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Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain]

 FA5_HUMAN               Reviewed;        2224 AA.
P12259; A8K6E8; Q14285; Q2EHR5; Q5R346; Q5R347; Q6UPU6; Q8WWQ6;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 4.
20-JUN-2018, entry version 219.
RecName: Full=Coagulation factor V;
AltName: Full=Activated protein C cofactor;
AltName: Full=Proaccelerin, labile factor;
Contains:
RecName: Full=Coagulation factor V heavy chain;
Contains:
RecName: Full=Coagulation factor V light chain;
Flags: Precursor;
Name=F5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEOLYTIC CLEAVAGE AT ARG-737; ARG-1046
AND ARG-1573 BY THROMBIN, AND VARIANTS ARG-858; ARG-865; GLU-925;
PHE-1397 AND VAL-1764.
PubMed=3110773; DOI=10.1073/pnas.84.14.4846;
Jenny R.J., Pittman D.D., Toole J.J., Kriz R.W., Aldape R.A.,
Hewick R.M., Kaufman R.J., Mann K.G.;
"Complete cDNA and derived amino acid sequence of human factor V.";
Proc. Natl. Acad. Sci. U.S.A. 84:4846-4850(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1567832; DOI=10.1021/bi00130a007;
Cripe L.D., Moore K.D., Kane W.H.;
"Structure of the gene for human coagulation factor V.";
Biochemistry 31:3777-3785(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THPH2 GLN-534, AND VARIANTS
SER-15; HIS-107; THR-413; LYS-513; SER-809; THR-817; ARG-858; ARG-865;
SER-915; GLU-925; SER-969; LEU-980; GLN-1146; ILE-1285; SER-1404;
ALA-1530 AND THR-2148.
SeattleSNPs variation discovery resource;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THPH2
GLN-534.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1030, AND VARIANT LYS-513.
TISSUE=Placenta;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1600, AND VARIANTS ARG-858; ARG-865;
GLU-925 AND ILE-1285.
PubMed=2827731; DOI=10.1021/bi00394a033;
Kane W.H., Ichinose A., Hagen F.S., Davie E.W.;
"Cloning of cDNAs coding for the heavy chain region and connecting
region of human factor V, a blood coagulation factor with four types
of internal repeats.";
Biochemistry 26:6508-6514(1987).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 658-1598.
Kostka H.;
"Human coagulation factor V, exon 13, missense mutation Asn713Ser.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 660-1598, AND VARIANTS ARG-858; ARG-865;
GLU-925 AND PHE-1397.
PubMed=11758222;
Xie F., Cheng F., Zhu X.;
"Studies on hereditary deficiency of coagulation factor V.";
Zhonghua Xue Ye Xue Za Zhi 22:453-456(2001).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1188-1215 AND 1315-2224.
PubMed=3092220; DOI=10.1073/pnas.83.18.6800;
Kane W.H., Davie E.W.;
"Cloning of a cDNA coding for human factor V, a blood coagulation
factor homologous to factor VIII and ceruloplasmin.";
Proc. Natl. Acad. Sci. U.S.A. 83:6800-6804(1986).
[10]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=8454869;
Shen N.L.L., Fan S.-T., Pyati J., Graff R., Lapolla R.J.,
Edgington T.S.;
"The serine protease cofactor factor V is synthesized by
lymphocytes.";
J. Immunol. 150:2992-3001(1993).
[11]
ENZYME REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=6323392;
Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.;
"Mechanism of inhibition of activated protein C by protein C
inhibitor.";
J. Biochem. 95:187-195(1984).
[12]
COPPER-BINDING.
PubMed=6490642;
Mann K.G., Lawler C.M., Vehar G.A., Church W.R.;
"Coagulation Factor V contains copper ion.";
J. Biol. Chem. 259:12949-12951(1984).
[13]
ENZYME REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=2844223; DOI=10.1021/bi00412a005;
Meijers J.C., Kanters D.H., Vlooswijk R.A., van Erp H.E., Hessing M.,
Bouma B.N.;
"Inactivation of human plasma kallikrein and factor XIa by protein C
inhibitor.";
Biochemistry 27:4231-4237(1988).
[14]
SULFATION.
PubMed=8204629; DOI=10.1021/bi00188a026;
Pittman D.D., Tomkinson K.N., Michnick D., Selighsohn U.,
Kaufman R.J.;
"Posttranslational sulfation of factor V is required for efficient
thrombin cleavage and activation and for full procoagulant activity.";
Biochemistry 33:6952-6959(1994).
[15]
SULFATION.
PubMed=2168225;
Hortin G.L.;
"Sulfation of tyrosine residues in coagulation factor V.";
Blood 76:946-952(1990).
[16]
PROTEOLYTIC CLEAVAGE AT ARG-334; ARG-534; ARG-707 AND LYS-1022 BY
ACTIVATED PROTEIN C.
PubMed=7989361;
Kalafatis M., Rand M.D., Mann K.G.;
"The mechanism of inactivation of human factor V and human factor Va
by activated protein C.";
J. Biol. Chem. 269:31869-31880(1994).
[17]
HETERODIMER WITH SERPINA5.
PubMed=8665956; DOI=10.1111/j.1432-1033.1996.0088q.x;
Kise H., Nishioka J., Kawamura J., Suzuki K.;
"Characterization of semenogelin II and its molecular interaction with
prostate-specific antigen and protein C inhibitor.";
Eur. J. Biochem. 238:88-96(1996).
[18]
ENZYME REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=9556620; DOI=10.1074/jbc.273.18.11281;
Nishioka J., Ning M., Hayashi T., Suzuki K.;
"Protein C inhibitor secreted from activated platelets efficiently
inhibits activated protein C on phosphatidylethanolamine of platelet
membrane and microvesicles.";
J. Biol. Chem. 273:11281-11287(1998).
[19]
INVOLVEMENT IN RPRGL1 SUSCEPTIBILITY.
PubMed=11018168; DOI=10.1056/NEJM200010053431405;
Martinelli I., Taioli E., Cetin I., Marinoni A., Gerosa S.,
Villa M.V., Bozzo M., Mannucci P.M.;
"Mutations in coagulation factors in women with unexplained late fetal
loss.";
N. Engl. J. Med. 343:1015-1018(2000).
[20]
ENZYME REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=15140131; DOI=10.1111/j.1538-7836.2004.00733.x;
Hayashi T., Nishioka J., Kamada H., Asanuma K., Kondo H.,
Gabazza E.C., Ido M., Suzuki K.;
"Characterization of a novel human protein C inhibitor (PCI) gene
transgenic mouse useful for studying the role of PCI in physiological
and pathological conditions.";
J. Thromb. Haemost. 2:949-961(2004).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297; ASN-460; ASN-821;
ASN-977 AND ASN-1559.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-640, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[25]
PHOSPHORYLATION AT SER-859.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[26]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2065-2224.
PubMed=10586886; DOI=10.1038/46594;
Macedo-Ribeiro S., Bode W., Huber R., Quinn-Allen M.A., Kim S.W.,
Ortel T.L., Bourenkov G.P., Bartunik H.D., Stubbs M.T., Kane W.H.,
Fuentes-Prior P.;
"Crystal structures of the membrane-binding C2 domain of human
coagulation factor V.";
Nature 402:434-439(1999).
[27]
VARIANT VAL-1764.
PubMed=7874144;
Bayston T.A., Ireland H., Olds R.J., Thein S.L., Lane D.A.;
"A polymorphism in the human coagulation factor V gene.";
Hum. Mol. Genet. 3:2085-2085(1994).
[28]
VARIANT THPH2 GLN-534.
PubMed=8164741; DOI=10.1038/369064a0;
Bertina R.M., Koeleman B.P.C., Koster T., Rosendaal F.R., Dirven R.J.,
de Ronde H., van der Velden P.A., Reitsma P.H.;
"Mutation in blood coagulation factor V associated with resistance to
activated protein C.";
Nature 369:64-67(1994).
[29]
VARIANTS ILE-1285 AND ARG-1327.
PubMed=8713778;
Lunghi B., Iacoviello L., Gemmati D., Dilasio M.G., Castoldi E.,
Pinotti M., Castaman G., Redaelli R., Mariani G., Marchetti G.,
Bernardi F.;
"Detection of new polymorphic markers in the factor V gene:
association with factor V levels in plasma.";
Thromb. Haemost. 75:45-48(1996).
[30]
ASSOCIATION OF VARIANT LEIDEN GLN-534 WITH SUSCEPTIBILITY TO
BUDD-CHIARI SYNDROME.
PubMed=9245936; DOI=10.1136/gut.40.6.798;
Mahmoud A.E.A., Elias E., Beauchamp N., Wilde J.T.;
"Prevalence of the factor V Leiden mutation in hepatic and portal vein
thrombosis.";
Gut 40:798-800(1997).
[31]
VARIANT HONG KONG GLY-334, AND VARIANT LYS-513.
PubMed=9454741;
Chan W.P., Lee C.K., Kwong Y.L., Lam C.K., Liang R.;
"A novel mutation of Arg306 of factor V gene in Hong Kong Chinese.";
Blood 91:1135-1139(1998).
[32]
VARIANT THPH2 THR-334.
PubMed=9454742;
Williamson D., Brown K., Luddington R., Baglin C., Baglin T.;
"Factor V Cambridge: a new mutation (Arg306-to-Thr) associated with
resistance to activated protein C.";
Blood 91:1140-1144(1998).
[33]
VARIANT HONG KONG GLY-334.
PubMed=9746807;
Liang R., Lee C.K., Wat M.S., Kwong Y.L., Lam C.K., Liu H.W.;
"Clinical significance of Arg306 mutations of factor V gene.";
Blood 92:2599-2600(1998).
[34]
VARIANT THPH2 GLN-534, AND VARIANTS HIS-107; THR-413; LYS-513;
SER-809; THR-817; ARG-858; ARG-865; GLU-925; GLN-1146; ALA-1530;
SER-1685; VAL-1749; VAL-1764; ILE-1820 AND GLY-2222.
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).
[35]
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).
[36]
VARIANT FA5D CYS-1730, VARIANT THPH2 GLN-534, AND VARIANT ARG-1327.
PubMed=10942390;
Castoldi E., Simioni P., Kalafatis M., Lunghi B., Tormene D.,
Girelli D., Girolami A., Bernardi F.;
"Combinations of 4 mutations (FV R506Q, FV H1299R, FV Y1702C, PT
20210G/A) affecting the prothrombinase complex in a thrombophilic
family.";
Blood 96:1443-1448(2000).
[37]
VARIANTS THPH2 ARG-613 AND CYS-1730.
PubMed=11435304; DOI=10.1182/blood.V98.2.358;
van Wijk R., Nieuwenhuis K., van den Berg M., Huizinga E.G.,
van der Meijden B.B., Kraaijenhagen R.J., van Solinge W.W.;
"Five novel mutations in the gene for human blood coagulation factor V
associated with type I factor V deficiency.";
Blood 98:358-367(2001).
[38]
VARIANT THPH2 HIS-2102.
PubMed=11858490;
Schrijver I., Houissa-Kastally R., Jones C.D., Garcia K.C.,
Zehnder J.L.;
"Novel factor V C2-domain mutation (R2074H) in two families with
factor V deficiency and bleeding.";
Thromb. Haemost. 87:294-299(2002).
[39]
VARIANT FA5D CYS-2102, AND CHARACTERIZATION OF VARIANT FA5D CYS-2102.
PubMed=12393490; DOI=10.1182/blood-2002-06-1928;
Duga S., Montefusco M.C., Asselta R., Malcovati M., Peyvandi F.,
Santagostino E., Mannucci P.M., Tenchini M.L.;
"Arg2074Cys missense mutation in the C2 domain of factor V causing
moderately severe factor V deficiency: molecular characterization by
expression of the recombinant protein.";
Blood 101:173-177(2003).
[40]
VARIANT THPH2 THR-387.
PubMed=14617013; DOI=10.1046/j.1365-2141.2003.04624.x;
Mumford A.D., McVey J.H., Morse C.V., Gomez K., Steen M.,
Norstrom E.A., Tuddenham E.G.D., Dahlback B., Bolton-Maggs P.H.B.;
"Factor V I359T: a novel mutation associated with thrombosis and
resistance to activated protein C.";
Br. J. Haematol. 123:496-501(2003).
[41]
ASSOCIATION OF VARIANT GLN-534 WITH SUSCEPTIBILITY TO ISCHSTR.
PubMed=15534175; DOI=10.1001/archneur.61.11.1652;
Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.;
"Meta-analysis of genetic studies in ischemic stroke: thirty-two genes
involving approximately 18,000 cases and 58,000 controls.";
Arch. Neurol. 61:1652-1661(2004).
[42]
CHARACTERIZATION OF VARIANT THPH2 THR-387.
PubMed=14695241; DOI=10.1182/blood-2003-06-2092;
Steen M., Norstroem E.A., Tholander A.-L., Bolton-Maggs P.H.B.,
Mumford A., McVey J.H., Tuddenham E.G.D., Dahlbaeck B.;
"Functional characterization of factor V-Ile359Thr: a novel mutation
associated with thrombosis.";
Blood 103:3381-3387(2004).
[43]
VARIANT [LARGE SCALE ANALYSIS] ALA-775.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Central regulator of hemostasis. It serves as a critical
cofactor for the prothrombinase activity of factor Xa that results
in the activation of prothrombin to thrombin.
-!- ENZYME REGULATION: Inhibited by SERPINA5.
{ECO:0000269|PubMed:15140131, ECO:0000269|PubMed:2844223,
ECO:0000269|PubMed:6323392, ECO:0000269|PubMed:9556620}.
-!- SUBUNIT: Factor Va, the activated form of factor V, is composed of
a heavy chain and a light chain, non-covalently bound. The
interaction between the two chains is calcium-dependent. Forms
heterodimer with SERPINA5.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Plasma.
-!- DOMAIN: Domain B contains 35 x 9 AA tandem repeats, and 2 x 17 AA
repeats.
-!- PTM: Thrombin activates factor V proteolytically to the active
cofactor, factor Va (formation of a heavy chain at the N-terminus
and a light chain at the C-terminus).
-!- PTM: Sulfation is required for efficient thrombin cleavage and
activation and for full procoagulant activity.
{ECO:0000269|PubMed:2168225, ECO:0000269|PubMed:7989361,
ECO:0000269|PubMed:8204629}.
-!- PTM: Activated protein C inactivates factor V and factor Va by
proteolytic degradation. {ECO:0000269|PubMed:7989361}.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- DISEASE: Factor V deficiency (FA5D) [MIM:227400]: A blood
coagulation disorder leading to a hemorrhagic diathesis known as
parahemophilia. {ECO:0000269|PubMed:10942390,
ECO:0000269|PubMed:12393490}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Thrombophilia due to activated protein C resistance
(THPH2) [MIM:188055]: A hemostatic disorder due to defective
degradation of factor V by activated protein C. It is
characterized by a poor anticoagulant response to activated
protein C resulting in tendency to thrombosis.
{ECO:0000269|PubMed:10391209, ECO:0000269|PubMed:10942390,
ECO:0000269|PubMed:11435304, ECO:0000269|PubMed:11858490,
ECO:0000269|PubMed:14617013, ECO:0000269|PubMed:14695241,
ECO:0000269|PubMed:16710414, ECO:0000269|PubMed:8164741,
ECO:0000269|PubMed:9454742}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Budd-Chiari syndrome (BDCHS) [MIM:600880]: A syndrome
caused by obstruction of hepatic venous outflow involving either
the hepatic veins or the terminal segment of the inferior vena
cava. Obstructions are generally caused by thrombosis and lead to
hepatic congestion and ischemic necrosis. Clinical manifestations
observed in the majority of patients include hepatomegaly, right
upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is
associated with a combination of disease states including primary
myeloproliferative syndromes and thrombophilia due to factor V
Leiden, protein C deficiency and antithrombin III deficiency.
Budd-Chiari syndrome is a rare but typical complication in
patients with polycythemia vera. {ECO:0000269|PubMed:9245936}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an
acute neurologic event leading to death of neural tissue of the
brain and resulting in loss of motor, sensory and/or cognitive
function. Ischemic strokes, resulting from vascular occlusion, is
considered to be a highly complex disease consisting of a group of
heterogeneous disorders with multiple genetic and environmental
risk factors. {ECO:0000269|PubMed:15534175}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- DISEASE: Pregnancy loss, recurrent, 1 (RPRGL1) [MIM:614389]: A
common complication of pregnancy, resulting in spontaneous
abortion before the fetus has reached viability. The term includes
all miscarriages from the time of conception until 24 weeks of
gestation. Recurrent pregnancy loss is defined as 3 or more
consecutive spontaneous abortions. {ECO:0000269|PubMed:11018168}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABD23003.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI23065.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Factor V entry;
URL="https://en.wikipedia.org/wiki/Factor_V";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/f5/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=F5";
-----------------------------------------------------------------------
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EMBL; M16967; AAA52424.1; -; mRNA.
EMBL; L32779; AAB59401.1; -; Genomic_DNA.
EMBL; L32755; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32756; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32757; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32758; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32759; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32760; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32761; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32762; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32763; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32764; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32765; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32766; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32767; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32768; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32769; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32770; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32771; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32772; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32773; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32774; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32775; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32776; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32777; AAB59401.1; JOINED; Genomic_DNA.
EMBL; L32778; AAB59401.1; JOINED; Genomic_DNA.
EMBL; AY364535; AAQ55063.1; -; Genomic_DNA.
EMBL; Z99572; CAB16748.1; -; Genomic_DNA.
EMBL; Z99572; CAI23065.1; ALT_SEQ; Genomic_DNA.
EMBL; AK291613; BAF84302.1; -; mRNA.
EMBL; M14335; AAB59532.1; -; mRNA.
EMBL; DQ377944; ABD23003.1; ALT_SEQ; Genomic_DNA.
EMBL; AJ297255; CAC82573.1; -; mRNA.
CCDS; CCDS1281.1; -.
PIR; A56172; KFHU5.
RefSeq; NP_000121.2; NM_000130.4.
UniGene; Hs.30054; -.
PDB; 1CZS; X-ray; 1.90 A; A=2065-2224.
PDB; 1CZT; X-ray; 1.87 A; A=2065-2224.
PDB; 1CZV; X-ray; 2.40 A; A/B=2065-2224.
PDB; 1FV4; Model; -; H=29-691, L=1574-2224.
PDB; 1Y61; Model; -; H=29-737, L=1574-2224.
PDB; 3P6Z; X-ray; 1.70 A; C/I=685-737.
PDB; 3P70; X-ray; 2.55 A; M/N/O/P=685-737.
PDB; 3S9C; X-ray; 1.80 A; B=1561-1574.
PDBsum; 1CZS; -.
PDBsum; 1CZT; -.
PDBsum; 1CZV; -.
PDBsum; 1FV4; -.
PDBsum; 1Y61; -.
PDBsum; 3P6Z; -.
PDBsum; 3P70; -.
PDBsum; 3S9C; -.
ProteinModelPortal; P12259; -.
SMR; P12259; -.
BioGrid; 108452; 13.
DIP; DIP-47331N; -.
IntAct; P12259; 3.
MINT; P12259; -.
STRING; 9606.ENSP00000356771; -.
BindingDB; P12259; -.
ChEMBL; CHEMBL3618; -.
DrugBank; DB00055; Drotrecogin alfa.
DrugBank; DB05777; Thrombomodulin Alfa.
CarbonylDB; P12259; -.
iPTMnet; P12259; -.
PhosphoSitePlus; P12259; -.
BioMuta; F5; -.
DMDM; 308153653; -.
MaxQB; P12259; -.
PaxDb; P12259; -.
PeptideAtlas; P12259; -.
PRIDE; P12259; -.
ProteomicsDB; 52838; -.
DNASU; 2153; -.
Ensembl; ENST00000367797; ENSP00000356771; ENSG00000198734.
GeneID; 2153; -.
KEGG; hsa:2153; -.
UCSC; uc001ggg.2; human.
CTD; 2153; -.
DisGeNET; 2153; -.
EuPathDB; HostDB:ENSG00000198734.10; -.
GeneCards; F5; -.
GeneReviews; F5; -.
HGNC; HGNC:3542; F5.
HPA; HPA002036; -.
MalaCards; F5; -.
MIM; 188055; phenotype.
MIM; 227400; phenotype.
MIM; 600880; phenotype.
MIM; 601367; phenotype.
MIM; 612309; gene.
MIM; 614389; phenotype.
neXtProt; NX_P12259; -.
OpenTargets; ENSG00000198734; -.
Orphanet; 131; Budd-Chiari syndrome.
Orphanet; 329217; Cerebral sinovenous thrombosis.
Orphanet; 326; Congenital factor V deficiency.
Orphanet; 391320; East Texas bleeding disorder.
Orphanet; 64738; Non rare thrombophilia.
PharmGKB; PA159; -.
eggNOG; ENOG410IJ6Y; Eukaryota.
eggNOG; ENOG4111F6G; LUCA.
GeneTree; ENSGT00910000143988; -.
HOVERGEN; HBG005631; -.
InParanoid; P12259; -.
KO; K03902; -.
PhylomeDB; P12259; -.
TreeFam; TF329807; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P12259; -.
ChiTaRS; F5; human.
EvolutionaryTrace; P12259; -.
GeneWiki; Factor_V; -.
GenomeRNAi; 2153; -.
PRO; PR:P12259; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000198734; -.
CleanEx; HS_F5; -.
ExpressionAtlas; P12259; baseline and differential.
Genevisible; P12259; HS.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0008015; P:blood circulation; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
Gene3D; 2.60.120.260; -; 2.
Gene3D; 2.60.40.420; -; 5.
InterPro; IPR011707; Cu-oxidase_3.
InterPro; IPR033138; Cu_oxidase_CS.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR000421; FA58C.
InterPro; IPR024715; Factor_5/8_like.
InterPro; IPR008979; Galactose-bd-like_sf.
Pfam; PF07732; Cu-oxidase_3; 2.
Pfam; PF00754; F5_F8_type_C; 2.
PIRSF; PIRSF000354; Factors_V_VIII; 1.
SMART; SM00231; FA58C; 2.
SUPFAM; SSF49503; SSF49503; 6.
SUPFAM; SSF49785; SSF49785; 2.
PROSITE; PS01285; FA58C_1; 2.
PROSITE; PS01286; FA58C_2; 2.
PROSITE; PS50022; FA58C_3; 2.
PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
1: Evidence at protein level;
3D-structure; Blood coagulation; Calcium; Complete proteome; Copper;
Disease mutation; Disulfide bond; Glycoprotein; Hemostasis;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Secreted; Signal; Sulfation; Thrombophilia; Zymogen.
SIGNAL 1 28
CHAIN 29 2224 Coagulation factor V.
/FTId=PRO_0000002978.
CHAIN 29 737 Coagulation factor V heavy chain.
/FTId=PRO_0000002979.
PROPEP 738 1573 Activation peptide (connecting region).
/FTId=PRO_0000002980.
CHAIN 1574 2224 Coagulation factor V light chain.
/FTId=PRO_0000002981.
DOMAIN 30 329 F5/8 type A 1.
DOMAIN 30 193 Plastocyanin-like 1.
DOMAIN 203 329 Plastocyanin-like 2.
DOMAIN 348 684 F5/8 type A 2.
DOMAIN 348 526 Plastocyanin-like 3.
DOMAIN 536 684 Plastocyanin-like 4.
REPEAT 895 911 1-1.
REPEAT 912 928 1-2.
REPEAT 1185 1193 2-1.
REPEAT 1194 1202 2-2.
REPEAT 1203 1211 2-3.
REPEAT 1212 1220 2-4.
REPEAT 1221 1229 2-5.
REPEAT 1230 1238 2-6.
REPEAT 1239 1247 2-7.
REPEAT 1248 1256 2-8.
REPEAT 1257 1265 2-9.
REPEAT 1266 1274 2-10.
REPEAT 1275 1283 2-11.
REPEAT 1284 1292 2-12.
REPEAT 1293 1301 2-13.
REPEAT 1302 1310 2-14.
REPEAT 1311 1319 2-15.
REPEAT 1320 1328 2-16.
REPEAT 1329 1337 2-17.
REPEAT 1338 1346 2-18.
REPEAT 1347 1355 2-19.
REPEAT 1356 1364 2-20.
REPEAT 1365 1373 2-21.
REPEAT 1374 1382 2-22.
REPEAT 1383 1391 2-23.
REPEAT 1392 1400 2-24.
REPEAT 1401 1409 2-25.
REPEAT 1410 1418 2-26.
REPEAT 1419 1427 2-27.
REPEAT 1428 1436 2-28.
REPEAT 1437 1445 2-29.
REPEAT 1446 1454 2-30.
REPEAT 1455 1463 2-31.
REPEAT 1464 1472 2-32.
REPEAT 1473 1481 2-33.
REPEAT 1482 1490 2-34.
REPEAT 1493 1501 2-35.
DOMAIN 1578 1907 F5/8 type A 3.
DOMAIN 1578 1751 Plastocyanin-like 5.
DOMAIN 1761 1907 Plastocyanin-like 6.
DOMAIN 1907 2061 F5/8 type C 1. {ECO:0000255|PROSITE-
ProRule:PRU00081}.
DOMAIN 2066 2221 F5/8 type C 2. {ECO:0000255|PROSITE-
ProRule:PRU00081}.
REGION 692 1573 B.
REGION 895 928 2 X 17 AA tandem repeats.
REGION 1185 1501 35 X 9 AA approximate tandem repeats of
[TNP]-L-S-P-D-L-S-Q-T.
METAL 139 139 Calcium. {ECO:0000250}.
METAL 140 140 Calcium. {ECO:0000250}.
METAL 1843 1843 Copper. {ECO:0000250}.
METAL 1845 1845 Copper. {ECO:0000250}.
SITE 334 335 Cleavage; by activated protein C.
{ECO:0000269|PubMed:7989361}.
SITE 534 535 Cleavage; by activated protein C.
{ECO:0000269|PubMed:7989361}.
SITE 707 708 Cleavage; by activated protein C.
{ECO:0000269|PubMed:7989361}.
SITE 737 738 Cleavage; by thrombin.
{ECO:0000269|PubMed:3110773}.
SITE 1022 1023 Cleavage; by activated protein C.
{ECO:0000269|PubMed:7989361}.
SITE 1046 1047 Cleavage; by thrombin.
{ECO:0000269|PubMed:3110773}.
SITE 1573 1574 Cleavage; by thrombin.
{ECO:0000269|PubMed:3110773}.
MOD_RES 640 640 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 693 693 Sulfotyrosine. {ECO:0000255}.
MOD_RES 724 724 Sulfotyrosine. {ECO:0000255}.
MOD_RES 726 726 Sulfotyrosine. {ECO:0000255}.
MOD_RES 859 859 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 1522 1522 Sulfotyrosine. {ECO:0000255}.
MOD_RES 1538 1538 Sulfotyrosine. {ECO:0000255}.
MOD_RES 1543 1543 Sulfotyrosine. {ECO:0000255}.
MOD_RES 1593 1593 Sulfotyrosine. {ECO:0000255}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 460 460 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 554 554 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 741 741 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 752 752 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 760 760 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 776 776 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 782 782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 821 821 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 938 938 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 977 977 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 1074 1074 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1083 1083 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1103 1103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1106 1106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1479 1479 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1499 1499 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1559 1559 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 1703 1703 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2010 2010 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2209 2209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 167 193 {ECO:0000255|PROSITE-ProRule:PRU00081}.
DISULFID 248 329 {ECO:0000255|PROSITE-ProRule:PRU00081}.
DISULFID 500 526 {ECO:0000255|PROSITE-ProRule:PRU00081}.
DISULFID 603 684 {ECO:0000255|PROSITE-ProRule:PRU00081}.
DISULFID 1725 1751 {ECO:0000305}.
DISULFID 1907 2061 {ECO:0000255|PROSITE-ProRule:PRU00081}.
DISULFID 2066 2221 {ECO:0000255|PROSITE-ProRule:PRU00081}.
VARIANT 15 15 G -> S (in dbSNP:rs9332485).
{ECO:0000269|Ref.3}.
/FTId=VAR_021297.
VARIANT 107 107 D -> H (in dbSNP:rs6019).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.3}.
/FTId=VAR_013886.
VARIANT 334 334 R -> G (in Hong Kong; does not predispose
to clinical thrombosis;
dbSNP:rs118203905).
{ECO:0000269|PubMed:9454741,
ECO:0000269|PubMed:9746807}.
/FTId=VAR_013620.
VARIANT 334 334 R -> T (in THPH2; Cambridge;
dbSNP:rs118203906).
{ECO:0000269|PubMed:9454742}.
/FTId=VAR_013621.
VARIANT 387 387 I -> T (in THPH2; Liverpool; mutant
protein is expressed with an additional
carbohydrate chain; dbSNP:rs118203911).
{ECO:0000269|PubMed:14617013,
ECO:0000269|PubMed:14695241}.
/FTId=VAR_032698.
VARIANT 413 413 M -> T (in dbSNP:rs6033).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.3}.
/FTId=VAR_013887.
VARIANT 513 513 R -> K (in dbSNP:rs6020).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:9454741,
ECO:0000269|Ref.3}.
/FTId=VAR_013622.
VARIANT 534 534 R -> Q (in THPH2; factor V Leiden;
associated with susceptibility to Budd-
Chiari syndrome; associated with
susceptibility to ischemic stroke;
dbSNP:rs6025).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10942390,
ECO:0000269|PubMed:16710414,
ECO:0000269|PubMed:8164741,
ECO:0000269|Ref.3}.
/FTId=VAR_001213.
VARIANT 613 613 C -> R (in THPH2; Nijkerk).
{ECO:0000269|PubMed:11435304}.
/FTId=VAR_032699.
VARIANT 775 775 S -> A (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035817.
VARIANT 781 781 S -> R (in dbSNP:rs13306350).
/FTId=VAR_047740.
VARIANT 809 809 P -> S (in dbSNP:rs6031).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.3}.
/FTId=VAR_013888.
VARIANT 817 817 N -> T (in dbSNP:rs6018).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.3}.
/FTId=VAR_013889.
VARIANT 858 858 K -> R (in dbSNP:rs4524).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:11758222,
ECO:0000269|PubMed:2827731,
ECO:0000269|PubMed:3110773,
ECO:0000269|Ref.3}.
/FTId=VAR_001214.
VARIANT 865 865 H -> R (in dbSNP:rs4525).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:11758222,
ECO:0000269|PubMed:2827731,
ECO:0000269|PubMed:3110773,
ECO:0000269|Ref.3}.
/FTId=VAR_001215.
VARIANT 915 915 T -> S (in dbSNP:rs9332695).
{ECO:0000269|Ref.3}.
/FTId=VAR_021298.
VARIANT 925 925 K -> E (in dbSNP:rs6032).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:11758222,
ECO:0000269|PubMed:2827731,
ECO:0000269|PubMed:3110773,
ECO:0000269|Ref.3}.
/FTId=VAR_013890.
VARIANT 969 969 N -> S (in dbSNP:rs9332604).
{ECO:0000269|Ref.3}.
/FTId=VAR_021299.
VARIANT 980 980 R -> L (in dbSNP:rs9332605).
{ECO:0000269|Ref.3}.
/FTId=VAR_021300.
VARIANT 1146 1146 H -> Q (in dbSNP:rs6005).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.3}.
/FTId=VAR_013891.
VARIANT 1285 1285 L -> I (in dbSNP:rs1046712).
{ECO:0000269|PubMed:2827731,
ECO:0000269|PubMed:8713778,
ECO:0000269|Ref.3}.
/FTId=VAR_013892.
VARIANT 1327 1327 H -> R (in dbSNP:rs1800595).
{ECO:0000269|PubMed:10942390,
ECO:0000269|PubMed:8713778}.
/FTId=VAR_013893.
VARIANT 1397 1397 L -> F (in dbSNP:rs13306334).
{ECO:0000269|PubMed:11758222,
ECO:0000269|PubMed:3110773}.
/FTId=VAR_047741.
VARIANT 1404 1404 P -> S (in dbSNP:rs9332608).
{ECO:0000269|Ref.3}.
/FTId=VAR_021301.
VARIANT 1530 1530 E -> A (in dbSNP:rs6007).
{ECO:0000269|PubMed:10391209,
ECO:0000269|Ref.3}.
/FTId=VAR_013894.
VARIANT 1685 1685 T -> S (in dbSNP:rs6011).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013895.
VARIANT 1730 1730 Y -> C (in FA5D; Seoul 2;
dbSNP:rs118203907).
{ECO:0000269|PubMed:10942390,
ECO:0000269|PubMed:11435304}.
/FTId=VAR_032700.
VARIANT 1749 1749 L -> V (in dbSNP:rs6034).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013896.
VARIANT 1764 1764 M -> V (in dbSNP:rs6030).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:3110773,
ECO:0000269|PubMed:7874144}.
/FTId=VAR_013897.
VARIANT 1820 1820 M -> I (in dbSNP:rs6026).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013898.
VARIANT 2102 2102 R -> C (in FA5D; impairs both factor V
secretion and activity;
dbSNP:rs118203910).
{ECO:0000269|PubMed:12393490}.
/FTId=VAR_032701.
VARIANT 2102 2102 R -> H (in THPH2).
{ECO:0000269|PubMed:11858490}.
/FTId=VAR_017329.
VARIANT 2148 2148 M -> T (in dbSNP:rs9332701).
{ECO:0000269|Ref.3}.
/FTId=VAR_021302.
VARIANT 2185 2185 K -> R (in dbSNP:rs6679078).
/FTId=VAR_034603.
VARIANT 2222 2222 D -> G (in dbSNP:rs6027).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013899.
CONFLICT 741 741 N -> S (in Ref. 7; ABD23003).
{ECO:0000305}.
CONFLICT 908 908 E -> K (in Ref. 1; AAA52424 and 8;
CAC82573). {ECO:0000305}.
CONFLICT 991 991 K -> E (in Ref. 5; BAF84302).
{ECO:0000305}.
CONFLICT 2213 2213 A -> T (in Ref. 1; AAA52424).
{ECO:0000305}.
TURN 1569 1571 {ECO:0000244|PDB:3S9C}.
TURN 2072 2074 {ECO:0000244|PDB:1CZT}.
STRAND 2075 2077 {ECO:0000244|PDB:1CZV}.
HELIX 2079 2081 {ECO:0000244|PDB:1CZT}.
STRAND 2082 2085 {ECO:0000244|PDB:1CZT}.
STRAND 2093 2095 {ECO:0000244|PDB:1CZV}.
HELIX 2098 2100 {ECO:0000244|PDB:1CZT}.
STRAND 2107 2109 {ECO:0000244|PDB:1CZT}.
STRAND 2111 2113 {ECO:0000244|PDB:1CZT}.
STRAND 2123 2139 {ECO:0000244|PDB:1CZT}.
STRAND 2141 2143 {ECO:0000244|PDB:1CZT}.
STRAND 2146 2163 {ECO:0000244|PDB:1CZT}.
STRAND 2182 2185 {ECO:0000244|PDB:1CZT}.
STRAND 2188 2211 {ECO:0000244|PDB:1CZT}.
STRAND 2213 2222 {ECO:0000244|PDB:1CZT}.
SEQUENCE 2224 AA; 251703 MW; 24AEF3FEA7332E37 CRC64;
MFPGCPRLWV LVVLGTSWVG WGSQGTEAAQ LRQFYVAAQG ISWSYRPEPT NSSLNLSVTS
FKKIVYREYE PYFKKEKPQS TISGLLGPTL YAEVGDIIKV HFKNKADKPL SIHPQGIRYS
KLSEGASYLD HTFPAEKMDD AVAPGREYTY EWSISEDSGP THDDPPCLTH IYYSHENLIE
DFNSGLIGPL LICKKGTLTE GGTQKTFDKQ IVLLFAVFDE SKSWSQSSSL MYTVNGYVNG
TMPDITVCAH DHISWHLLGM SSGPELFSIH FNGQVLEQNH HKVSAITLVS ATSTTANMTV
GPEGKWIISS LTPKHLQAGM QAYIDIKNCP KKTRNLKKIT REQRRHMKRW EYFIAAEEVI
WDYAPVIPAN MDKKYRSQHL DNFSNQIGKH YKKVMYTQYE DESFTKHTVN PNMKEDGILG
PIIRAQVRDT LKIVFKNMAS RPYSIYPHGV TFSPYEDEVN SSFTSGRNNT MIRAVQPGET
YTYKWNILEF DEPTENDAQC LTRPYYSDVD IMRDIASGLI GLLLICKSRS LDRRGIQRAA
DIEQQAVFAV FDENKSWYLE DNINKFCENP DEVKRDDPKF YESNIMSTIN GYVPESITTL
GFCFDDTVQW HFCSVGTQNE ILTIHFTGHS FIYGKRHEDT LTLFPMRGES VTVTMDNVGT
WMLTSMNSSP RSKKLRLKFR DVKCIPDDDE DSYEIFEPPE STVMATRKMH DRLEPEDEES
DADYDYQNRL AAALGIRSFR NSSLNQEEEE FNLTALALEN GTEFVSSNTD IIVGSNYSSP
SNISKFTVNN LAEPQKAPSH QQATTAGSPL RHLIGKNSVL NSSTAEHSSP YSEDPIEDPL
QPDVTGIRLL SLGAGEFKSQ EHAKHKGPKV ERDQAAKHRF SWMKLLAHKV GRHLSQDTGS
PSGMRPWEDL PSQDTGSPSR MRPWKDPPSD LLLLKQSNSS KILVGRWHLA SEKGSYEIIQ
DTDEDTAVNN WLISPQNASR AWGESTPLAN KPGKQSGHPK FPRVRHKSLQ VRQDGGKSRL
KKSQFLIKTR KKKKEKHTHH APLSPRTFHP LRSEAYNTFS ERRLKHSLVL HKSNETSLPT
DLNQTLPSMD FGWIASLPDH NQNSSNDTGQ ASCPPGLYQT VPPEEHYQTF PIQDPDQMHS
TSDPSHRSSS PELSEMLEYD RSHKSFPTDI SQMSPSSEHE VWQTVISPDL SQVTLSPELS
QTNLSPDLSH TTLSPELIQR NLSPALGQMP ISPDLSHTTL SPDLSHTTLS LDLSQTNLSP
ELSQTNLSPA LGQMPLSPDL SHTTLSLDFS QTNLSPELSH MTLSPELSQT NLSPALGQMP
ISPDLSHTTL SLDFSQTNLS PELSQTNLSP ALGQMPLSPD PSHTTLSLDL SQTNLSPELS
QTNLSPDLSE MPLFADLSQI PLTPDLDQMT LSPDLGETDL SPNFGQMSLS PDLSQVTLSP
DISDTTLLPD LSQISPPPDL DQIFYPSESS QSLLLQEFNE SFPYPDLGQM PSPSSPTLND
TFLSKEFNPL VIVGLSKDGT DYIEIIPKEE VQSSEDDYAE IDYVPYDDPY KTDVRTNINS
SRDPDNIAAW YLRSNNGNRR NYYIAAEEIS WDYSEFVQRE TDIEDSDDIP EDTTYKKVVF
RKYLDSTFTK RDPRGEYEEH LGILGPIIRA EVDDVIQVRF KNLASRPYSL HAHGLSYEKS
SEGKTYEDDS PEWFKEDNAV QPNSSYTYVW HATERSGPES PGSACRAWAY YSAVNPEKDI
HSGLIGPLLI CQKGILHKDS NMPMDMREFV LLFMTFDEKK SWYYEKKSRS SWRLTSSEMK
KSHEFHAING MIYSLPGLKM YEQEWVRLHL LNIGGSQDIH VVHFHGQTLL ENGNKQHQLG
VWPLLPGSFK TLEMKASKPG WWLLNTEVGE NQRAGMQTPF LIMDRDCRMP MGLSTGIISD
SQIKASEFLG YWEPRLARLN NGGSYNAWSV EKLAAEFASK PWIQVDMQKE VIITGIQTQG
AKHYLKSCYT TEFYVAYSSN QINWQIFKGN STRNVMYFNG NSDASTIKEN QFDPPIVARY
IRISPTRAYN RPTLRLELQG CEVNGCSTPL GMENGKIENK QITASSFKKS WWGDYWEPFR
ARLNAQGRVN AWQAKANNNK QWLEIDLLKI KKITAIITQG CKSLSSEMYV KSYTIHYSEQ
GVEWKPYRLK SSMVDKIFEG NTNTKGHVKN FFNPPIISRF IRVIPKTWNQ SIALRLELFG
CDIY


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