutat. 4:163-165(1994).
[73]
VARIANTS HEMB.
PubMed=8680410; DOI=10.1002/humu.1380060410;
Wulff K., Schroeder W., Wehnert M., Herrmann F.H.;
"Twenty-five novel mutations of the factor IX gene in haemophilia B.";
Hum. Mutat. 6:346-348(1995).
[74]
VARIANT WARFARIN SENSITIVITY THR-37.
PubMed=8833911; DOI=10.1172/JCI118956;
Chu K., Wu S.M., Stanley T., Stafford D.W., High K.A.;
"A mutation in the propeptide of factor IX leads to warfarin
sensitivity by a novel mechanism.";
J. Clin. Invest. 98:1619-1625(1996).
[75]
VARIANTS HEMB LYS-113; MET-342; ARG-413 AND VAL-424.
PubMed=9222764;
DOI=10.1002/(SICI)1098-1004(1997)10:1<76::AID-HUMU11>3.3.CO;2-0;
Caglayan S.H., Goekmen Y., Aktuglu G., Guergey A., Sommer S.S.;
"Mutations associated with hemophilia B in Turkish patients.";
Hum. Mutat. 10:76-79(1997).
[76]
VARIANT HEMB PRO-397.
PubMed=9590153;
DOI=10.1002/(SICI)1096-8652(199805)58:1<72::AID-AJH13>3.0.CO;2-7;
Chan V., Chan V.W.Y., Yip B., Chim C.S., Chan T.K.;
"Hemophilia B in a female carrier due to skewed inactivation of the
normal X-chromosome.";
Am. J. Hematol. 58:72-76(1998).
[77]
VARIANTS HEMB ARG-119 AND THR-454.
PubMed=9452115;
David D., Moreira I., Morais S., de Deus G.;
"Five novel factor IX mutations in unrelated hemophilia B patients.";
Hum. Mutat. Suppl. 1:S301-S303(1998).
[78]
VARIANTS HEMB GLN-43; TRP-43; THR-46; SER-106; CYS-115; PHE-155;
GLN-379; GLU-387; VAL-432 AND CYS-450.
PubMed=9600455;
DOI=10.1002/(SICI)1098-1004(1998)11:5<372::AID-HUMU4>3.0.CO;2-M;
Heit J.A., Thorland E.C., Ketterling R.P., Lind T.J., Daniels T.M.,
Zapata R.E., Ordonez S.M., Kasper C.K., Sommer S.S.;
"Germline mutations in Peruvian patients with hemophilia B: pattern of
mutation in Amerindians is similar to the putative endogenous germline
pattern.";
Hum. Mutat. 11:372-376(1998).
[79]
VARIANTS HEMB.
PubMed=10698280;
Wulff K., Bykowska K., Lopaciuk S., Herrmann F.H.;
"Molecular analysis of hemophilia B in Poland: 12 novel mutations of
the factor IX gene.";
Acta Biochim. Pol. 46:721-726(1999).
[80]
VARIANTS HEMB.
PubMed=10094553;
DOI=10.1002/(SICI)1098-1004(1999)13:2<160::AID-HUMU9>3.0.CO;2-C;
Montejo J.M., Magallon M., Tizzano E., Solera J.;
"Identification of twenty-one new mutations in the factor IX gene by
SSCP analysis.";
Hum. Mutat. 13:160-165(1999).
[81]
VARIANT ALA-194.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[82]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[83]
VARIANTS HEMB CYS-169 AND THR-333.
PubMed=11122099; DOI=10.1046/j.1365-2141.2000.02389.x;
Vidal F., Farssac E., Altisent C., Puig L., Gallardo D.;
"Factor IX gene sequencing by a simple and sensitive 15-hour procedure
for haemophilia B diagnosis: identification of two novel mutations.";
Br. J. Haematol. 111:549-551(2000).
[84]
VARIANTS HEMB TYR-28; LEU-43; GLN-43; SER-52; ASP-106; LYS-124;
TYR-134; GLN-226; GLY-226; TRP-226; LYS-241; TYR-252; GLN-294;
PHE-316; ARG-318; GLY-379; ILE-383; PHE-383; ILE-395; PHE-396; ARG-407
AND GLU-412.
PubMed=12588353; DOI=10.1046/j.1365-2141.2003.04141.x;
Onay U.V., Kavakli K., Kilinc Y., Gurgey A., Aktuglu G., Kemahli S.,
Ozbek U., Caglayan S.H.;
"Molecular pathology of haemophilia B in Turkish patients:
identification of a large deletion and 33 independent point
mutations.";
Br. J. Haematol. 120:656-659(2003).
[85]
VARIANTS HEMB TRP-43; ARG-84; ARG-125; VAL-125; PHE-170; ARG-302;
MET-342; LEU-344; LEU-395; THR-414; TYR-435; GLU-442 AND TRP-449.
PubMed=12604421;
Espinos C., Casana P., Haya S., Cid A.R., Aznar J.A.;
"Molecular analyses in hemophilia B families: identification of six
new mutations in the factor IX gene.";
Haematologica 88:235-236(2003).
[86]
VARIANT THPH8 LEU-384, CHARACTERIZATION OF VARIANT THPH8 LEU-384,
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19846852; DOI=10.1056/NEJMoa0904377;
Simioni P., Tormene D., Tognin G., Gavasso S., Bulato C.,
Iacobelli N.P., Finn J.D., Spiezia L., Radu C., Arruda V.R.;
"X-linked thrombophilia with a mutant factor IX (factor IX Padua).";
N. Engl. J. Med. 361:1671-1675(2009).
[87]
VARIANTS HEMB ALA-194 AND HIS-241.
PubMed=25470321; DOI=10.1111/hae.12553;
Saini S., Hamasaki-Katagiri N., Pandey G.S., Yanover C., Guelcher C.,
Simhadri V.L., Dandekar S., Guerrera M.F., Kimchi-Sarfaty C.,
Sauna Z.E.;
"Genetic determinants of immunogenicity to factor IX during the
treatment of haemophilia B.";
Haemophilia 21:210-218(2015).
[88]
VARIANTS HEMB SER-20; TYR-28; SER-46; ASP-54; GLU-58; ARG-84; HIS-138;
GLN-226; ILE-284 DEL; MET-296; LYS-328; TYR-328; THR-414 AND
TYR-THR-LYS-VAL-447 INS, AND CHARACTERIZATION OF VARIANTS HEMB SER-20;
TYR-28; SER-46; ASP-54; GLU-58; ARG-84; HIS-138; GLN-226; ILE-284 DEL;
MET-296; LYS-328; TYR-328; THR-414 AND TYR-THR-LYS-VAL-447 INS.
PubMed=25251685; DOI=10.1111/hae.12534;
Guo Z.P., Yang L.H., Qin X.Y., Liu X.E., Chen J.F., Zhang Y.F.;
"Comprehensive analysis of phenotypes and genetics in 21 Chinese
families with haemophilia B: characterization of five novel
mutations.";
Haemophilia 20:859-865(2014).
-!- FUNCTION: Factor IX is a vitamin K-dependent plasma protein that
participates in the intrinsic pathway of blood coagulation by
converting factor X to its active form in the presence of Ca(2+)
ions, phospholipids, and factor VIIIa.
{ECO:0000269|PubMed:1730085, ECO:0000269|PubMed:19846852,
ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198,
ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:8295821}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Ile bond in factor
X to form factor Xa. {ECO:0000269|PubMed:12444082,
ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198,
ECO:0000269|PubMed:2592373}.
-!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
disulfide-linked (PubMed:20121198, PubMed:20121197,
PubMed:20080729). Interacts with SERPINC1.
{ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198,
ECO:0000269|PubMed:2592373}.
-!- INTERACTION:
P00451:F8; NbExp=2; IntAct=EBI-9640450, EBI-11621603;
Q3U4G3:Xxylt1 (xeno); NbExp=3; IntAct=EBI-9640450, EBI-16178491;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19846852,
ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:3857619,
ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P00740-1; Sequence=Displayed;
Name=2;
IsoId=P00740-2; Sequence=VSP_047689;
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level)
(PubMed:3857619, PubMed:8295821, PubMed:2592373, PubMed:9169594,
PubMed:19846852). Synthesized primarily in the liver and secreted
in plasma. {ECO:0000269|PubMed:19846852,
ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:3857619}.
-!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla)
residues in the Gla domain. Calcium can also bind, with stronger
affinity, to another site beyond the Gla domain (PubMed:6425296).
Under physiological ion concentrations, Ca(2+) is displaced by
Mg(2+) from some of the gammaglutamate residues in the N-terminal
Gla domain. This leads to a subtle conformation change that may
affect the interaction with its binding protein (By similarity).
{ECO:0000250|UniProtKB:P00741, ECO:0000269|PubMed:14722079,
ECO:0000269|PubMed:1730085, ECO:0000269|PubMed:6425296}.
-!- PTM: Activated by factor XIa, which excises the activation peptide
(PubMed:9169594, PubMed:1730085). The propeptide can also be
removed by snake venom protease (PubMed:20004170,
PubMed:20080729). {ECO:0000269|PubMed:1730085,
ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:8295821,
ECO:0000269|PubMed:9169594}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000269|PubMed:6688526}.
-!- PTM: Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro.
Xylosylation at this site is minor.
-!- DISEASE: Hemophilia B (HEMB) [MIM:306900]: An X-linked blood
coagulation disorder characterized by a permanent tendency to
hemorrhage, due to factor IX deficiency. It is phenotypically
similar to hemophilia A, but patients present with fewer symptoms.
Many patients are asymptomatic until the hemostatic system is
stressed by surgery or trauma. {ECO:0000269|PubMed:10094553,
ECO:0000269|PubMed:10698280, ECO:0000269|PubMed:11122099,
ECO:0000269|PubMed:12588353, ECO:0000269|PubMed:12604421,
ECO:0000269|PubMed:1346975, ECO:0000269|PubMed:1615485,
ECO:0000269|PubMed:1902289, ECO:0000269|PubMed:1958666,
ECO:0000269|PubMed:2162822, ECO:0000269|PubMed:2339358,
ECO:0000269|PubMed:2372509, ECO:0000269|PubMed:2472424,
ECO:0000269|PubMed:25251685, ECO:0000269|PubMed:25470321,
ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:2713493,
ECO:0000269|PubMed:2714791, ECO:0000269|PubMed:2738071,
ECO:0000269|PubMed:2753873, ECO:0000269|PubMed:2773937,
ECO:0000269|PubMed:2775660, ECO:0000269|PubMed:3009023,
ECO:0000269|PubMed:3243764, ECO:0000269|PubMed:3401602,
ECO:0000269|PubMed:3790720, ECO:0000269|PubMed:6603618,
ECO:0000269|PubMed:7981722, ECO:0000269|PubMed:8076946,
ECO:0000269|PubMed:8199596, ECO:0000269|PubMed:8257988,
ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:8680410,
ECO:0000269|PubMed:9169594, ECO:0000269|PubMed:9222764,
ECO:0000269|PubMed:9452115, ECO:0000269|PubMed:9590153,
ECO:0000269|PubMed:9600455}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Mutations in position 43 (Oxford-3, San Dimas) and
46 (Cambridge) prevents cleavage of the propeptide
(PubMed:12588353, PubMed:2738071, PubMed:3009023, PubMed:8295821,
PubMed:9169594, PubMed:9600455, PubMed:25251685). Mutation in
position 93 (Alabama) probably fails to bind to cell membranes
(PubMed:3790720). Mutation in position 191 (Chapel-Hill) or in
position 226 (Nagoya or Hilo) prevent cleavage of the activation
peptide (PubMed:6603618, PubMed:8076946, PubMed:12588353,
PubMed:2162822, PubMed:25251685, PubMed:2713493).
{ECO:0000269|PubMed:12588353, ECO:0000269|PubMed:2162822,
ECO:0000269|PubMed:25251685, ECO:0000269|PubMed:2713493,
ECO:0000269|PubMed:2738071, ECO:0000269|PubMed:3009023,
ECO:0000269|PubMed:3790720, ECO:0000269|PubMed:6603618,
ECO:0000269|PubMed:8076946, ECO:0000269|PubMed:8295821,
ECO:0000269|PubMed:9169594, ECO:0000269|PubMed:9600455}.
-!- DISEASE: Thrombophilia, X-linked, due to factor IX defect (THPH8)
[MIM:300807]: A hemostatic disorder characterized by a tendency to
thrombosis. {ECO:0000269|PubMed:19846852}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- PHARMACEUTICAL: Available under the name BeneFix (Baxter and
American Home Products). Used to treat hemophilia B.
-!- MISCELLANEOUS: In 1952, one of the earliest researchers of the
disease, Dr. R.G. Macfarlane used the patient's surname,
Christmas, to refer to the disease and also to refer to the
clotting factor which he called the 'Christmas Factor' At the time
Stephen Christmas was a 5-year-old boy. He died in 1993 at the age
of 46 from acquired immunodeficiency syndrome contracted through
treatment with blood products.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Factor IX entry;
URL="https://en.wikipedia.org/wiki/Factor_IX";
-!- WEB RESOURCE: Name=Factor IX Mutation Database;
URL="http://www.factorix.org/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f9/";
-!- WEB RESOURCE: Name=BeneFix; Note=Clinical information on BeneFix;
URL="http://www.pfizer.com/products/product-detail/benefix";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The Christmas Factor
- Issue 41 of December 2003;
URL="http://web.expasy.org/spotlight/back_issues/041";
-----------------------------------------------------------------------
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EMBL; J00136; AAA98726.1; -; mRNA.
EMBL; J00137; AAA52763.1; -; mRNA.
EMBL; K02053; AAA56822.1; -; Genomic_DNA.
EMBL; K02048; AAA56822.1; JOINED; Genomic_DNA.
EMBL; K02049; AAA56822.1; JOINED; Genomic_DNA.
EMBL; K02051; AAA56822.1; JOINED; Genomic_DNA.
EMBL; K02052; AAA56822.1; JOINED; Genomic_DNA.
EMBL; K02402; AAB59620.1; -; Genomic_DNA.
EMBL; M11309; AAA52023.1; -; mRNA.
EMBL; AL033403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB186358; BAD89383.1; -; mRNA.
EMBL; AF536327; AAM96188.1; -; Genomic_DNA.
EMBL; FR846239; CCA61111.1; -; mRNA.
EMBL; AK292749; BAF85438.1; -; mRNA.
EMBL; CH471150; EAW88433.1; -; Genomic_DNA.
EMBL; BC109214; AAI09215.1; -; mRNA.
EMBL; BC109215; AAI09216.1; -; mRNA.
EMBL; S68634; AAB29758.1; -; Genomic_DNA.
EMBL; M35672; AAA51981.1; -; mRNA.
EMBL; M19063; AAA52456.1; -; Genomic_DNA.
EMBL; S66752; AAB28588.1; -; Genomic_DNA.
CCDS; CCDS14666.1; -. [P00740-1]
CCDS; CCDS83495.1; -. [P00740-2]
PIR; A00922; KFHU.
RefSeq; NP_000124.1; NM_000133.3. [P00740-1]
RefSeq; NP_001300842.1; NM_001313913.1. [P00740-2]
UniGene; Hs.522798; -.
PDB; 1CFH; NMR; -; A=47-93.
PDB; 1CFI; NMR; -; A=47-93.
PDB; 1EDM; X-ray; 1.50 A; B/C=92-130.
PDB; 1IXA; NMR; -; A=92-130.
PDB; 1MGX; NMR; -; A=47-93.
PDB; 1NL0; X-ray; 2.20 A; G=47-91.
PDB; 1RFN; X-ray; 2.80 A; A=227-461, B=133-188.
PDB; 2WPH; X-ray; 1.50 A; E=133-191, S=227-461.
PDB; 2WPI; X-ray; 1.99 A; E=133-191, S=227-461.
PDB; 2WPJ; X-ray; 1.60 A; E=133-191, S=227-461.
PDB; 2WPK; X-ray; 2.21 A; E=133-191, S=227-461.
PDB; 2WPL; X-ray; 1.82 A; E=133-191, S=227-461.
PDB; 2WPM; X-ray; 2.00 A; E=133-191, S=227-461.
PDB; 3KCG; X-ray; 1.70 A; H=227-461, L=131-188.
PDB; 3LC3; X-ray; 1.90 A; A/C=227-461, B/D=133-188.
PDB; 3LC5; X-ray; 2.62 A; A=227-461, B=133-188.
PDB; 4WM0; X-ray; 2.37 A; D=92-130.
PDB; 4WMA; X-ray; 1.62 A; D=92-130.
PDB; 4WMB; X-ray; 2.05 A; D=92-130.
PDB; 4WMI; X-ray; 1.87 A; D=92-130.
PDB; 4WMK; X-ray; 2.08 A; D=92-130.
PDB; 4WN2; X-ray; 1.95 A; D=92-130.
PDB; 4WNH; X-ray; 1.95 A; D=92-130.
PDB; 4YZU; X-ray; 1.41 A; A=227-461, B=131-191.
PDB; 4Z0K; X-ray; 1.41 A; A=227-461, B=131-191.
PDB; 4ZAE; X-ray; 1.86 A; A=227-461, B=131-191.
PDB; 5EGM; X-ray; 1.84 A; A=227-461, B=131-191.
PDB; 5F84; X-ray; 2.50 A; B=92-130.
PDB; 5F85; X-ray; 2.15 A; B=92-130.
PDB; 5F86; X-ray; 1.90 A; B=92-130.
PDB; 5JB8; X-ray; 1.45 A; E=134-191, S=227-461.
PDB; 5JB9; X-ray; 1.30 A; E=134-191, S=227-461.
PDB; 5JBA; X-ray; 1.40 A; E=134-191, S=227-461.
PDB; 5JBB; X-ray; 1.56 A; E=134-191, S=227-461.
PDB; 5JBC; X-ray; 1.90 A; E=134-191, S=227-461.
PDB; 5TNO; X-ray; 1.54 A; A=227-461, B=130-191.
PDB; 5TNT; X-ray; 1.40 A; A=227-461, B=130-191.
PDB; 5VYG; X-ray; 2.20 A; A/B/C=92-130.
PDBsum; 1CFH; -.
PDBsum; 1CFI; -.
PDBsum; 1EDM; -.
PDBsum; 1IXA; -.
PDBsum; 1MGX; -.
PDBsum; 1NL0; -.
PDBsum; 1RFN; -.
PDBsum; 2WPH; -.
PDBsum; 2WPI; -.
PDBsum; 2WPJ; -.
PDBsum; 2WPK; -.
PDBsum; 2WPL; -.
PDBsum; 2WPM; -.
PDBsum; 3KCG; -.
PDBsum; 3LC3; -.
PDBsum; 3LC5; -.
PDBsum; 4WM0; -.
PDBsum; 4WMA; -.
PDBsum; 4WMB; -.
PDBsum; 4WMI; -.
PDBsum; 4WMK; -.
PDBsum; 4WN2; -.
PDBsum; 4WNH; -.
PDBsum; 4YZU; -.
PDBsum; 4Z0K; -.
PDBsum; 4ZAE; -.
PDBsum; 5EGM; -.
PDBsum; 5F84; -.
PDBsum; 5F85; -.
PDBsum; 5F86; -.
PDBsum; 5JB8; -.
PDBsum; 5JB9; -.
PDBsum; 5JBA; -.
PDBsum; 5JBB; -.
PDBsum; 5JBC; -.
PDBsum; 5TNO; -.
PDBsum; 5TNT; -.
PDBsum; 5VYG; -.
ProteinModelPortal; P00740; -.
SMR; P00740; -.
BioGrid; 108456; 39.
DIP; DIP-58520N; -.
ELM; P00740; -.
IntAct; P00740; 4.
STRING; 9606.ENSP00000218099; -.
BindingDB; P00740; -.
ChEMBL; CHEMBL2016; -.
DrugBank; DB00025; Antihemophilic Factor (Recombinant).
DrugBank; DB13150; Coagulation factor VII human.
DrugBank; DB00170; Menadione.
DrugBank; DB05131; TTP889.
GuidetoPHARMACOLOGY; 2364; -.
Allergome; 9616; Hom s Factor IX.
MEROPS; S01.214; -.
iPTMnet; P00740; -.
PhosphoSitePlus; P00740; -.
UniCarbKB; P00740; -.
BioMuta; F9; -.
PaxDb; P00740; -.
PeptideAtlas; P00740; -.
PRIDE; P00740; -.
DNASU; 2158; -.
Ensembl; ENST00000218099; ENSP00000218099; ENSG00000101981. [P00740-1]
Ensembl; ENST00000394090; ENSP00000377650; ENSG00000101981. [P00740-2]
GeneID; 2158; -.
KEGG; hsa:2158; -.
UCSC; uc004fas.2; human. [P00740-1]
CTD; 2158; -.
DisGeNET; 2158; -.
EuPathDB; HostDB:ENSG00000101981.10; -.
GeneCards; F9; -.
GeneReviews; F9; -.
HGNC; HGNC:3551; F9.
MalaCards; F9; -.
MIM; 300746; gene.
MIM; 300807; phenotype.
MIM; 306900; phenotype.
neXtProt; NX_P00740; -.
OpenTargets; ENSG00000101981; -.
Orphanet; 169799; Mild hemophilia B.
Orphanet; 169796; Moderately severe hemophilia B.
Orphanet; 169793; Severe hemophilia B.
Orphanet; 177929; Symptomatic form of hemophilia B in female carriers.
PharmGKB; PA27954; -.
eggNOG; ENOG410IGPV; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118890; -.
HOGENOM; HOG000251821; -.
HOVERGEN; HBG013304; -.
InParanoid; P00740; -.
KO; K01321; -.
OMA; VTPICIA; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P00740; -.
TreeFam; TF327329; -.
BRENDA; 3.4.21.22; 2681.
Reactome; R-HSA-140834; Extrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors.
Reactome; R-HSA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RK; P00740; -.
SIGNOR; P00740; -.
EvolutionaryTrace; P00740; -.
GeneWiki; Factor_IX; -.
GenomeRNAi; 2158; -.
PMAP-CutDB; P00740; -.
PRO; PR:P00740; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000101981; -.
CleanEx; HS_F9; -.
Genevisible; P00740; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; NAS:BHF-UCL.
GO; GO:0007596; P:blood coagulation; IDA:UniProtKB.
GO; GO:0007598; P:blood coagulation, extrinsic pathway; TAS:Reactome.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0006465; P:signal peptide processing; TAS:Reactome.
GO; GO:0031638; P:zymogen activation; IDA:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
InterPro; IPR035694; Coagulation_factor_IX.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR012224; Pept_S1A_FX.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR44064:SF4; PTHR44064:SF4; 1.
Pfam; PF00008; EGF; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001143; Factor_X; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00069; GLA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemophilia;
Hemostasis; Hydrolase; Hydroxylation; Magnesium; Metal-binding;
Pharmaceutical; Phosphoprotein; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal;
Sulfation; Thrombophilia; Zymogen.
SIGNAL 1 28 {ECO:0000255}.
PROPEP 29 46 {ECO:0000269|PubMed:2592373}.
/FTId=PRO_0000027755.
CHAIN 47 461 Coagulation factor IX.
/FTId=PRO_0000027756.
CHAIN 47 191 Coagulation factor IXa light chain.
/FTId=PRO_0000027757.
PROPEP 192 226 Activation peptide.
/FTId=PRO_0000027758.
CHAIN 227 461 Coagulation factor IXa heavy chain.
/FTId=PRO_0000027759.
DOMAIN 47 92 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 93 129 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 130 171 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 227 459 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 267 267 Charge relay system.
{ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:659613}.
ACT_SITE 315 315 Charge relay system.
{ECO:0000269|PubMed:659613}.
ACT_SITE 411 411 Charge relay system.
{ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:659613}.
METAL 47 47 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:1NL0,
ECO:0000269|PubMed:14722079}.
METAL 48 48 Calcium 2. {ECO:0000244|PDB:1NL0,
ECO:0000269|PubMed:14722079}.
METAL 53 53 Calcium 1; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 53 53 Calcium 2; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 54 54 Calcium 2; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 54 54 Calcium 3; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 61 61 Calcium 4 or magnesium 1; via 4-
carboxyglutamate. {ECO:0000244|PDB:1NL0,
ECO:0000250|UniProtKB:P00741,
ECO:0000305|PubMed:14722079}.
METAL 63 63 Calcium 1; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 63 63 Calcium 2; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 63 63 Calcium 3; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 66 66 Calcium 4 or magnesium 1; via 4-
carboxyglutamate. {ECO:0000244|PDB:1NL0,
ECO:0000250|UniProtKB:P00741,
ECO:0000305|PubMed:14722079}.
METAL 67 67 Calcium 1; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 72 72 Calcium 5 or magnesium 2; via 4-
carboxyglutamate. {ECO:0000244|PDB:1NL0,
ECO:0000250|UniProtKB:P00741,
ECO:0000305|PubMed:14722079}.
METAL 73 73 Calcium 2; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 73 73 Calcium 3; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 76 76 Calcium 3; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 76 76 Calcium 5 or magnesium 2; via 4-
carboxyglutamate. {ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 76 76 Calcium 5; via 4-carboxyglutamate.
{ECO:0000244|PDB:1NL0,
ECO:0000305|PubMed:14722079}.
METAL 82 82 Calcium 6 or magnesium 3; via 4-
carboxyglutamate.
{ECO:0000250|UniProtKB:P00741}.
METAL 86 86 Calcium 6 or magnesium 3; via 4-
carboxyglutamate.
{ECO:0000250|UniProtKB:P00741}.
METAL 93 93 Calcium 7. {ECO:0000244|PDB:1EDM,
ECO:0000269|PubMed:7606779}.
METAL 94 94 Calcium 7; via carbonyl oxygen.
{ECO:0000244|PDB:1EDM,
ECO:0000269|PubMed:7606779}.
METAL 96 96 Calcium 7. {ECO:0000244|PDB:1EDM,
ECO:0000269|PubMed:7606779}.
METAL 110 110 Calcium 7. {ECO:0000244|PDB:1EDM,
ECO:0000269|PubMed:7606779}.
METAL 111 111 Calcium 7; via carbonyl oxygen.
{ECO:0000244|PDB:1EDM,
ECO:0000269|PubMed:7606779}.
METAL 281 281 Calcium 8. {ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:10467148,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
METAL 283 283 Calcium 8; via carbonyl oxygen.
{ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:10467148,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
METAL 286 286 Calcium 8; via carbonyl oxygen.
{ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:10467148,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
METAL 288 288 Calcium 8. {ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:10467148,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
METAL 291 291 Calcium 8. {ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:10467148,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
SITE 191 192 Cleavage; by factor XIa.
SITE 226 227 Cleavage; by factor XIa.
MOD_RES 53 53 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 54 54 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 61 61 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 63 63 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 66 66 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 67 67 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 72 72 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 73 73 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 76 76 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 79 79 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 82 82 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 86 86 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00741,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 110 110 (3R)-3-hydroxyaspartate.
{ECO:0000269|PubMed:6688526}.
MOD_RES 114 114 Phosphoserine. {ECO:0000269|Ref.28}.
MOD_RES 201 201 Sulfotyrosine.
{ECO:0000269|PubMed:11133752}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000269|PubMed:11133752,
ECO:0000269|PubMed:25456591}.
MOD_RES 205 205 Phosphothreonine; alternate.
{ECO:0000269|PubMed:25456591}.
CARBOHYD 85 85 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591}.
CARBOHYD 99 99 O-linked (Glc...) serine; alternate.
{ECO:0000269|PubMed:21949356,
ECO:0000269|PubMed:25456591}.
/FTId=CAR_000009.
CARBOHYD 99 99 O-linked (Xyl...) serine; alternate.
{ECO:0000269|PubMed:21949356}.
CARBOHYD 107 107 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:25456591}.
/FTId=CAR_000010.
CARBOHYD 203 203 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 205 205 O-linked (GalNAc...) threonine;
alternate. {ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:8172892}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 215 215 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591,
ECO:0000269|PubMed:8172892}.
CARBOHYD 225 225 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:25456591}.
DISULFID 64 69 {ECO:0000250|UniProtKB:P00741}.
DISULFID 97 108 {ECO:0000244|PDB:1EDM,
ECO:0000244|PDB:1IXA,
ECO:0000269|PubMed:1304885,
ECO:0000269|PubMed:7606779}.
DISULFID 102 117 {ECO:0000244|PDB:1EDM,
ECO:0000244|PDB:1IXA,
ECO:0000269|PubMed:1304885,
ECO:0000269|PubMed:7606779}.
DISULFID 119 128 {ECO:0000244|PDB:1EDM,
ECO:0000244|PDB:1IXA,
ECO:0000269|PubMed:1304885,
ECO:0000269|PubMed:7606779}.
DISULFID 134 145 {ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPL,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
DISULFID 141 155 {ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPL,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
DISULFID 157 170 {ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPL,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
DISULFID 178 335 Interchain (between light and heavy
chains). {ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPL,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
DISULFID 252 268 {ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPL,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
DISULFID 382 396 {ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPL,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
DISULFID 407 435 {ECO:0000244|PDB:1RFN,
ECO:0000244|PDB:2WPH,
ECO:0000244|PDB:2WPI,
ECO:0000244|PDB:2WPJ,
ECO:0000244|PDB:2WPK,
ECO:0000244|PDB:2WPL,
ECO:0000244|PDB:2WPM,
ECO:0000244|PDB:3KCG,
ECO:0000244|PDB:3LC3,
ECO:0000244|PDB:3LC5,
ECO:0000269|PubMed:20004170,
ECO:0000269|PubMed:20080729,
ECO:0000269|PubMed:20121197,
ECO:0000269|PubMed:20121198}.
VAR_SEQ 93 130 Missing (in isoform 2).
{ECO:0000303|Ref.6}.
/FTId=VSP_047689.
VARIANT 7 7 I -> F (in dbSNP:rs150190385).
{ECO:0000269|PubMed:2773937}.
/FTId=VAR_006520.
VARIANT 17 17 I -> N (in HEMB; severe; UK 22).
/FTId=VAR_006521.
VARIANT 20 20 L -> S (in HEMB; unknown pathological
significance; decreased protein
abundance; decreased function in blood
coagulation).
{ECO:0000269|PubMed:25251685}.
/FTId=VAR_073975.
VARIANT 28 28 C -> R (in HEMB; moderate; HB130;
dbSNP:rs387906481).
/FTId=VAR_006522.
VARIANT 28 28 C -> Y (in HEMB; decreased protein
abundance; decreased function in blood
coagulation).
{ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:25251685}.
/FTId=VAR_017343.
VARIANT 30 30 V -> I (in HEMB).
/FTId=VAR_006523.
VARIANT 37 37 A -> T (in warfarin sensitivity; reduced
affinity of the glutamate carboxylase for
the factor IX precursor;
dbSNP:rs367569299).
{ECO:0000269|PubMed:8833911}.
/FTId=VAR_017307.
VARIANT 43 43 R -> L (in HEMB; severe; Bendorf, Beuten,
Gleiwitz; impairs removal of propeptide).
{ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:9169594}.
/FTId=VAR_006525.
VARIANT 43 43 R -> Q (in HEMB; severe; San Dimas,
Oxford-3, Strasbourg-2; impairs removal
of propeptide).
{ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:2738071,
ECO:0000269|PubMed:3009023,
ECO:0000269|PubMed:8295821,
ECO:0000269|PubMed:9169594,
ECO:0000269|PubMed:9600455}.
/FTId=VAR_006524.
VARIANT 43 43 R -> W (in HEMB; severe; Boxtel, Heiden,
Lienen; impairs removal of propeptide).
{ECO:0000269|PubMed:12604421,
ECO:0000269|PubMed:9169594,
ECO:0000269|PubMed:9600455}.
/FTId=VAR_006526.
VARIANT 45 45 K -> N (in HEMB; severe; Seattle E).
/FTId=VAR_006527.
VARIANT 46 46 R -> S (in HEMB; severe; Cambridge;
impaired processing of the propeptide;
impaired gamma-carboxylation; decreased
protein abundance; loss of function in
blood coagulation).
{ECO:0000269|PubMed:25251685}.
/FTId=VAR_006528.
VARIANT 46 46 R -> T (in HEMB; severe).
{ECO:0000269|PubMed:9600455}.
/FTId=VAR_006529.
VARIANT 48 48 N -> I (in HEMB; severe; Calgary-16).
/FTId=VAR_006530.
VARIANT 49 49 S -> P (in HEMB).
/FTId=VAR_006531.
VARIANT 52 52 L -> S (in HEMB; severe; Gla mutant).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017344.
VARIANT 53 53 E -> A (in HEMB; severe; Oxford-B2; Gla
mutant).
/FTId=VAR_006532.
VARIANT 54 54 E -> D (in HEMB; unknown pathological
significance; no effect on protein
abundance; loss of function in blood
coagulation).
{ECO:0000269|PubMed:25251685}.
/FTId=VAR_073976.
VARIANT 54 54 E -> G (in HEMB; severe; HB151; Gla
mutant).
/FTId=VAR_006533.
VARIANT 55 55 F -> C (in HEMB).
/FTId=VAR_006534.
VARIANT 58 58 G -> A (in HEMB; severe; Hong Kong-1).
/FTId=VAR_006535.
VARIANT 58 58 G -> E (in HEMB; unknown pathological
significance; no effect on protein
abundance; loss of function in blood
coagulation).
{ECO:0000269|PubMed:25251685}.
/FTId=VAR_073977.
VARIANT 58 58 G -> R (in HEMB; severe; Los Angeles-4).
/FTId=VAR_006536.
VARIANT 62 63 Missing (in HEMB; severe).
/FTId=VAR_006537.
VARIANT 66 66 E -> V (in HEMB; moderate).
/FTId=VAR_006538.
VARIANT 67 67 E -> K (in HEMB; severe; Nagoya-4; Gla
mutant).
/FTId=VAR_006539.
VARIANT 71 71 F -> S (in HEMB; severe).
/FTId=VAR_006540.
VARIANT 73 73 E -> K (in HEMB; severe; Seattle-3; Gla
mutant; dbSNP:rs137852225).
{ECO:0000269|PubMed:2472424}.
/FTId=VAR_006541.
VARIANT 73 73 E -> V (in HEMB; severe; Chongqing; Gla
mutant; dbSNP:rs137852226).
{ECO:0000269|PubMed:2339358}.
/FTId=VAR_006542.
VARIANT 75 75 R -> Q (in HEMB; mild;
dbSNP:rs137852228).
{ECO:0000269|PubMed:2773937}.
/FTId=VAR_017308.
VARIANT 79 79 E -> D (in HEMB; dbSNP:rs137852229).
{ECO:0000269|PubMed:2773937}.
/FTId=VAR_017309.
VARIANT 84 84 T -> R (in HEMB; decreased protein
abundance; loss of function in blood
coagulation).
{ECO:0000269|PubMed:12604421,
ECO:0000269|PubMed:25251685}.
/FTId=VAR_017345.
VARIANT 91 91 Y -> C (in HEMB; moderate).
/FTId=VAR_006543.
VARIANT 93 93 D -> G (in HEMB; moderate; Alabama;
dbSNP:rs137852230).
{ECO:0000269|PubMed:3790720}.
/FTId=VAR_006544.
VARIANT 96 96 Q -> P (in HEMB; severe; New London;
dbSNP:rs137852231).
/FTId=VAR_006545.
VARIANT 97 97 C -> S (in HEMB).
/FTId=VAR_006546.
VARIANT 101 101 P -> R (in HEMB).
/FTId=VAR_006547.
VARIANT 102 102 C -> R (in HEMB; severe; Basel).
/FTId=VAR_006548.
VARIANT 106 106 G -> D (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017346.
VARIANT 106 106 G -> S (in HEMB; mild; Durham;
dbSNP:rs137852233).
{ECO:0000269|PubMed:2472424,
ECO:0000269|PubMed:9600455}.
/FTId=VAR_006549.
VARIANT 108 108 C -> S (in HEMB).
/FTId=VAR_006550.
VARIANT 110 110 D -> N (in HEMB; severe; Oxford-D1;
dbSNP:rs137852274).
/FTId=VAR_006551.
VARIANT 112 112 I -> S (in HEMB).
/FTId=VAR_006552.
VARIANT 113 113 N -> K (in HEMB; mild).
{ECO:0000269|PubMed:9222764}.
/FTId=VAR_006553.
VARIANT 115 115 Y -> C (in HEMB; severe).
{ECO:0000269|PubMed:9600455}.
/FTId=VAR_006554.
VARIANT 119 119 C -> F (in HEMB; severe).
/FTId=VAR_006555.
VARIANT 119 119 C -> R (in HEMB; Iran).
{ECO:0000269|PubMed:9452115}.
/FTId=VAR_006556.
VARIANT 124 124 E -> K (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017347.
VARIANT 125 125 G -> E (in HEMB).
/FTId=VAR_006557.
VARIANT 125 125 G -> R (in HEMB).
{ECO:0000269|PubMed:12604421}.
/FTId=VAR_017348.
VARIANT 125 125 G -> V (in HEMB).
{ECO:0000269|PubMed:12604421}.
/FTId=VAR_006558.
VARIANT 129 130 Missing (in HEMB).
/FTId=VAR_006559.
VARIANT 134 134 C -> Y (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017349.
VARIANT 136 136 I -> T (in HEMB; mild).
/FTId=VAR_006560.
VARIANT 138 138 N -> H (in HEMB; unknown pathological
significance; decreased protein
abundance; decreased function in blood
coagulation).
{ECO:0000269|PubMed:25251685}.
/FTId=VAR_073978.
VARIANT 139 139 G -> D (in HEMB; severe).
/FTId=VAR_006561.
VARIANT 139 139 G -> S (in HEMB).
/FTId=VAR_006562.
VARIANT 155 155 C -> F (in HEMB; severe).
{ECO:0000269|PubMed:9600455}.
/FTId=VAR_006563.
VARIANT 160 160 G -> E (in HEMB; mild).
/FTId=VAR_006564.
VARIANT 167 167 Q -> H (in HEMB; mild).
/FTId=VAR_006565.
VARIANT 169 169 S -> C (in HEMB).
{ECO:0000269|PubMed:11122099}.
/FTId=VAR_017350.
VARIANT 170 170 C -> F (in HEMB).
{ECO:0000269|PubMed:12604421}.
/FTId=VAR_017351.
VARIANT 178 178 C -> R (in HEMB).
/FTId=VAR_006566.
VARIANT 178 178 C -> W (in HEMB; severe).
/FTId=VAR_006567.
VARIANT 191 191 R -> C (in HEMB; moderate; Albuquerque,
Cardiff-1; dbSNP:rs137852237).
{ECO:0000269|PubMed:2775660}.
/FTId=VAR_006569.
VARIANT 191 191 R -> H (in HEMB; moderate; Chapel-Hill,
Chicago-2; dbSNP:rs137852238).
{ECO:0000269|PubMed:6603618,
ECO:0000269|PubMed:8076946}.
/FTId=VAR_006568.
VARIANT 194 194 T -> A (in dbSNP:rs6048).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:25470321,
ECO:0000269|PubMed:2994716,
ECO:0000269|PubMed:3857619,
ECO:0000269|PubMed:6329734}.
/FTId=VAR_011773.
VARIANT 226 226 R -> G (in HEMB; severe; Madrid).
{ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:8076946}.
/FTId=VAR_006571.
VARIANT 226 226 R -> Q (in HEMB; severe; Hilo and Novara;
no effect on protein abundance; loss of
function in blood coagulation;
dbSNP:rs137852241).
{ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:2162822,
ECO:0000269|PubMed:25251685,
ECO:0000269|PubMed:2713493}.
/FTId=VAR_006572.
VARIANT 226 226 R -> W (in HEMB; severe; Nagoya-1,
Dernbach, Deventer, Idaho;
dbSNP:rs137852240).
{ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:2162822,
ECO:0000269|PubMed:2592373}.
/FTId=VAR_006570.
VARIANT 227 227 V -> D (in HEMB; mild).
/FTId=VAR_006573.
VARIANT 227 227 V -> F (in HEMB; Milano;
dbSNP:rs137852242).
{ECO:0000269|PubMed:2162822}.
/FTId=VAR_017310.
VARIANT 228 228 V -> F (in HEMB; severe; Kashihara;
dbSNP:rs137852243).
{ECO:0000269|PubMed:2753873}.
/FTId=VAR_017311.
VARIANT 228 228 V -> L (in HEMB; mild; Cardiff-2;
dbSNP:rs137852243).
{ECO:0000269|PubMed:2372509}.
/FTId=VAR_006574.
VARIANT 241 241 Q -> H (in HEMB).
{ECO:0000269|PubMed:25470321}.
/FTId=VAR_006575.
VARIANT 241 241 Q -> K (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017352.
VARIANT 252 252 C -> S (in HEMB; severe;
dbSNP:rs267606792).
{ECO:0000269|PubMed:1615485}.
/FTId=VAR_017312.
VARIANT 252 252 C -> Y (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017353.
VARIANT 253 253 G -> E (in HEMB; severe).
/FTId=VAR_006576.
VARIANT 253 253 G -> R (in HEMB; severe; Luanda).
{ECO:0000269|PubMed:8257988}.
/FTId=VAR_006577.
VARIANT 265 265 A -> T (in HEMB; mild).
/FTId=VAR_006578.
VARIANT 268 268 C -> W (in HEMB; moderate;
dbSNP:rs137852246).
{ECO:0000269|PubMed:2773937}.
/FTId=VAR_017313.
VARIANT 279 279 A -> T (in HEMB; mild;
dbSNP:rs137852247).
{ECO:0000269|PubMed:2773937,
ECO:0000269|PubMed:8076946}.
/FTId=VAR_006579.
VARIANT 283 283 N -> D (in HEMB; severe).
/FTId=VAR_006580.
VARIANT 284 284 Missing (in HEMB; severe; decreased
protein abundance; loss of function in
blood coagulation).
{ECO:0000269|PubMed:25251685}.
/FTId=VAR_073979.
VARIANT 286 286 Missing (in HEMB; severe).
/FTId=VAR_006581.
VARIANT 291 291 E -> V (in HEMB; Monschau;
dbSNP:rs137852279).
{ECO:0000269|PubMed:1346975}.
/FTId=VAR_017314.
VARIANT 294 294 R -> G (in HEMB; severe).
/FTId=VAR_006582.
VARIANT 294 294 R -> Q (in HEMB; mild to moderate;
Dreihacken, Penafiel and Seattle-4;
dbSNP:rs137852249).
{ECO:0000269|PubMed:12588353,
ECO:0000269|PubMed:1346975,
ECO:0000269|PubMed:2472424,
ECO:0000269|PubMed:7981722,
ECO:0000269|PubMed:8257988}.
/FTId=VAR_006583.
VARIANT 296 296 V -> M (in HEMB; unknown pathological
significance; decreased protein
abundance; decreased function in blood
coagulation).
{ECO:0000269|PubMed:25251685}.
/FTId=VAR_073980.
VARIANT 302 302 H -> R (in HEMB).
{ECO:0000269|PubMed:12604421}.
/FTId=VAR_006584.
VARIANT 306 306 N -> S (in HEMB; mild;
dbSNP:rs137852251).
{ECO:0000269|PubMed:2773937}.
/FTId=VAR_017315.
VARIANT 316 316 I -> F (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_006585.
VARIANT 318 318 L -> R (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017354.
VARIANT 321 321 L -> Q (in HEMB; severe).
/FTId=VAR_006586.
VARIANT 328 328 N -> K (in HEMB; unknown pathological
significance; decreased protein
abundance; decreased function in blood
coagulation).
{ECO:0000269|PubMed:25251685}.
/FTId=VAR_073981.
VARIANT 328 328 N -> Y (in HEMB; moderate; decreased
protein abundance; decreased function in
blood coagulation).
{ECO:0000269|PubMed:25251685}.
/FTId=VAR_073982.
VARIANT 333 333 P -> H (in HEMB; severe).
/FTId=VAR_006587.
VARIANT 333 333 P -> T (in HEMB).
{ECO:0000269|PubMed:11122099}.
/FTId=VAR_017355.
VARIANT 342 342 T -> K (in HEMB; mild).
/FTId=VAR_006588.
VARIANT 342 342 T -> M (in HEMB; moderate;
dbSNP:rs137852254).
{ECO:0000269|PubMed:12604421,
ECO:0000269|PubMed:2773937,
ECO:0000269|PubMed:9222764}.
/FTId=VAR_006589.
VARIANT 344 344 I -> L (in HEMB).
{ECO:0000269|PubMed:12604421}.
/FTId=VAR_017356.
VARIANT 351 351 G -> D (in HEMB).
/FTId=VAR_006590.
VARIANT 356 356 W -> C (in HEMB; severe).
/FTId=VAR_006591.
VARIANT 357 357 G -> E (in HEMB; severe; Amagasaki;
dbSNP:rs137852275).
{ECO:0000269|PubMed:1958666}.
/FTId=VAR_006592.
VARIANT 357 357 G -> R (in HEMB; dbSNP:rs137852257).
{ECO:0000269|PubMed:2773937}.
/FTId=VAR_017316.
VARIANT 362 362 K -> E (in HEMB; moderate).
/FTId=VAR_006593.
VARIANT 363 363 G -> W (in HEMB).
/FTId=VAR_006594.
VARIANT 366 366 A -> D (in HEMB).
/FTId=VAR_006595.
VARIANT 379 379 R -> G (in HEMB; moderate).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_006596.
VARIANT 379 379 R -> Q (in HEMB; severe; Iceland-1,
London and Sesimbra; dbSNP:rs137852259).
{ECO:0000269|PubMed:8076946,
ECO:0000269|PubMed:8257988,
ECO:0000269|PubMed:9600455}.
/FTId=VAR_006597.
VARIANT 382 382 C -> Y (in HEMB).
/FTId=VAR_006598.
VARIANT 383 383 L -> F (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017358.
VARIANT 383 383 L -> I (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017357.
VARIANT 384 384 R -> L (in THPH8; factor IX Padua; higher
specific activity than wild-type;
dbSNP:rs137852283).
{ECO:0000269|PubMed:19846852}.
/FTId=VAR_062999.
VARIANT 387 387 K -> E (in HEMB; mild).
{ECO:0000269|PubMed:9600455}.
/FTId=VAR_006599.
VARIANT 390 390 I -> F (in HEMB; severe).
/FTId=VAR_006600.
VARIANT 394 394 M -> K (in HEMB).
/FTId=VAR_006601.
VARIANT 395 395 F -> I (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017359.
VARIANT 395 395 F -> L (in HEMB).
{ECO:0000269|PubMed:12604421}.
/FTId=VAR_017360.
VARIANT 396 396 C -> F (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017361.
VARIANT 396 396 C -> S (in HEMB; severe;
dbSNP:rs137852273).
/FTId=VAR_006602.
VARIANT 397 397 A -> P (in HEMB; mild; Hong Kong-11;
dbSNP:rs137852281).
{ECO:0000269|PubMed:9590153}.
/FTId=VAR_017317.
VARIANT 404 404 R -> T (in HEMB).
/FTId=VAR_006603.
VARIANT 407 407 C -> R (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017362.
VARIANT 407 407 C -> S (in HEMB; severe).
/FTId=VAR_006604.
VARIANT 410 410 D -> H (in HEMB; Mechtal;
dbSNP:rs137852278).
{ECO:0000269|PubMed:1346975}.
/FTId=VAR_017318.
VARIANT 411 411 S -> G (in HEMB; Varel;
dbSNP:rs137852277).
{ECO:0000269|PubMed:1346975}.
/FTId=VAR_017320.
VARIANT 411 411 S -> I (in HEMB; Schmallenberg;
dbSNP:rs137852276).
{ECO:0000269|PubMed:1346975}.
/FTId=VAR_017319.
VARIANT 412 412 G -> E (in HEMB).
{ECO:0000269|PubMed:12588353}.
/FTId=VAR_017363.
VARIANT 413 413 G -> R (in HEMB; moderate to severe).
{ECO:0000269|PubMed:7981722,
ECO:0000269|PubMed:9222764}.
/FTId=VAR_006605.
VARIANT 414 414 P -> T (in HEMB; Bergamo; increased
protein abundance; loss of function in
blood coagulation; dbSNP:rs137852265).
{ECO:0000269|PubMed:12604421,
ECO:0000269|PubMed:2162822,
ECO:0000269|PubMed:25251685}.
/FTId=VAR_017321.
VARIANT 419 419 V -> E (in HEMB; moderately severe;
dbSNP:rs137852280).
{ECO:0000269|PubMed:8076946,
ECO:0000269|PubMed:8199596}.
/FTId=VAR_006606.
VARIANT 424 424 F -> V (in HEMB).
{ECO:0000269|PubMed:9222764}.
/FTId=VAR_006607.
VARIANT 426 426 T -> P (in HEMB; severe; Barcelos).
{ECO:0000269|PubMed:8257988}.
/FTId=VAR_006608.
VARIANT 430 430 S -> T (in HEMB).
/FTId=VAR_006609.
VARIANT 431 431 W -> G (in HEMB).
/FTId=VAR_006610.
VARIANT 431 431 W -> R (in HEMB; moderate).
/FTId=VAR_006611.
VARIANT 432 432 G -> S (in HEMB; severe).
/FTId=VAR_006612.
VARIANT 432 432 G -> V (in HEMB; severe).
{ECO:0000269|PubMed:9600455}.
/FTId=VAR_006613.
VARIANT 433 433 E -> A (in HEMB).
/FTId=VAR_006614.
VARIANT 433 433 E -> K (in HEMB; dbSNP:rs767828752).
/FTId=VAR_006615.
VARIANT 435 435 C -> Y (in HEMB).
{ECO:0000269|PubMed:12604421}.
/FTId=VAR_017364.
VARIANT 436 436 A -> V (in HEMB; moderately severe;
Niigata; dbSNP:rs137852266).
{ECO:0000269|PubMed:3243764}.
/FTId=VAR_006616.
VARIANT 442 442 G -> E (in HEMB).
{ECO:0000269|PubMed:12604421}.
/FTId=VAR_017365.
VARIANT 442 442 G -> R (in HEMB; severe; Angers;
dbSNP:rs137852267).
{ECO:0000269|PubMed:2714791}.
/FTId=VAR_017322.
VARIANT 443 443 I -> T (in HEMB; moderately severe; Long
Beach, Los Angeles and Vancouver;
dbSNP:rs137852268).
{ECO:0000269|PubMed:1902289,
ECO:0000269|PubMed:3401602}.
/FTId=VAR_017323.
VARIANT 445 445 T -> TIYT (in HEMB; severe; Lousada).
/FTId=VAR_006617.
VARIANT 447 447 V -> VYTKV (in HEMB; reduced protein
abundance; loss of function in blood
coagulation).
{ECO:0000269|PubMed:25251685}.
/FTId=VAR_073983.
VARIANT 449 449 R -> Q (in HEMB; mild;
dbSNP:rs143018900).
{ECO:0000269|PubMed:8076946}.
/FTId=VAR_006618.
VARIANT 449 449 R -> W (in HEMB; mild;
dbSNP:rs757996262).
{ECO:0000269|PubMed:12604421}.
/FTId=VAR_006619.
VARIANT 450 450 Y -> C (in HEMB; severe).
{ECO:0000269|PubMed:9600455}.
/FTId=VAR_006620.
VARIANT 453 453 W -> R (in HEMB; dbSNP:rs137852269).
{ECO:0000269|PubMed:2773937}.
/FTId=VAR_017324.
VARIANT 454 454 I -> T (in HEMB; Italy).
{ECO:0000269|PubMed:9452115}.
/FTId=VAR_006621.
VARIANT 461 461 T -> P (in dbSNP:rs4149751).
{ECO:0000269|Ref.7}.
/FTId=VAR_014308.
MUTAGEN 305 305 Y->F: Strongly increases enzyme activity
with a synthetic peptide substrate; when
associated with T-311; A-365 and T-391.
{ECO:0000269|PubMed:12444082}.
MUTAGEN 311 311 K->T: Strongly increases enzyme activity
with a synthetic peptide substrate; when
associated with F-305; A-365 and T-391.
{ECO:0000269|PubMed:12444082}.
MUTAGEN 312 312 Y->A: Strongly decreases enzyme activity
with a synthetic peptide substrate.
{ECO:0000269|PubMed:12444082}.
MUTAGEN 391 391 Y->T: Strongly increases enzyme activity
with a synthetic peptide substrate; when
associated with F-305; T-311 and A-365.
{ECO:0000269|PubMed:12444082}.
STRAND 50 52 {ECO:0000244|PDB:1NL0}.
HELIX 60 64 {ECO:0000244|PDB:1NL0}.
STRAND 65 67 {ECO:0000244|PDB:1CFH}.
HELIX 71 75 {ECO:0000244|PDB:1NL0}.
STRAND 78 80 {ECO:0000244|PDB:1NL0}.
HELIX 81 90 {ECO:0000244|PDB:1NL0}.
TURN 96 99 {ECO:0000244|PDB:1EDM}.
STRAND 102 105 {ECO:0000244|PDB:4WMA}.
STRAND 107 111 {ECO:0000244|PDB:1EDM}.
STRAND 114 118 {ECO:0000244|PDB:1EDM}.
TURN 125 128 {ECO:0000244|PDB:4WMA}.
TURN 134 136 {ECO:0000244|PDB:2WPH}.
HELIX 137 140 {ECO:0000244|PDB:5JB9}.
STRAND 142 148 {ECO:0000244|PDB:5JB9}.
TURN 149 151 {ECO:0000244|PDB:5JB9}.
STRAND 152 156 {ECO:0000244|PDB:5JB9}.
STRAND 161 163 {ECO:0000244|PDB:5JB9}.
STRAND 165 168 {ECO:0000244|PDB:2WPI}.
STRAND 170 172 {ECO:0000244|PDB:5JB9}.
STRAND 174 176 {ECO:0000244|PDB:5JB9}.
STRAND 187 189 {ECO:0000244|PDB:2WPJ}.
STRAND 241 248 {ECO:0000244|PDB:5JB9}.
STRAND 252 258 {ECO:0000244|PDB:5JB9}.
STRAND 261 264 {ECO:0000244|PDB:5JB9}.
HELIX 266 268 {ECO:0000244|PDB:5JB9}.
STRAND 269 271 {ECO:0000244|PDB:5JB9}.
STRAND 276 280 {ECO:0000244|PDB:5JB9}.
STRAND 282 286 {ECO:0000244|PDB:1RFN}.
STRAND 292 301 {ECO:0000244|PDB:5JB9}.
TURN 303 306 {ECO:0000244|PDB:5JB9}.
STRAND 307 310 {ECO:0000244|PDB:5JB9}.
TURN 311 314 {ECO:0000244|PDB:4YZU}.
STRAND 317 323 {ECO:0000244|PDB:5JB9}.
HELIX 339 347 {ECO:0000244|PDB:5JB9}.
STRAND 350 360 {ECO:0000244|PDB:5JB9}.
STRAND 370 377 {ECO:0000244|PDB:5JB9}.
HELIX 379 384 {ECO:0000244|PDB:5JB9}.
STRAND 394 398 {ECO:0000244|PDB:5JB9}.
STRAND 414 419 {ECO:0000244|PDB:5JB9}.
STRAND 422 431 {ECO:0000244|PDB:5JB9}.
STRAND 433 436 {ECO:0000244|PDB:5JB9}.
STRAND 442 446 {ECO:0000244|PDB:5JB9}.
HELIX 447 450 {ECO:0000244|PDB:5JB9}.
HELIX 451 457 {ECO:0000244|PDB:5JB9}.
SEQUENCE 461 AA; 51778 MW; C4720C1234477EF5 CRC64;
MQRVNMIMAE SPGLITICLL GYLLSAECTV FLDHENANKI LNRPKRYNSG KLEEFVQGNL
ERECMEEKCS FEEAREVFEN TERTTEFWKQ YVDGDQCESN PCLNGGSCKD DINSYECWCP
FGFEGKNCEL DVTCNIKNGR CEQFCKNSAD NKVVCSCTEG YRLAENQKSC EPAVPFPCGR
VSVSQTSKLT RAETVFPDVD YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW
QVVLNGKVDA FCGGSIVNEK WIVTAAHCVE TGVKITVVAG EHNIEETEHT EQKRNVIRII
PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS GYVSGWGRVF
HKGRSALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH EGGRDSCQGD SGGPHVTEVE
GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T


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