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Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide]

 PROC_HUMAN              Reviewed;         461 AA.
P04070; B4DPQ7; Q15189; Q15190; Q16001; Q53S74; Q9UC55;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1986, sequence version 1.
23-FEB-2022, entry version 258.
RecName: Full=Vitamin K-dependent protein C;
EC=3.4.21.69;
AltName: Full=Anticoagulant protein C;
AltName: Full=Autoprothrombin IIA;
AltName: Full=Blood coagulation factor XIV;
Contains:
RecName: Full=Vitamin K-dependent protein C light chain;
Contains:
RecName: Full=Vitamin K-dependent protein C heavy chain;
Contains:
RecName: Full=Activation peptide;
Flags: Precursor;
Name=PROC;
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).
PubMed=2991859; DOI=10.1093/nar/13.14.5233;
Beckmann R.J., Schmidt R.J., Santerre R.F., Plutzky J., Crabtree G.R.,
Long G.L.;
"The structure and evolution of a 461 amino acid human protein C precursor
and its messenger RNA, based upon the DNA sequence of cloned human liver
cDNAs.";
Nucleic Acids Res. 13:5233-5247(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], HYDROXYLATION AT ASP-113, GLYCOSYLATION
AT ASN-290; ASN-355 AND ASN-371, AND GAMMA-CARBOXYGLUTAMATION AT GLU-48;
GLU-49; GLU-56; GLU-58; GLU-61; GLU-62; GLU-67; GLU-68 AND GLU-71.
PubMed=2991887; DOI=10.1073/pnas.82.14.4673;
Foster D.C., Yoshitake S., Davie E.W.;
"The nucleotide sequence of the gene for human protein C.";
Proc. Natl. Acad. Sci. U.S.A. 82:4673-4677(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3511471; DOI=10.1073/pnas.83.3.546;
Plutzky J., Hoskins J.A., Long G.L., Crabtree G.R.;
"Evolution and organization of the human protein C gene.";
Proc. Natl. Acad. Sci. U.S.A. 83:546-550(1986).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
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).
[9]
PROTEIN SEQUENCE OF 42-57, AND VARIANT THPH3 SER-42.
TISSUE=Blood;
PubMed=8560401;
Miyata T., Zheng Y.-Z., Sakata T., Kato H.;
"Protein C Osaka 10 with aberrant propeptide processing: loss of
anticoagulant activity due to an amino acid substitution in the protein C
precursor.";
Thromb. Haemost. 74:1003-1008(1995).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-64, AND VARIANT PROC DEFICIENCY
GLY-57.
PubMed=8477066;
Mimuro J., Muramatsu S., Kaneko M., Yoshitake S., Iijima K., Nakamura K.,
Sakata Y., Matsuda M.;
"An abnormal protein C (protein C Yonago) with an amino acid substitution
of Gly for Arg-15 caused by a single base mutation of C to G in codon 57
(CGG-->GGG). Deteriorated calcium-dependent conformation of the gamma-
carboxyglutamic acid domain relevant to a thrombotic tendency.";
Int. J. Hematol. 57:9-14(1993).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 106-461 (ISOFORM 1).
PubMed=6589623; DOI=10.1073/pnas.81.15.4766;
Foster D.C., Davie E.W.;
"Characterization of a cDNA coding for human protein C.";
Proc. Natl. Acad. Sci. U.S.A. 81:4766-4770(1984).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-178 AND 267-332, AND VARIANTS
THPH4 PRO-178 AND HIS-328.
PubMed=7878626;
Long G.L., Tomczak J.A., Rainville I.R., Dreyfus M., Schramm W.,
Schwarz H.P.;
"Homozygous type I protein C deficiency in two unrelated families
exhibiting thrombophilia related to Ala136-->Pro or Arg286-->His
mutations.";
Thromb. Haemost. 72:526-533(1994).
[13]
GLYCOSYLATION AT ASN-371.
PubMed=1694179;
Miletich J.P., Broze G.J. Jr.;
"Beta protein C is not glycosylated at asparagine 329. The rate of
translation may influence the frequency of usage at asparagine-X-cysteine
sites.";
J. Biol. Chem. 265:11397-11404(1990).
[14]
HYDROXYLATION.
PubMed=1544894;
Harris R.J., Ling V.T., Spellman M.W.;
"O-linked fucose is present in the first epidermal growth factor domain of
factor XII but not protein C.";
J. Biol. Chem. 267:5102-5107(1992).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-290.
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).
[16]
GLYCOSYLATION AT THR-19, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.m111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of N- and
O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 11:1-17(2012).
[17]
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).
[18]
PHOSPHORYLATION AT SER-347.
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).
[19]
3D-STRUCTURE MODELING OF 175-450.
PubMed=8003977; DOI=10.1002/pro.5560030407;
Fisher C.L., Greengard J.S., Griffin J.H.;
"Models of the serine protease domain of the human antithrombotic plasma
factor activated protein C and its zymogen.";
Protein Sci. 3:588-599(1994).
[20]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 84-461.
PubMed=9003757; DOI=10.1002/j.1460-2075.1996.tb01073.x;
Mather T., Oganessyan V., Hof P., Huber R., Foundling S., Esmon C.,
Bode W.;
"The 2.8 A crystal structure of Gla-domainless activated protein C.";
EMBO J. 15:6822-6831(1996).
[21]
REVIEW ON PROC VARIANTS.
PubMed=8446940;
Reitsma P.H., Poort S.R., Bernardi F., Gandrille S., Long G.L., Sala N.,
Cooper D.N.;
"Protein C deficiency: a database of mutations.";
Thromb. Haemost. 69:77-84(1993).
[22]
VARIANT THPH3 CYS-444.
PubMed=2437584; DOI=10.1073/pnas.84.9.2829;
Romeo G., Hassan H.J., Staempfli S., Roncuzzi L., Cianetti L., Leonardi A.,
Vicente V., Mannucci P.M., Bertina R.M., Peschle C., Cortese R.;
"Hereditary thrombophilia: identification of nonsense and missense
mutations in the protein C gene.";
Proc. Natl. Acad. Sci. U.S.A. 84:2829-2832(1987).
[23]
VARIANT THPH3 TRP-211.
PubMed=2602169; DOI=10.1093/nar/17.24.10513;
Grundy C.B., Chitolie A., Talbot S., Bevan D., Kakkar V.V., Cooper D.N.;
"Protein C London 1: recurrent mutation at Arg-169 (CGG-->TGG) in the
protein C gene causing thrombosis.";
Nucleic Acids Res. 17:10513-10513(1989).
[24]
VARIANT THPH3 CYS-272.
PubMed=1868249;
Reitsma P.H., Poort S.R., Allaart C.F., Briet E., Bertina R.M.;
"The spectrum of genetic defects in a panel of 40 Dutch families with
symptomatic protein C deficiency type I: heterogeneity and founder
effects.";
Blood 78:890-894(1991).
[25]
VARIANTS THPH3 ALA-62 AND MET-76.
PubMed=1347706;
Bovill E.G., Tomczak J.A., Grant B., Bhushan F., Pillemer E.,
Rainville I.R., Long G.L.;
"Protein CVermont: symptomatic type II protein C deficiency associated with
two GLA domain mutations.";
Blood 79:1456-1465(1992).
[26]
VARIANT THPH4 ASP-418.
PubMed=1611081;
Sugahara Y., Miura O., Yuen P., Aoki N.;
"Protein C deficiency Hong Kong 1 and 2: hereditary protein C deficiency
caused by two mutant alleles, a 5-nucleotide deletion and a missense
mutation.";
Blood 80:126-133(1992).
[27]
VARIANT THPH4 LEU-289.
PubMed=1511988; DOI=10.1007/bf00221963;
Grundy C.B., Chisholm M., Kakkar V.V., Cooper D.N.;
"A novel homozygous missense mutation in the protein C (PROC) gene causing
recurrent venous thrombosis.";
Hum. Genet. 89:683-684(1992).
[28]
VARIANTS THPH3 GLN-220 AND TRP-220.
PubMed=1511989; DOI=10.1007/bf00221964;
Grundy C.B., Schulman S., Tengborn L., Kakkar V.V., Cooper D.N.;
"Two different missense mutations at Arg 178 of the protein C (PROC) gene
causing recurrent venous thrombosis.";
Hum. Genet. 89:685-686(1992).
[29]
VARIANT THPH3 GLN-220.
PubMed=1301959; DOI=10.1002/humu.1380010607;
Gandrille S., Vidaud M., Aiach M., Alhenc-Gelas M., Fischer A.M.,
Gouault-Heilman M., Toulon P., Fiessinger J.-N., Goossens M.;
"Two novel mutations responsible for hereditary type I protein C
deficiency: characterization by denaturing gradient gel electrophoresis.";
Hum. Mutat. 1:491-500(1992).
[30]
VARIANT THPH4 SER-334.
PubMed=1593215;
Yamamoto K., Matsushita T., Sugiura I., Takamatsu J., Iwasaki E., Wada H.,
Deguchi K., Shirakawa S., Saito H.;
"Homozygous protein C deficiency: identification of a novel missense
mutation that causes impaired secretion of the mutant protein C.";
J. Lab. Clin. Med. 119:682-689(1992).
[31]
VARIANTS TRP-38; CYS-42; HIS-42; GLN-271 AND ASN-294.
PubMed=8324221;
Gandrille S., Alhenc-Gelas M., Gaussem P., Aillaud M.-F., Dupuy E.,
Juhan-Vague I., Aiach M.;
"Five novel mutations located in exons III and IX of the protein C gene in
patients presenting with defective protein C anticoagulant activity.";
Blood 82:159-168(1993).
[32]
VARIANTS GLY-14; GLN-211; TYR-244; GLN-253; LEU-321; CYS-328; ILE-385;
THR-388 AND VAL-388.
PubMed=8499565; DOI=10.1097/00001721-199304000-00009;
Poort S.R., Pabinger-Fasching I., Mannhalter C., Reitsma P.H.,
Bertina R.M.;
"Twelve novel and two recurrent mutations in 14 Austrian families with
hereditary protein C deficiency.";
Blood Coagul. Fibrinolysis 4:273-280(1993).
[33]
VARIANT THPH3 TRP-57.
PubMed=8499568; DOI=10.1097/00001721-199304000-00014;
Millar D.S., Grundy C.B., Bignell P., Moffat E.H., Martin R., Kakkar V.V.,
Cooper D.N.;
"A Gla domain mutation (Arg 15-->Trp) in the protein C (PROC) gene causing
type 2 protein C deficiency and recurrent venous thrombosis.";
Blood Coagul. Fibrinolysis 4:345-347(1993).
[34]
VARIANTS THPH3 ARG-145; LEU-210; TRP-211; THR-243; LEU-321; MET-340 AND
TYR-426.
PubMed=8292730;
Tsay W., Greengard J.S., Montgomery R.R., McPherson R.A., Fucci J.C.,
Koerper M.A., Coughlin J., Griffin J.H.;
"Genetic mutations in ten unrelated American patients with symptomatic type
1 protein C deficiency.";
Blood Coagul. Fibrinolysis 4:791-796(1993).
[35]
VARIANT THPH3 SER-423.
PubMed=8398832; DOI=10.1111/j.1365-2141.1993.tb03066.x;
Marchetti G., Patracchini P., Gemmati D., Castaman G., Rodeghiero F.,
Wacey A., Cooper D.N., Tuddenham E.G., Bernardi F.;
"Symptomatic type II protein C deficiency caused by a missense mutation
(Gly 381-->Ser) in the substrate-binding pocket.";
Br. J. Haematol. 84:285-289(1993).
[36]
VARIANT PRO-312.
PubMed=7919373;
Gandrille S., Jude B., Alhenc-Gelas M., Emmerich J., Aiach M.;
"First de novo mutations in the protein C gene of two patients with type I
deficiency: a missense mutation and a splice site deletion.";
Blood 84:2566-2570(1994).
[37]
VARIANT THPH4 144-ASN-GLY-145 DELINS LYS.
PubMed=7841323;
Millar D.S., Allgrove J., Rodeck C., Kakkar V.V., Cooper D.N.;
"A homozygous deletion/insertion mutation in the protein C (PROC) gene
causing neonatal Purpura fulminans: prenatal diagnosis in an at-risk
pregnancy.";
Blood Coagul. Fibrinolysis 5:647-649(1994).
[38]
VARIANT THPH4 ALA-367.
PubMed=7841324;
Witt I., Beck S., Seydewitz H.H., Tasangil C., Schenck W.;
"A novel homozygous missense mutation (Val 325-->Ala) in the protein C gene
causing neonatal purpura fulminans.";
Blood Coagul. Fibrinolysis 5:651-653(1994).
[39]
VARIANTS THPH3 LEU-369; ARG-392; ASN-401 AND HIS-441.
PubMed=7865674; DOI=10.1097/00001721-199410000-00003;
Zheng Y.-Z., Sakata T., Matsusue T., Umeyama H., Kato H., Miyata T.;
"Six missense mutations associated with type I and type II protein C
deficiency and implications obtained from molecular modelling.";
Blood Coagul. Fibrinolysis 5:687-696(1994).
[40]
VARIANT ASP-49.
PubMed=7974343;
Gaussem P., Gandrille S., Duchemin J., Emmerich J., Alhenc-Gelas M.,
Aillaud M.-F., Aiach M.;
"Influence of six mutations of the protein C gene on the Gla domain
conformation and calcium affinity.";
Thromb. Haemost. 71:748-754(1994).
[41]
VARIANTS CYS-89; PRO-220 AND THR-301.
PubMed=7605880; DOI=10.1097/00001721-199504000-00009;
Millar D.S., Bevan D., Chitolie A., Reynaud J., Chisholm M., Kakkar V.V.,
Cooper D.N.;
"Three novel mutations in the protein C (PROC) gene causing venous
thrombosis.";
Blood Coagul. Fibrinolysis 6:138-140(1995).
[42]
VARIANTS THPH3 TRP-57; ARG-114; ARG-324; CYS-328 AND LEU-369, AND VARIANT
THR-43.
PubMed=7792728;
Lind B., Schwartz M., Thorsen S.;
"Six different point mutations in seven Danish families with symptomatic
protein C deficiency.";
Thromb. Haemost. 73:186-193(1995).
[43]
VARIANTS THPH3 CYS-32 AND ASN-436.
PubMed=8829639;
DOI=10.1002/(sici)1098-1004(1996)7:2<176::aid-humu16>3.0.co;2-#;
Ireland H.A., Boisclair M.D., Taylor J., Thompson E., Thein S.L.,
Girolami A., de Caterina M., Scopacasa F., de Stefano V., Leone G.,
Finazzi G., Cohen H., Lane D.A.;
"Two novel (R(-11)C; T394D) and two repeat missense mutations in the
protein C gene associated with venous thrombosis in six kindreds.";
Hum. Mutat. 7:176-179(1996).
[44]
VARIANTS THPH3 GLN-220 AND MET-340.
PubMed=9798967;
Couture P., Demers C., Morissette J., Delage R., Jomphe M., Couture L.,
Simard J.;
"Type I protein C deficiency in French Canadians: evidence of a founder
effect and association of specific protein C gene mutations with plasma
protein C levels.";
Thromb. Haemost. 80:551-556(1998).
[45]
VARIANT SER-317, CHARACTERIZATION OF SER-317, AND SUBCELLULAR LOCATION.
PubMed=22531345; DOI=10.1097/pat.0b013e328353a218;
Yu T., Dai J., Liu H., Wang J., Ding Q., Wang H., Wang X., Fu Q.;
"Homozygous protein C deficiency with late onset venous thrombosis:
identification and in vitro expression study of a novel Pro275Ser
mutation.";
Pathology 44:348-353(2012).
[46]
VARIANTS GLU-70; GLY-106; ALA-118; TYR-175; VAL-181; TRP-189; GLN-211;
TRP-220; ARG-223; GLY-240; HIS-297; LEU-312; VAL-327 AND LEU-420.
PubMed=22545135; DOI=10.1371/journal.pone.0035773;
Tang L., Guo T., Yang R., Mei H., Wang H., Lu X., Yu J., Wang Q., Hu Y.;
"Genetic background analysis of protein C deficiency demonstrates a
recurrent mutation associated with venous thrombosis in Chinese
population.";
PLoS ONE 7:E35773-E35773(2012).
[47]
VARIANT ALA-357, CHARACTERIZATION OF ALA-357, AND FUNCTION.
PubMed=25651845; DOI=10.1182/blood-2014-12-617274;
Ding Q., Yang L., Dinarvand P., Wang X., Rezaie A.R.;
"Protein C Thr315Ala variant results in gain of function but manifests as
type II deficiency in diagnostic assays.";
Blood 125:2428-2434(2015).
[48]
VARIANTS THPH3 HIS-297 AND LEU-420, CHARACTERIZATION OF VARIANTS THPH3
HIS-297 AND LEU-420, AND SUBCELLULAR LOCATION.
PubMed=25748729; DOI=10.1016/j.gene.2015.03.002;
Liu H., Wang H.F., Tang L., Yang Y., Wang Q.Y., Zeng W., Wu Y.Y.,
Cheng Z.P., Hu B., Guo T., Hu Y.;
"Compound heterozygous protein C deficiency in a family with venous
thrombosis: Identification and in vitro study of p.Asp297His and
p.Val420Leu mutations.";
Gene 563:35-40(2015).
[49]
VARIANTS THPH4 GLY-77 AND GLU-163, VARIANT THPH3 VAL-163, FUNCTION AS
ANTICOAGULANT, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS THPH4
GLY-77 AND GLU-163, AND CHARACTERIZATION OF VARIANT THPH3 VAL-163.
PubMed=25618265; DOI=10.1016/j.thromres.2015.01.011;
Kovacs K.B., Pataki I., Bardos H., Fekete A., Pfliegler G., Haramura G.,
Gindele R., Komaromi I., Balla G., Adany R., Muszbek L., Bereczky Z.;
"Molecular characterization of p.Asp77Gly and the novel p.Ala163Val and
p.Ala163Glu mutations causing protein C deficiency.";
Thromb. Res. 135:718-726(2015).
-!- FUNCTION: Protein C is a vitamin K-dependent serine protease that
regulates blood coagulation by inactivating factors Va and VIIIa in the
presence of calcium ions and phospholipids (PubMed:25618265). Exerts a
protective effect on the endothelial cell barrier function
(PubMed:25651845). {ECO:0000269|PubMed:25618265,
ECO:0000269|PubMed:25651845}.
-!- CATALYTIC ACTIVITY:
Reaction=Degradation of blood coagulation factors Va and VIIIa.;
EC=3.4.21.69;
-!- SUBUNIT: Synthesized as a single chain precursor, which is cleaved into
a light chain and a heavy chain held together by a disulfide bond. The
enzyme is then activated by thrombin, which cleaves a tetradecapeptide
from the amino end of the heavy chain; this reaction, which occurs at
the surface of endothelial cells, is strongly promoted by
thrombomodulin.
-!- INTERACTION:
P04070; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1383018, EBI-3867333;
P04070; P51511: MMP15; NbExp=2; IntAct=EBI-1383018, EBI-1383043;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25618265}. Golgi
apparatus {ECO:0000269|PubMed:22531345, ECO:0000269|PubMed:25748729}.
Endoplasmic reticulum {ECO:0000269|PubMed:22531345,
ECO:0000269|PubMed:25748729}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P04070-1; Sequence=Displayed;
Name=2;
IsoId=P04070-2; Sequence=VSP_054393, VSP_054394;
-!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
-!- PTM: The vitamin K-dependent, enzymatic carboxylation of some Glu
residues allows the modified protein to bind calcium.
-!- PTM: N- and O-glycosylated. Partial (70%) N-glycosylation of Asn-371
with an atypical N-X-C site produces a higher molecular weight form
referred to as alpha. The lower molecular weight form, not N-
glycosylated at Asn-371, is beta. O-glycosylated with core 1 or
possibly core 8 glycans. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:1694179, ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:2991887}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
and asparagine is (R) stereospecific within EGF domains.
{ECO:0000269|PubMed:1544894, ECO:0000269|PubMed:2991887}.
-!- PTM: May be phosphorylated on a Ser or Thr in a region (AA 25-30) of
the propeptide.
-!- DISEASE: Thrombophilia due to protein C deficiency, autosomal dominant
(THPH3) [MIM:176860]: A hemostatic disorder characterized by impaired
regulation of blood coagulation and a tendency to recurrent venous
thrombosis. Individuals with decreased amounts of protein C are
classically referred to as having type I protein C deficiency and those
with normal amounts of a functionally defective protein as having type
II deficiency. {ECO:0000269|PubMed:1301959, ECO:0000269|PubMed:1347706,
ECO:0000269|PubMed:1511989, ECO:0000269|PubMed:1868249,
ECO:0000269|PubMed:2437584, ECO:0000269|PubMed:25618265,
ECO:0000269|PubMed:25748729, ECO:0000269|PubMed:2602169,
ECO:0000269|PubMed:7792728, ECO:0000269|PubMed:7865674,
ECO:0000269|PubMed:8292730, ECO:0000269|PubMed:8398832,
ECO:0000269|PubMed:8499568, ECO:0000269|PubMed:8560401,
ECO:0000269|PubMed:8829639, ECO:0000269|PubMed:9798967}. Note=The
disease is caused by variants affecting the gene represented in this
entry.
-!- DISEASE: Thrombophilia due to protein C deficiency, autosomal recessive
(THPH4) [MIM:612304]: A hemostatic disorder characterized by impaired
regulation of blood coagulation and a tendency to recurrent venous
thrombosis. It results in a thrombotic condition that can manifest as a
severe neonatal disorder or as a milder disorder with late-onset
thrombophilia. The severe form leads to neonatal death through massive
neonatal venous thrombosis. Often associated with ecchymotic skin
lesions which can turn necrotic called purpura fulminans, this disorder
is very rare. {ECO:0000269|PubMed:1511988, ECO:0000269|PubMed:1593215,
ECO:0000269|PubMed:1611081, ECO:0000269|PubMed:25618265,
ECO:0000269|PubMed:7841323, ECO:0000269|PubMed:7841324,
ECO:0000269|PubMed:7878626}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- MISCELLANEOUS: Calcium also binds, with stronger affinity to another
site, beyond the GLA domain. This GLA-independent binding site is
necessary for the recognition of the thrombin-thrombomodulin complex.
-!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
-!- SEQUENCE CAUTION:
Sequence=S76088; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Protein C entry;
URL="https://en.wikipedia.org/wiki/Protein_C";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/proc/";
---------------------------------------------------------------------------
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EMBL; X02750; CAA26528.1; -; mRNA.
EMBL; M11228; AAA60166.1; -; Genomic_DNA.
EMBL; M12712; AAA60165.1; -; Genomic_DNA.
EMBL; M12683; AAA60165.1; JOINED; Genomic_DNA.
EMBL; M12684; AAA60165.1; JOINED; Genomic_DNA.
EMBL; M12685; AAA60165.1; JOINED; Genomic_DNA.
EMBL; M12686; AAA60165.1; JOINED; Genomic_DNA.
EMBL; M12687; AAA60165.1; JOINED; Genomic_DNA.
EMBL; AF378903; AAK56377.1; -; Genomic_DNA.
EMBL; AK298454; BAG60669.1; -; mRNA.
EMBL; AC068282; AAY15044.1; -; Genomic_DNA.
EMBL; CH471103; EAW95320.1; -; Genomic_DNA.
EMBL; BC034377; AAH34377.1; -; mRNA.
EMBL; S58668; AAB26335.1; -; Genomic_DNA.
EMBL; K02059; AAA60164.1; -; mRNA.
EMBL; S76088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; S76090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS2145.1; -. [P04070-1]
PIR; A22331; KXHU.
RefSeq; NP_000303.1; NM_000312.3. [P04070-1]
PDB; 1AUT; X-ray; 2.80 A; C=212-461, L=84-197.
PDB; 1LQV; X-ray; 1.60 A; C/D=43-75.
PDB; 3F6U; X-ray; 2.80 A; H=212-451, L=91-188.
PDB; 3JTC; X-ray; 1.60 A; C/D=43-75.
PDB; 4DT7; X-ray; 1.90 A; E/F=204-223.
PDB; 6M3B; X-ray; 2.20 A; A=212-461, D=43-197.
PDB; 6M3C; X-ray; 3.70 A; A/C/G=212-461, B/D/I=43-197.
PDBsum; 1AUT; -.
PDBsum; 1LQV; -.
PDBsum; 3F6U; -.
PDBsum; 3JTC; -.
PDBsum; 4DT7; -.
PDBsum; 6M3B; -.
PDBsum; 6M3C; -.
SASBDB; P04070; -.
SMR; P04070; -.
BioGRID; 111608; 14.
ComplexPortal; CPX-6224; Active Protein C complex.
ELM; P04070; -.
IntAct; P04070; 11.
MINT; P04070; -.
STRING; 9606.ENSP00000234071; -.
BindingDB; P04070; -.
ChEMBL; CHEMBL4444; -.
DrugBank; DB13192; Antihemophilic factor human.
DrugBank; DB00025; Antihemophilic factor, human recombinant.
DrugBank; DB09131; Cupric Chloride.
DrugBank; DB09332; Kappadione.
DrugBank; DB13998; Lonoctocog alfa.
DrugBank; DB00170; Menadione.
DrugBank; DB13999; Moroctocog alfa.
DrugBank; DB13149; Protein S human.
DrugBank; DB00464; Sodium tetradecyl sulfate.
DrugBank; DB14738; Turoctocog alfa pegol.
DrugCentral; P04070; -.
GuidetoPHARMACOLOGY; 2396; -.
MEROPS; S01.218; -.
GlyConnect; 620; 17 N-Linked glycans (2 sites), 1 O-Linked glycan (1 site).
GlyGen; P04070; 7 sites, 43 N-linked glycans (5 sites), 2 O-linked glycans (2 sites).
iPTMnet; P04070; -.
PhosphoSitePlus; P04070; -.
BioMuta; PROC; -.
DMDM; 131067; -.
jPOST; P04070; -.
MassIVE; P04070; -.
MaxQB; P04070; -.
PaxDb; P04070; -.
PeptideAtlas; P04070; -.
PRIDE; P04070; -.
ProteomicsDB; 4804; -.
ProteomicsDB; 51646; -. [P04070-1]
ABCD; P04070; 2 sequenced antibodies.
Antibodypedia; 791; 725 antibodies from 41 providers.
DNASU; 5624; -.
Ensembl; ENST00000234071; ENSP00000234071; ENSG00000115718.
GeneID; 5624; -.
KEGG; hsa:5624; -.
MANE-Select; ENST00000234071.8; ENSP00000234071.4; NM_000312.4; NP_000303.1.
UCSC; uc002tok.4; human. [P04070-1]
CTD; 5624; -.
DisGeNET; 5624; -.
GeneCards; PROC; -.
HGNC; HGNC:9451; PROC.
HPA; ENSG00000115718; Tissue enriched (liver).
MalaCards; PROC; -.
MIM; 176860; phenotype.
MIM; 612283; gene.
MIM; 612304; phenotype.
neXtProt; NX_P04070; -.
OpenTargets; ENSG00000115718; -.
Orphanet; 64738; NON RARE IN EUROPE: Non rare thrombophilia.
Orphanet; 745; Severe hereditary thrombophilia due to congenital protein C deficiency.
PharmGKB; PA33799; -.
VEuPathDB; HostDB:ENSG00000115718; -.
eggNOG; ENOG502QQ3W; Eukaryota.
GeneTree; ENSGT00940000154505; -.
HOGENOM; CLU_006842_19_5_1; -.
InParanoid; P04070; -.
OrthoDB; 1314811at2759; -.
PhylomeDB; P04070; -.
TreeFam; TF327329; -.
BRENDA; 3.4.21.69; 2681.
PathwayCommons; P04070; -.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-140875; Common 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.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
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-8957275; Post-translational protein phosphorylation.
SABIO-RK; P04070; -.
SignaLink; P04070; -.
SIGNOR; P04070; -.
BioGRID-ORCS; 5624; 1 hit in 1035 CRISPR screens.
ChiTaRS; PROC; human.
EvolutionaryTrace; P04070; -.
GeneWiki; Protein_C; -.
GenomeRNAi; 5624; -.
Pharos; P04070; Tchem.
PRO; PR:P04070; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; P04070; protein.
Bgee; ENSG00000115718; Expressed in right lobe of liver and 118 other tissues.
ExpressionAtlas; P04070; baseline and differential.
Genevisible; P04070; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:ComplexPortal.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0030195; P:negative regulation of blood coagulation; IDA:ComplexPortal.
GO; GO:0050819; P:negative regulation of coagulation; IMP:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; IMP:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 2.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
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; Direct protein sequencing;
Disease variant; Disulfide bond; EGF-like domain; Endoplasmic reticulum;
Gamma-carboxyglutamic acid; Glycoprotein; Golgi apparatus; Hemostasis;
Hydrolase; Hydroxylation; Phosphoprotein; Protease; Reference proteome;
Repeat; Secreted; Serine protease; Signal; Thrombophilia; Zymogen.
SIGNAL 1..18
/evidence="ECO:0000255"
PROPEP 19..42
/id="PRO_0000028107"
CHAIN 43..461
/note="Vitamin K-dependent protein C"
/id="PRO_0000028108"
CHAIN 43..197
/note="Vitamin K-dependent protein C light chain"
/id="PRO_0000028109"
CHAIN 200..461
/note="Vitamin K-dependent protein C heavy chain"
/id="PRO_0000028110"
PEPTIDE 200..211
/note="Activation peptide"
/id="PRO_0000028111"
DOMAIN 43..88
/note="Gla"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
DOMAIN 97..132
/note="EGF-like 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 136..176
/note="EGF-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 212..450
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
ACT_SITE 253
/note="Charge relay system"
ACT_SITE 299
/note="Charge relay system"
ACT_SITE 402
/note="Charge relay system"
SITE 211..212
/note="Cleavage; by thrombin"
MOD_RES 48
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2991887"
MOD_RES 49
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2991887"
MOD_RES 56
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2991887"
MOD_RES 58
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2991887"
MOD_RES 61
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2991887"
MOD_RES 62
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2991887"
MOD_RES 67
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2991887"
MOD_RES 68
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2991887"
MOD_RES 71
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:2991887"
MOD_RES 113
/note="(3R)-3-hydroxyaspartate"
/evidence="ECO:0000269|PubMed:2991887"
MOD_RES 347
/note="Phosphoserine; by FAM20C"
/evidence="ECO:0000269|PubMed:26091039"
CARBOHYD 19
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:22171320"
CARBOHYD 139
/note="N-linked (GlcNAc...) asparagine"
CARBOHYD 290
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:2991887"
CARBOHYD 355
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:2991887"
CARBOHYD 371
/note="N-linked (GlcNAc...) asparagine; atypical; partial"
/evidence="ECO:0000269|PubMed:1694179,
ECO:0000269|PubMed:2991887"
DISULFID 59..64
DISULFID 92..111
DISULFID 101..106
DISULFID 105..120
DISULFID 122..131
DISULFID 140..151
DISULFID 147..160
DISULFID 162..175
DISULFID 183..319
/note="Interchain (between light and heavy chains)"
DISULFID 238..254
DISULFID 373..387
DISULFID 398..426
VAR_SEQ 1
/note="M -> MAAGRRTCSISTTRPCASASRM (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_054393"
VAR_SEQ 133
/note="R -> RGEGERWMLAGGGAGLGPGWGRGTSTSCPRPPLPA (in isoform
2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_054394"
VARIANT 14
/note="W -> G (in patients with PROC deficiency)"
/evidence="ECO:0000269|PubMed:8499565"
/id="VAR_006634"
VARIANT 32
/note="R -> C (in THPH3)"
/evidence="ECO:0000269|PubMed:8829639"
/id="VAR_006635"
VARIANT 38
/note="R -> W (in patients with PROC deficiency;
dbSNP:rs769900251)"
/evidence="ECO:0000269|PubMed:8324221"
/id="VAR_006636"
VARIANT 42
/note="R -> C (in patients with PROC deficiency;
dbSNP:rs774572099)"
/evidence="ECO:0000269|PubMed:8324221"
/id="VAR_006638"
VARIANT 42
/note="R -> H (in Malakoff; low anticoagulant activity;
dbSNP:rs369504169)"
/evidence="ECO:0000269|PubMed:8324221"
/id="VAR_006637"
VARIANT 42
/note="R -> S (in THPH3; type II; Osaka-10; alters
proteolytic processing so that S-42 is the N-terminus of
the mature protein; dbSNP:rs774572099)"
/evidence="ECO:0000269|PubMed:8560401"
/id="VAR_055074"
VARIANT 43
/note="A -> T (in dbSNP:rs767626189)"
/evidence="ECO:0000269|PubMed:7792728"
/id="VAR_006639"
VARIANT 49
/note="E -> D (in patients with PROC deficiency)"
/evidence="ECO:0000269|PubMed:7974343"
/id="VAR_006640"
VARIANT 51
/note="R -> C (in patients with PROC deficiency;
dbSNP:rs764546127)"
/id="VAR_006641"
VARIANT 57
/note="R -> G (in Yonago; defective anticoagulant
activity)"
/evidence="ECO:0000269|PubMed:8477066"
/id="VAR_006643"
VARIANT 57
/note="R -> Q (in patients with PROC deficiency;
dbSNP:rs574949343)"
/id="VAR_006644"
VARIANT 57
/note="R -> W (in THPH3; dbSNP:rs757583846)"
/evidence="ECO:0000269|PubMed:7792728,
ECO:0000269|PubMed:8499568"
/id="VAR_006642"
VARIANT 62
/note="E -> A (in THPH3; Vermont-1; dbSNP:rs121918148)"
/evidence="ECO:0000269|PubMed:1347706"
/id="VAR_006645"
VARIANT 70
/note="K -> E (in patients with PROC deficiency;
dbSNP:rs199469481)"
/evidence="ECO:0000269|PubMed:22545135"
/id="VAR_074296"
VARIANT 76
/note="V -> M (in THPH3; Vermont-1; dbSNP:rs121918149)"
/evidence="ECO:0000269|PubMed:1347706"
/id="VAR_006646"
VARIANT 77
/note="D -> G (in THPH4; no effect on secretion; no effect
on catalytic activity in vitro)"
/evidence="ECO:0000269|PubMed:25618265"
/id="VAR_073145"
VARIANT 89
/note="G -> C (in patients with PROC deficiency)"
/evidence="ECO:0000269|PubMed:7605880"
/id="VAR_006647"
VARIANT 106
/note="C -> G (in patients with PROC deficiency;
dbSNP:rs199469479)"
/evidence="ECO:0000269|PubMed:22545135"
/id="VAR_074297"
VARIANT 108
/note="H -> N (in patients with PROC deficiency; La Jolla-
1; dbSNP:rs200234655)"
/id="VAR_006648"
VARIANT 109
/note="G -> R (in patients with PROC deficiency)"
/id="VAR_006649"
VARIANT 114..118
/note="Missing (in patients with PROC deficiency)"
/id="VAR_006650"
VARIANT 114
/note="G -> R (in THPH3; dbSNP:rs374476971)"
/evidence="ECO:0000269|PubMed:7792728"
/id="VAR_006651"
VARIANT 118
/note="F -> A (in patients with PROC deficiency; requires 2
nucleotide substitutions)"
/evidence="ECO:0000269|PubMed:22545135"
/id="VAR_074298"
VARIANT 118
/note="F -> L (in patients with PROC deficiency;
dbSNP:rs1553424043)"
/id="VAR_006652"
VARIANT 119..124
/note="Missing (in patients with PROC deficiency; St Louis-
2)"
/id="VAR_006653"
VARIANT 120..125
/note="Missing (in patients with PROC deficiency; St Louis-
3)"
/id="VAR_006654"
VARIANT 144..145
/note="NG -> K (in THPH4; neonatal purpura fulminans)"
/evidence="ECO:0000269|PubMed:7841323"
/id="VAR_006655"
VARIANT 145
/note="G -> R (in THPH3; dbSNP:rs370813536)"
/evidence="ECO:0000269|PubMed:8292730"
/id="VAR_006656"
VARIANT 147
/note="C -> Y (in patients with PROC deficiency;
dbSNP:rs1247269491)"
/id="VAR_006657"
VARIANT 149
/note="H -> P (in patients with PROC deficiency;
dbSNP:rs121918159)"
/id="VAR_006658"
VARIANT 161
/note="S -> R (in patients with PROC deficiency;
dbSNP:rs1433503391)"
/id="VAR_006659"
VARIANT 163
/note="A -> E (in THPH4; drastically reduced secretion;
colocalizes with 26S proteasome)"
/evidence="ECO:0000269|PubMed:25618265"
/id="VAR_073146"
VARIANT 163
/note="A -> V (in THPH3; drastically reduced secretion;
colocalizes with 26S proteasome)"
/evidence="ECO:0000269|PubMed:25618265"
/id="VAR_073147"
VARIANT 175
/note="C -> Y (in patients with PROC deficiency;
dbSNP:rs199469474)"
/evidence="ECO:0000269|PubMed:22545135"
/id="VAR_074299"
VARIANT 178
/note="A -> P (in THPH4; Clamart; dbSNP:rs1254257945)"
/evidence="ECO:0000269|PubMed:7878626"
/id="VAR_006660"
VARIANT 181
/note="F -> V (in patients with PROC deficiency;
dbSNP:rs199469470)"
/evidence="ECO:0000269|PubMed:22545135"
/id="VAR_074300"
VARIANT 183
/note="C -> R (in patients with PROC deficiency;
dbSNP:rs748920874)"
/id="VAR_006661"
VARIANT 189
/note="R -> W (in patients with PROC deficiency; La Jolla-
3; dbSNP:rs146922325)"
/evidence="ECO:0000269|PubMed:22545135"
/id="VAR_006662"
VARIANT 194
/note="R -> C (in patients with PROC deficiency;
dbSNP:rs371071104)"
/id="VAR_006663"
VARIANT 210
/note="P -> L (in THPH3; dbSNP:rs121918145)"
/evidence="ECO:0000269|PubMed:8292730"
/id="VAR_006664"
VARIANT 211
/note="R -> Q (in patients with PROC deficiency;
dbSNP:rs199469476)"
/evidence="ECO:0000269|PubMed:22545135,
ECO:0000269|PubMed:8499565"
/id="VAR_006666"
VARIANT 211
/note="R -> W (in THPH3; London-1/Tochigi;
dbSNP:rs121918143)"
/evidence="ECO:0000269|PubMed:2602169,
ECO:0000269|PubMed:8292730"
/id="VAR_006665"
VARIANT 220
/note="R -> P (in patients with PROC deficiency)"
/evidence="ECO:0000269|PubMed:7605880"
/id="VAR_006667"
VARIANT 220
/note="R -> Q (in THPH3; Vermont-3; dbSNP:rs121918153)"
/evidence="ECO:0000269|PubMed:1301959,
ECO:0000269|PubMed:1511989, ECO:0000269|PubMed:9798967"
/id="VAR_006669"
VARIANT 220
/note="R -> W (in THPH3; dbSNP:rs121918152)"
/evidence="ECO:0000269|PubMed:1511989,
ECO:0000269|PubMed:22545135"
/id="VAR_006668"
VARIANT 223
/note="S -> R (in patients with PROC deficiency;
dbSNP:rs199469483)"
/evidence="ECO:0000269|PubMed:22545135"
/id="VAR_074301"
VARIANT 226
/note="Q -> H (in patients with PROC deficiency;
dbSNP:rs121918155)"
/id="VAR_006670"
VARIANT 240
/note="A -> G (in patients with PROC deficiency)"
/evidence="ECO:0000269|PubMed:22545135"
/id="VAR_074302"
VARIANT 243
/note="I -> T (in THPH3; dbSNP:rs774584131)"
/evidence="ECO:0000269|PubMed:8292730"
/id="VAR_006671"
VARIANT 244
/note="H -> Y (in patients with PROC deficiency;
dbSNP:rs759557871)"
/evidence="ECO:0000269|PubMed:8499565"
/id="VAR_006672"
VARIANT 253
/note="H -> Q (in patients with PROC deficiency;
dbSNP:rs1458669732)"
/evidence="ECO:0000269|PubMed:8499565"
/id="VAR_006673"
VARIANT 265
/note="L -> F (in patients with PROC deficiency;
dbSNP:rs121918156)"
/id="VAR_006674"
VARIANT 271
/note="R -> Q (in Marseille; low anticoagulant activity;
dbSNP:rs752290840)"
/evidence="ECO:0000269|PubMed:8324221"
/id="VAR_006675"
VARIANT 271
/note="R -> W (in patients with PROC deficiency;
dbSNP:rs767112991)"
/id="VAR_006676"
VARIANT 272
/note="R -> C (in THPH3; dbSNP:rs121918154)"
/evidence="ECO:0000269|PubMed:1868249"
/id="VAR_006677"
VARIANT 281
/note="D -> DLD (in patients with PROC deficiency)"
/id="VAR_006678"
VARIANT 289
/note="P -> L (in THPH4; dbSNP:rs121918151)"
/evidence="ECO:0000269|PubMed:1511988"
/id="VAR_006679"
VARIANT 294
/note="S -> N (in Paris; low anticoagulant activity;
dbSNP:rs200721675)"
/evidence="ECO:0000269|PubMed:8324221"
/id="VAR_006680"
VARIANT 297
/note="D -> H (in THPH3; also found in patients with PROC
deficiency; decrease in vitamin-K dependent serine protease
activity; decreased Golgi localization; dbSNP:rs199469471)"
/evidence="ECO:0000269|PubMed:22545135,
ECO:0000269|PubMed:25748729"
/id="VAR_074303"
VARIANT 298
/note="N -> D (in patients with PROC deficiency)"
/id="VAR_006681"
VARIANT 301
/note="A -> T (in patients with PROC deficiency;
dbSNP:rs1343264503)"
/evidence="ECO:0000269|PubMed:7605880"
/id="VAR_006682"
VARIANT 301
/note="A -> V (in patients with PROC deficiency;
dbSNP:rs121918144)"
/id="VAR_006683"
VARIANT 309
/note="A -> T (in patients with PROC deficiency;
dbSNP:rs121918146)"
/id="VAR_006684"
VARIANT 312
/note="S -> L (in patients with PROC deficiency;
dbSNP:rs121918160)"
/evidence="ECO:0000269|PubMed:22545135"
/id="VAR_006685"
VARIANT 312
/note="S -> P (in a patient with PROC deficiency; sporadic
case)"
/evidence="ECO:0000269|PubMed:7919373"
/id="VAR_006686"
VARIANT 317
/note="P -> S (in patients with PROC deficiency; abolishes
Golgi localization)"
/evidence="ECO:0000269|PubMed:22531345"
/id="VAR_074304"
VARIANT 321
/note="P -> L (in THPH3; dbSNP:rs1321566264)"
/evidence="ECO:0000269|PubMed:8292730,
ECO:0000269|PubMed:8499565"
/id="VAR_006687"
VARIANT 324
/note="G -> R (in THPH3)"
/evidence="ECO:0000269|PubMed:7792728"
/id="VAR_006688"
VARIANT 327
/note="E -> V (in patients with PROC deficiency;
dbSNP:rs199469480)"
/evidence="ECO:0000269|PubMed:22545135"
/id="VAR_074305"
VARIANT 328
/note="R -> C (in THPH3; dbSNP:rs201907715)"
/evidence="ECO:0000269|PubMed:7792728,
ECO:0000269|PubMed:8499565"
/id="VAR_006689"
VARIANT 328
/note="R -> H (in THPH4; Muenchen)"
/evidence="ECO:0000269|PubMed:7878626"
/id="VAR_006690"
VARIANT 334
/note="G -> S (in THPH4; dbSNP:rs121918150)"
/evidence="ECO:0000269|PubMed:1593215"
/id="VAR_006691"
VARIANT 340
/note="T -> M (in THPH3; Vermont-2; dbSNP:rs766261022)"
/evidence="ECO:0000269|PubMed:8292730,
ECO:0000269|PubMed:9798967"
/id="VAR_006692"
VARIANT 343
/note="G -> D (in patients with PROC deficiency)"
/id="VAR_006693"
VARIANT 357
/note="T -> A (gain of function mutation; abolishes
glycosylation at N-313; decreases its catalytic activity;
significant loss of its protective effect on endothelial
barrier function; increased activation by thrombin)"
/evidence="ECO:0000269|PubMed:25651845"
/id="VAR_074306"
VARIANT 363
/note="Missing (in patients with PROC deficiency)"
/id="VAR_006694"
VARIANT 367
/note="V -> A (in THPH4; neonatal purpura fulminans;
dbSNP:rs767730328)"
/evidence="ECO:0000269|PubMed:7841324"
/id="VAR_006695"
VARIANT 369
/note="P -> L (in THPH3; Osaka-6; dbSNP:rs1211098698)"
/evidence="ECO:0000269|PubMed:7792728,
ECO:0000269|PubMed:7865674"
/id="VAR_006696"
VARIANT 385
/note="M -> I (in patients with PROC deficiency)"
/evidence="ECO:0000269|PubMed:8499565"
/id="VAR_006697"
VARIANT 388
/note="A -> T (in patients with PROC deficiency)"
/evidence="ECO:0000269|PubMed:8499565"
/id="VAR_006698"
VARIANT 388
/note="A -> V (in patients with PROC deficiency;
dbSNP:rs769277939)"
/evidence="ECO:0000269|PubMed:8499565"
/id="VAR_006699"
VARIANT 392
/note="G -> R (in THPH3; Osaka-9; dbSNP:rs756467027)"
/evidence="ECO:0000269|PubMed:7865674"
/id="VAR_006700"
VARIANT 394
/note="R -> W (in patients with PROC deficiency;
dbSNP:rs759316085)"
/id="VAR_006701"
VARIANT 401
/note="D -> N (in THPH3; La Jolla-2/Osaka-7 and -8;
dbSNP:rs142742242)"
/evidence="ECO:0000269|PubMed:7865674"
/id="VAR_006702"
VARIANT 418
/note="G -> D (in THPH4; Hong Kong-2)"
/evidence="ECO:0000269|PubMed:1611081"
/id="VAR_006703"
VARIANT 420
/note="V -> L (in THPH3; also found in patients with PROC
deficiency; decrease in vitamin-K dependent serine protease
activity; dbSNP:rs199469472)"
/evidence="ECO:0000269|PubMed:22545135,
ECO:0000269|PubMed:25748729"
/id="VAR_074307"
VARIANT 423
/note="G -> S (in THPH3)"
/evidence="ECO:0000269|PubMed:8398832"
/id="VAR_006704"
VARIANT 426
/note="C -> Y (in THPH3)"
/evidence="ECO:0000269|PubMed:8292730"
/id="VAR_006705"
VARIANT 433
/note="G -> S (in patients with PROC deficiency; Purmerend;
dbSNP:rs1266965698)"
/id="VAR_006706"
VARIANT 436
/note="T -> N (in THPH3)"
/evidence="ECO:0000269|PubMed:8829639"
/id="VAR_006707"
VARIANT 441
/note="Y -> H (in THPH3; Osaka-4; dbSNP:rs753436021)"
/evidence="ECO:0000269|PubMed:7865674"
/id="VAR_006708"
VARIANT 444
/note="W -> C (in THPH3; dbSNP:rs121918142)"
/evidence="ECO:0000269|PubMed:2437584"
/id="VAR_006709"
VARIANT 445
/note="I -> M (in patients with PROC deficiency;
dbSNP:rs121918157)"
/id="VAR_006710"
CONFLICT 106
/note="C -> Q (in Ref. 11; AAA60164)"
/evidence="ECO:0000305"
CONFLICT 445
/note="I -> IL (in Ref. 3; AAA60165)"
/evidence="ECO:0000305"
HELIX 48..50
/evidence="ECO:0007829|PDB:1LQV"
HELIX 55..59
/evidence="ECO:0007829|PDB:1LQV"
HELIX 66..73
/evidence="ECO:0007829|PDB:1LQV"
STRAND 101..103
/evidence="ECO:0007829|PDB:6M3B"
TURN 104..107
/evidence="ECO:0007829|PDB:6M3B"
STRAND 108..111
/evidence="ECO:0007829|PDB:6M3B"
STRAND 120..122
/evidence="ECO:0007829|PDB:6M3B"
STRAND 126..128
/evidence="ECO:0007829|PDB:6M3B"
STRAND 138..142
/evidence="ECO:0007829|PDB:6M3B"
HELIX 143..146
/evidence="ECO:0007829|PDB:6M3B"
STRAND 148..153
/evidence="ECO:0007829|PDB:6M3B"
STRAND 158..161
/evidence="ECO:0007829|PDB:6M3B"
STRAND 166..168
/evidence="ECO:0007829|PDB:6M3B"
STRAND 175..177
/evidence="ECO:0007829|PDB:6M3B"
STRAND 179..181
/evidence="ECO:0007829|PDB:6M3B"
STRAND 226..230
/evidence="ECO:0007829|PDB:6M3B"
STRAND 236..244
/evidence="ECO:0007829|PDB:6M3B"
STRAND 247..250
/evidence="ECO:0007829|PDB:6M3B"
HELIX 252..255
/evidence="ECO:0007829|PDB:6M3B"
STRAND 262..266
/evidence="ECO:0007829|PDB:6M3B"
STRAND 269..272
/evidence="ECO:0007829|PDB:6M3B"
STRAND 278..287
/evidence="ECO:0007829|PDB:6M3B"
TURN 293..295
/evidence="ECO:0007829|PDB:6M3B"
STRAND 301..307
/evidence="ECO:0007829|PDB:6M3B"
HELIX 323..328
/evidence="ECO:0007829|PDB:6M3B"
TURN 329..331
/evidence="ECO:0007829|PDB:6M3B"
STRAND 336..341
/evidence="ECO:0007829|PDB:6M3B"
STRAND 357..359
/evidence="ECO:0007829|PDB:1AUT"
STRAND 361..368
/evidence="ECO:0007829|PDB:6M3B"
HELIX 370..376
/evidence="ECO:0007829|PDB:6M3B"
STRAND 385..388
/evidence="ECO:0007829|PDB:6M3B"
TURN 399..403
/evidence="ECO:0007829|PDB:6M3B"
STRAND 405..410
/evidence="ECO:0007829|PDB:6M3B"
STRAND 413..422
/evidence="ECO:0007829|PDB:6M3B"
STRAND 424..427
/evidence="ECO:0007829|PDB:6M3B"
STRAND 433..437
/evidence="ECO:0007829|PDB:6M3B"
HELIX 438..441
/evidence="ECO:0007829|PDB:6M3B"
HELIX 442..449
/evidence="ECO:0007829|PDB:6M3B"
SEQUENCE 461 AA; 52071 MW; 3531B0AE5345B39A CRC64;
MWQLTSLLLF VATWGISGTP APLDSVFSSS ERAHQVLRIR KRANSFLEEL RHSSLERECI
EEICDFEEAK EIFQNVDDTL AFWSKHVDGD QCLVLPLEHP CASLCCGHGT CIDGIGSFSC
DCRSGWEGRF CQREVSFLNC SLDNGGCTHY CLEEVGWRRC SCAPGYKLGD DLLQCHPAVK
FPCGRPWKRM EKKRSHLKRD TEDQEDQVDP RLIDGKMTRR GDSPWQVVLL DSKKKLACGA
VLIHPSWVLT AAHCMDESKK LLVRLGEYDL RRWEKWELDL DIKEVFVHPN YSKSTTDNDI
ALLHLAQPAT LSQTIVPICL PDSGLAEREL NQAGQETLVT GWGYHSSREK EAKRNRTFVL
NFIKIPVVPH NECSEVMSNM VSENMLCAGI LGDRQDACEG DSGGPMVASF HGTWFLVGLV
SWGEGCGLLH NYGVYTKVSR YLDWIHGHIR DKEAPQKSWA P


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Pathways :
WP1678: Nucleotide excision repair
WP1625: Base excision repair
WP1493: Carbon assimilation C4 pathway
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP1531: Vitamin D synthesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP1665: Limonene and pinene degradation
WP2344: vitamin B6 (pyridoxine, pyridoxal, pyridoxamine) biosynthesis and salvage pathway
WP1502: Mitochondrial biogenesis
WP1673: Naphthalene and anthracene degradation
WP2347: vitamin B5 (pantothenate) and CoA biosynthesis Pathway
WP2203: TSLP Signaling Pathway
WP2371: Parkinsons Disease Pathway
WP1690: Propanoate metabolism
WP2292: Chemokine signaling pathway
WP1644: DNA replication
WP1694: Pyrimidine metabolism
WP1713: Two-component system
WP1661: Glyoxylate and dicarboxylate metabolism
WP813: G Protein Signaling Pathways
WP210: Cytoplasmic Ribosomal Proteins
WP525: Mitochondrial Unfolded-Protein Response
WP1624: Bacterial secretion system
WP2199: Seed Development

Related Genes :
[PROC] Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide]
[F2] Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F9] 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]
[F7] Coagulation factor VII (EC 3.4.21.21) (Proconvertin) (Serum prothrombin conversion accelerator) (SPCA) (Eptacog alfa) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[F5] Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain]
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[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Stuart-Prower factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[yaiE ppnP yaiE_1 yaiE_2 A5U30_004171 A6592_08565 A8499_002689 A9819_01890 A9X72_19070 AAG43_001684 AAS29_000851 ABE90_005680 ACN68_10320 ACN81_25005 ACU57_12035 AM464_18935 APX88_10995 AT845_004245 AW118_21925 AW119_10870 AWP93_11760 B6R12_004630 B6R15_004744 B6R31_001962 B6R48_001853 B6R87_002119 BANRA_00925 BANRA_01371 BANRA_03594 BEA19_24120 BER14_23410 BFL24_02350 BG944_000956 BGZ_00885 BGZ_00919 BHS81_02405 BIZ41_26355 BJI68_13875 BJJ90_20310 BK292_14635 BK383_14985 BMC79_001982 BMT50_02930 BMT91_05310 BN17_01951 BO068_001728 BOB65_000444 BOH76_16090 BON63_11530 BON64_14410 BON65_18745 BON66_09075 BON67_24210 BON68_23505 BON69_11595 BON70_06170 BON71_09670 BON72_15085 BON73_05975 BON74_21685 BON75_11450 BON76_23825 BON77_14130 BON78_10125 BON79_13380 BON80_10900 BON81_13115 BON82_13085 BON83_20655 BON84_16485 BON86_03800 BON87_15370 BON88_22820 BON89_00190 BON90_16345 BON91_23895 BON92_15465 BON93_19270 BON94_14845 BON95_06500 BON96_22295 BON97_17555 BON98_18895 BR158_003623 BR331_05500 BRV34_002179 BRV41_001603 BTQ06_17790 BvCmsF30A_04718 BvCmsHHP019_02594 BvCmsHHP019_02735 BvCmsHHP056_01410 BvCmsKKP036_04281 BvCmsKKP061_04019 BvCmsKSNP073_05624 BvCmsNSP072_00997 BVL39_00880 BXT93_00165 BZL69_16805 C2M16_02670 C2U48_08110 C3F40_10585 C5N07_12740 C5Y87_03235 C9114_16640 C9160_00550 C9E67_23765 C9Z68_20485 CA593_01185 CCS08_21635 CDC27_00860 CDL36_14165 CDL37_09465 CG692_05055 CG831_000443 CIG67_05475 CO706_24355 COD53_04445 CQP61_20925 CR538_19495 CR539_06140 CT143_00140 CV83915_01183 CWS33_22875 CXJ73_003963 CY655_02075 D0X26_07420 D1912_23295 D3822_22465 D3C88_28950 D3G36_08025 D3Y67_14350 D4U49_03050 D9D43_14830 D9D77_05600 D9E34_09525 D9E49_06955 D9H94_24405 D9J03_17400 D9J61_02635 DAH18_14975 DAH19_15000 DAH20_16610 DAH21_08165 DAH22_13870 DAH23_10455 DAH24_10460 DAH25_11070 DAH26_10405 DAH27_14160 DAH28_13335 DAH29_17045 DAH30_15925 DAH31_19150 DAH32_11190 DAH33_11330 DAH34_21345 DAH35_16790 DAH36_12775 DAH37_05240 DAH38_03050 DAH40_06810 DAH41_17310 DAH42_11390 DAH43_09880 DAH45_10305 DAH46_11945 DAH47_09160 DAH48_11635 DAH49_09890 DAH50_14800 DD762_07680 DEN86_05080 DEN87_01895 DEN88_05530 DEN89_14495 DEN90_11705 DEN91_05595 DEN92_06605 DEN93_13160 DEN94_11850 DEN95_09255 DEN96_07805 DEN97_15340 DEN98_11210 DEN99_05370 DEO00_05905 DEO01_11320 DEO02_08475 DEO03_14045 DEO04_04545 DEO05_04540 DEO06_05185 DEO07_08010 DEO08_13690 DEO09_07095 DEO10_06445 DEO11_06460 DEO12_12645 DEO13_16025 DEO14_08240 DEO15_17360 DEO17_12810 DEO18_12120 DEO19_20575 DEO20_14385 DIV22_26285 DKP82_22400 DM870_16555 DN627_04525 DNQ45_00335 DRW19_06400 DS732_06920 DTL43_07415 DTL90_10740 DTM16_08110 DTM45_10960 DU321_19460 DXT69_08115 DXT70_02910 DXT71_02970 DXT73_01860 E0I42_07410 E2113_03255 E2114_20640 E2115_06350 E2116_09805 E2117_07700 E2118_06725 E2119_01725 E2120_11120 E2121_07545 E2122_06175 E2123_04610 E2124_09375 E2125_09480 E2127_09375 E2128_04435 E2129_13975 E2130_11240 E2131_02470 E2132_00415 E2133_20420 E2134_12225 E2135_01410 E2136_05910 E2646_12335 E3N34_04125 E3O05_19530 E4K51_12070 E4T14_06285 E4T84_01105 E5M02_10020 E5P22_04675 E5P23_08765 E5P24_15620 E5P25_17640 E5P26_04525 E5P27_05835 E5P28_11315 E5P29_09580 E5P30_10170 E5P31_06170 E5P32_04305 E5P33_10200 E5P34_17740 E5P35_04515 E5P36_01750 E5P37_17680 E5P39_06005 E5P40_13740 E5P41_01335 E5P42_04485 E5P43_05450 E5P44_02065 E5P45_03910 E5P46_02310 E5P47_06990 E5P48_01380 E5P49_02350 E5P50_09075 E5P51_09940 E5P52_05895 E5S34_07545 E5S35_14895 E5S36_15140 E5S37_02355 E5S38_06765 E5S39_10925 E5S42_13060 E5S43_12135 E5S44_09845 E5S45_13175 E5S47_09895 E5S48_09860 E5S51_13535 E5S52_06115 E5S53_04160 E5S54_01050 E5S55_03120 E5S56_05125 E5S57_11350 E5S58_11035 E5S59_10435 E5S61_09810 E5S62_19990 EA239_15730 EA435_05820 EAI46_25725 EAI46_25840 EAN77_07940 EAX79_06830 EBP16_12520 EC1094V2_3464 EC3234A_4c00610 EC95NR1_04612 ECs0441 ED648_16775 EHD79_03470 EHH55_15815 EI021_16245 EIZ93_00830 EKI52_09170 EL79_3454 EL80_3408 ELT16_09225 ELT17_22260 ELT20_08340 ELT22_04045 ELT23_00125 ELT24_03290 ELT25_05960 ELT26_23225 ELT27_21290 ELT28_09190 ELT29_22585 ELT30_06725 ELT31_00280 ELT32_10020 ELT33_03015 ELT34_07270 ELT35_08275 ELT36_04475 ELT38_00125 ELT39_01450 ELT40_25125 ELT41_07365 ELT44_03945 ELT45_03425 ELT46_04360 ELT48_00735 ELT49_21480 ELT50_02330 ELT51_16695 ELT52_03690 ELT54_10860 ELT55_05135 ELT56_20800 ELT58_21305 ELT59_12100 ELT60_00640 ELT61_02575 ELT63_02620 ELT72_05540 ELU07_05385 ELU82_03335 ELU83_10395 ELU85_08960 ELU88_10700 ELU89_08675 ELU90_21735 ELU91_00300 ELU94_04615 ELU95_12465 ELU96_05805 ELU97_00035 ELU98_06160 ELU99_22320 ELV00_13055 ELV01_00640 ELV02_05465 ELV03_00640 ELV04_00460 ELV05_14615 ELV07_00640 ELV08_00785 ELV09_05330 ELV11_02540 ELV12_06015 ELV13_00555 ELV15_22680 ELV20_14710 ELV21_14165 ELV22_01630 ELV23_01450 ELV24_16525 ELV26_21885 ELV28_08410 ELV29_01550 ELV40_10610 ELX48_13080 ELX56_03900 ELX61_20790 ELX66_07890 ELX68_02065 ELX69_19550 ELX70_07125 ELX76_05850 ELX79_24270 ELX83_01445 ELX85_08400 ELX96_14305 ELY02_06110 ELY05_09885 ELY23_04665 ELY24_07180 ELY31_04360 ELY32_22740 ELY36_06760 ELY39_06095 ELY41_15435 ELY48_07355 ELY50_04295 EPS76_10515 EQO00_19840 ERS085406_02227 ERS139208_01812 EVY14_00050 EWK56_10245 ExPECSC038_04895 EXX13_09665 EYV17_03100 EYV18_10135 EYX47_16280 EYY21_28950 F0L67_19465 F2N31_18495 F3N40_11580 F7F11_06850 F9B07_11235 F9S76_00660 F9S83_01525 F9V24_00540 F9X20_10705 FA849_16230 FA868_02660 FDM60_01545 FEL34_02665 FFF58_18140 FGG80_03620 FGY90_08925 FHD44_10100 FJQ51_13145 FKO60_24460 FOI11_011505 FOI11_08540 FPI65_02250 FQ007_13115 FQF29_11270 FTV90_10360 FTV92_11870 FTV93_12360 FV293_06120 FWK02_29295 FZC17_02065 FZN31_18905 G3565_02860 G3813_001670 G4A38_05410 G9448_08700 GAJ26_09340 GF147_12390 GF699_04160 GFY34_04590 GIB53_01735 GJ11_02375 GKE84_19495 GKF86_04910 GKF89_04055 GKG12_02940 GNO40_22710 GNZ05_01665 GP650_16700 GP662_13045 GP711_02810 GP946_18990 GP954_12950 GP979_17585 GQE64_07505 GQF59_00790 GQM04_16295 GQM09_10135 GQM13_16755 GQW07_10130 GQW68_15010 GQW80_20255 GRC73_12510 GRO95_09290 GRW05_15575 GRW57_16360 GRW81_04110 GSY44_11760 GTP88_03425 GUB08_22335 GUB92_14995 GUC01_07480 GUI33_03675 H0O53_01395 H0O72_08355 H6Y26_001325 HHH44_001374 HI055_001796 HIN64_001318 HJ942_001977 HJQ60_002362 HJS37_002167 HJU54_001570 HKA49_002910 HL563_20960 HLV18_07370 HLZ50_17655 HmCms169_03669 HMU06_13895 HMU48_14510 HMV41_12865 HMV95_11570 HNC36_06780 HNC59_10160 HNC66_06600 HNC99_09055 HV109_18115 HV209_02875 HV209_28635 HVV39_18775 HVW19_16065 HVW43_10265 HVX16_19490 HVY77_19945 HVZ71_18990 HX136_19525 I6H02_19720 IA00_002609 IAI11_04290 IFB95_004044 IH768_07535 IH772_12750 IT029_003225 J0541_001749 J4S20_001870 J5U05_002183 JE86ST02C_04160 JE86ST05C_04220 JFD_01983 JNP96_06385 NCTC10082_01078 NCTC10089_03910 NCTC10418_05682 NCTC10429_03762 NCTC10764_05371 NCTC10767_04209 NCTC10865_04787 NCTC10958_04085 NCTC11126_00022 NCTC11181_01145 NCTC11341_03896 NCTC12950_04180 NCTC13127_05156 NCTC13216_02895 NCTC7922_06246 NCTC7927_04270 NCTC8008_03382 NCTC8009_07014 NCTC8179_01642 NCTC8333_04532 NCTC8450_01367 NCTC8500_04283 NCTC8621_03984 NCTC8622_02997 NCTC8959_05017 NCTC8960_01314 NCTC8985_02798 NCTC9001_00537 NCTC9036_03840 NCTC9037_03956 NCTC9044_03501 NCTC9045_04434 NCTC9075_05103 NCTC9077_04792 NCTC9081_02496 NCTC9111_03977 NCTC9117_04804 NCTC9702_04480 NCTC9706_01114 NCTC9775_02088 NCTC9777_00174 ND22_001447 PGD_02920 RG28_02910 SAMEA3472044_00466 SAMEA3472056_03633 SAMEA3472067_03190 SAMEA3472080_01810 SAMEA3472147_04902 SAMEA3751407_02141 SAMEA3752557_00215 SAMEA3753106_00531 TUM18780_32860 WP2S18E08_35360 WP4S18E07_34480 WR15_04360] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F7 Cf7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[cysG cobA cysG_1 A9X72_01910 AAG43_001988 ACU57_16475 AM464_09505 APX88_19990 AT335_001457 AT845_000838 AW119_18405 B6R12_000433 B6R15_000438 B6R31_002265 B6R48_002892 B6R87_002674 BANRA_02000 BEA19_06265 BFL24_22825 BG944_001170 BGZ_02522 BGZ_04176 BHS81_20170 BJI68_14980 BJJ90_01855 BK292_07805 BK383_21245 BMT50_12020 BMT91_03480 BN17_33031 BO068_001511 BON68_10270 BON69_10260 BON71_12915 BON72_01440 BON73_10630 BON74_15490 BON76_01755 BON77_11870 BON80_05005 BON86_09425 BON87_12715 BON89_19425 BON92_08155 BON93_16715 BON94_27630 BON95_18940 BON96_09170 BON97_13605 BON98_09595 BTQ06_10895 BvCmsHHP019_00453 BvCmsHHP056_00471 BvCmsKKP036_03618 BvCmsKKP061_02746 BvCmsKSNP073_02778 BVL39_09270 BXT93_04970 C2U48_16615 C3F40_19450 C5N07_12010 C5Y87_16100 C9160_13305 C9E67_02520 CA593_09385 CCS08_20190 CDL36_09890 CDL37_28050 CG692_18475 CG831_001319 CO706_15490 COD53_10805 CQP61_02825 CR538_02140 CV83915_02742 D0X26_11130 D3Y67_21055 D9D77_07850 D9J03_02940 DAH17_09810 DAH19_16670 DAH23_09650 DAH24_08490 DAH25_10025 DAH26_09660 DAH33_06185 DAH36_11125 DAH37_15045 DAH38_04465 DAH40_11100 DAH42_05980 DAH43_07425 DAH45_06820 DAH46_07415 DAH47_06665 DAH48_07045 DAH49_06445 DAH50_22180 DEN87_09175 DEN88_06390 DEN91_13010 DEN92_11290 DEO01_08465 DEO04_11505 DEO05_10515 DEO06_10750 DEO07_11165 DEO08_07685 DEO09_11180 DEO10_12145 DEO11_11175 DEO12_09880 DEO18_07345 DEO19_07030 DKP82_18010 DM870_05140 DN627_01935 DRW19_01875 DS732_24620 DTL43_13910 DXT70_11025 DXT71_09335 DXT73_15385 E0I42_11615 E2113_03950 E2114_05545 E2115_14845 E2116_09525 E2118_13345 E2119_04420 E2120_03115 E2121_12250 E2122_12580 E2123_13315 E2124_03100 E2125_08230 E2127_11625 E2128_02995 E2129_07715 E2130_05310 E2131_12705 E2132_12455 E2134_14675 E2135_05845 E2136_12190 E4K51_10410 E4T14_04150 E5M02_05395 E5P23_12605 E5P26_08715 E5P27_11605 E5P28_09015 E5P29_17035 E5P30_17020 E5P31_08360 E5P32_02635 E5P34_04165 E5P35_02075 E5P36_22230 E5P39_05360 E5P40_03010 E5P41_03090 E5P42_18750 E5P43_17135 E5P44_02270 E5P45_13505 E5P46_16215 E5P47_07830 E5P48_15275 E5P49_19715 E5P50_07715 E5P51_03395 E5S34_10830 E5S36_14445 E5S37_08710 E5S38_11725 E5S39_08725 E5S42_07810 E5S44_10765 E5S45_09695 E5S46_17870 E5S51_12835 E5S54_06345 E5S56_12875 E5S57_11110 E5S58_13600 E5S61_12510 EAN77_07220 EAX79_11000 EC1094V2_285 EC3234A_57c00300 ECs4219 EHD79_06180 EHH55_25160 EIZ93_01520 EL79_0346 EL80_0339 ELT20_09645 ELT21_04095 ELT28_07415 ELT41_06680 ELT49_16745 ELT51_00160 ELT58_15470 ELV08_06310 ELV09_18525 ELV40_20320 ELX76_05275 ELX85_01910 ELY02_07910 ELY05_18405 ELY39_08945 ERS139208_04133 ExPECSC038_01180 EXX13_13990 EYV17_09700 EYV18_11775 EYX47_06865 F0L67_12565 F3N40_09040 F9S76_07985 F9V24_01660 F9X20_02300 FDM60_01830 FGG80_13590 FKO60_13910 FOI11_018920 FOI11_04260 FQF29_05650 FV293_08795 FY127_06225 G4A38_16850 G5632_11415 G9448_16805 GAJ26_06530 GF699_08140 GIB53_18980 GKF86_11410 GKF89_12400 GKG12_07200 GP650_08540 GP662_20205 GP946_11295 GQF59_06890 GQM09_05375 GQM13_20710 GQW80_09495 GRW81_14155 GSY44_04895 GTP88_00155 GUC01_14450 H0O72_13320 HHH44_000575 HJS37_002539 HLZ50_06645 HMU48_07765 HMV95_07770 HNC59_07440 HNC99_05445 HND12_12975 HV109_01850 HV209_14445 HVW04_17265 HVW43_18400 HVY77_01835 HVZ71_02090 HX136_01855 I6H00_19725 I6H01_10990 IA00_000722 IAI11_06870 IH772_08875 IT029_003044 J0541_002119 J4S20_001182 JFD_03780 JNP96_25645 NCTC10090_03474 NCTC10418_00625 NCTC10764_03803 NCTC10865_00602 NCTC10958_00745 NCTC13148_03528 NCTC13216_01418 NCTC4450_02421 NCTC8008_05413 NCTC8179_05884 NCTC8333_00435 NCTC8500_00246 NCTC9037_00596 NCTC9045_00486 NCTC9111_00814 NCTC9117_00666 PGD_00517 RG28_21890 SAMEA3472044_01095 SAMEA3472080_02892 SAMEA3751407_00091 SAMEA3753106_01911 TUM18780_03830 WP2S18E08_03400 WR15_02785] Siroheme synthase [Includes: Uroporphyrinogen-III C-methyltransferase (Urogen III methylase) (EC 2.1.1.107) (SUMT) (Uroporphyrinogen III methylase) (UROM); Precorrin-2 dehydrogenase (EC 1.3.1.76); Sirohydrochlorin ferrochelatase (EC 4.99.1.4)]
[] Botulinum neurotoxin type C (BoNT/C) (Bontoxilysin-C1) (BoNT/C1) (Botulinum neurotoxin type C1) [Cleaved into: Botulinum neurotoxin C light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin C heavy chain (HC)]
[F10] Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[nnr nnrD nnrE A3S59_13690 A3T49_17335 A3T75_18530 A3U47_10225 A3U54_09275 A3U78_16085 A3V15_17065 A3V28_15960 A3W22_12930 A4M41_16600 A5970_12510 A6267_12745 A6T07_15280 A7C55_07720 A7H28_15850 A9591_13875 A9C99_18275 A9D71_20055 A9S47_10990 A9S88_14770 A9X19_06535 AAA56_09530 AAB90_13650 ABA14_13890 ABP10_07270 ABQ42_14075 ACG84_16195 ACM10_17980 ACT92_14320 ACT96_14390 ADR00_04465 ADS36_15285 AGN17_13430 AGP91_11565 AH461_16240 AHV90_18155 AIE92_07590 AKX49_10100 AL461_13480 ALZ46_15575 AM316_12625 AM321_08345 AM525_15220 AN727_01255 AO198_17430 AO799_11345 AOL87_17660 AOL88_17815 AOU74_07580 APN68_15490 APO02_17555 AQ518_14155 AR267_17095 AS882_13920 ASN84_12635 ASV75_18200 AU760_14795 AU775_10415 AVB14_10850 AVI06_14750 B0A21_09265 B0F61_13105 B1868_15980 B4P96_15895 B4W84_18200 B4Z10_18285 B5C64_17865 B6339_13635 B6379_12905 B6396_17560 B6M83_15130 B6N80_13955 B7136_14330 B7900_15880 B7919_12405 B7C82_16710 B7J34_05280 B7M41_18735 B7Q10_20390 B8V98_15175 B8Y89_12815 B8Y98_13185 B8Z45_12040 B9176_15685 B9672_11375 B9673_18235 B9727_12095 B9756_14295 B9H85_18105 B9I48_18045 B9P12_16640 BB088_18985 BBL75_13960 BCA48_20120 BCB01_020120 BCB09_0020120 BCP76_14830 BCP85_15340 BCP91_17540 BH227_14585 BIB62_15765 BJO06_15955 BJO39_11850 BK099_19165 BK864_11970 BKF55_14350 BKO29_15730 BSD53_18530 BSD63_15630 BTC31_13980 BXJ37_18690 BZ670_13760 BZ697_16830 BZ722_12720 BZ742_17225 BZ751_18150 BZ759_12840 BZ809_15460 BZ833_13870 BZ881_13655 BZ894_14830 BZ908_18660 BZ939_15625 BZ955_18375 BZ980_09135 BZT14_03720 CA122_13445 CA124_14440 CAD25_13880 CAD70_18135 CAI12_16660 CB062_10255 CB096_14700 CB217_12805 CB220_14435 CB308_15940 CB345_18040 CB472_13065 CB501_11525 CB588_08220 CB596_12655 CB604_10145 CB666_16595 CB721_20345 CBB04_19195 CBB05_13840 CBK53_19215 CBN66_14655 CBN70_12475 CBP97_18655 CBQ45_13910 CBR92_19970 CBR95_11870 CBS03_20305 CBS08_20655 CBS18_16760 CBS39_20735 CBS55_14975 CBS77_09830 CBS78_13115 CBU16_17980 CC149_15825 CC297_18255 CC421_17090 CC678_12725 CC680_11650 CC754_11940 CC805_16855 CC853_16680 CCG98_12880 CCP20_16675 CD530_14030 CDG21_09565 CEA09_11005 CEI41_16725 CEM11_08675 CER90_13970 CEW05_18215 CFB87_11490 CFC01_18200 CFD56_12055 CRE05_02200 D0175_08570 D0A07_14920 D0W94_21365 D3E03_19475 D4415_18015 D4E56_15415 D4F08_19940 D4X57_18540 D4Z56_20190 D5A37_07260 D5O28_18970 D5O87_18615 D5X06_18105 D6J64_14370 D6K13_17205 D6P81_17650 D6R78_16230 D6S88_17785 D6T13_10065 D8Q93_17795 D8S08_07470 D9O81_17800 DLM07_05510 DLQ89_09585 DM648_22170 DMI96_14640 DN254_16985 DO678_17965 DOB11_13010 DOJ41_18470 DOR31_16660 DP790_14935 DP797_19060 DPF44_17095 DPR73_10030 DQ906_16405 DQY42_21185 DQZ81_15615 DRD18_11105 DRK03_17440 DRM04_20170 DRV81_18170 DRX23_19640 DRX96_13475 DS187_17705 DSH04_16815 DSH32_11170 DSN07_15575 DTD96_08125 DTF75_15870 DTI59_10095 DU772_16825 DU867_16745 DUA99_06710 DUB03_17090 DUG35_21095 DUG37_09455 DW487_05640 DY875_08435 DYT79_05520 E2D06_09125 E3C38_19875 E3C57_04960 E5382_12770 E5B97_15680 EAH10_10215 EBB65_17355 EBB99_17160 EBC54_19500 EBC72_13645 EES12_17090 EGL58_19555 EGM21_17370 EHF05_18050 EI456_17675 EI507_18340 EIL24_18235 EIL34_19605 EJG81_18690 EKH43_18120 EKP78_17715 EL812_18020 ELS48_18010 ELY67_16875 ENE83_16990 ERF73_18615 ETB65_18865 EU248_15750 EUZ49_23140 EVI13_02840 EVU69_19825 EZV86_08115 EZX35_16585 F9O36_14895 F9O65_17665 F9P74_18100 F9Q56_17905 FEE84_12285 FEO32_14500 FI281_14470 FI295_17155 FI296_17695 FII38_15555 FII69_17055 FPF90_15410 FTS15_19435 G0A20_15610 G0D20_21205 G0F92_04370 G0F99_20490 G0G00_15020 G0G01_14620 G0G02_01265 G0G04_14275 G0G05_11320 G0G06_08950 G0G07_03945 G0G14_13450 G0G15_05635 G0G16_18195 G0G17_18550 G0G20_12380 G0G22_03800 G0G23_02895 G0G27_20255 G0G31_04885 G0G32_18695 G0G35_22650 G0G37_21300 G0G38_05325 G0G39_05210 G0G40_00495 G0G41_05320 G0G43_20245 G0G45_03755 G0G49_12345 G0G50_02375 G0G51_12780 G0G52_02055 G0G53_14405 G0G54_12570 G0G55_02745 G0G60_04900 G0G61_21540 G0G62_03530 G0G64_11380 G2169_20120 G2170_17950 G2196_15620 G2210_18475 G2222_16940 G2233_16805 G2235_12530 G2237_14760 G2242_16685 G2243_18305 G2249_18265 G2264_16425 G2266_19975 G2271_14330 G2282_17940 G2286_15060 G2298_18170 G2300_17895 G2301_16625 G2322_17655 G2326_05510 G2331_17485 G2345_14690 G2351_11360 G2395_18425 G2410_17370 G2484_18475 G2668_16905 G2672_18505 G2673_12285 G2674_18195 G2681_14230 G2684_17165 G2685_16660 G2686_18420 G2687_17170 G2689_19715 G2693_13850 G2696_16030 G2699_17735 G2700_17140 G2703_18695 G2705_18350 G2706_16440 G2710_15110 G2716_19115 G2717_19090 G2719_18745 G2723_19745 G2726_18435 G2729_18855 G2730_16180 G2732_14990 G2737_11175 G2740_14430 G2745_14690 G2747_17475 G2749_19595 G2751_17145 G2757_17470 G2767_17765 G2784_16450 G2846_16730 G2849_14480 G2856_16940 G2858_16510 G2859_16270 G2860_18520 G2861_14560 G2862_16635 G2863_16285 G2866_13475 G2872_17555 G2874_18875 G2879_17610 G2880_17495 G2882_11825 G2888_18110 G2889_15285 G2890_17755 G2894_09340 G2896_13570 G2902_20700 G2905_11225 G2914_18010 G2939_05565 G2944_09900 G2954_06260 G2964_16835 G2968_15020 G2971_07585 G2973_04400 G2981_03795 G2984_05660 G2989_12910 G2991_03275 G3259_002224 G3346_003537 G3347_001862 G3348_002116 G3414_001902 G3453_002421 G3972_003350 G3984_004132 G3A07_07855 G3A13_18970 G3A29_16685 G3V00_002516 G3V03_003780 G3W49_001000 G4179_002628 G4B49_002728 G4B62_003839 G4D14_001210 G4G55_002523 G4G70_002745 G4J13_004244 G4J27_003406 G4K89_000861 G4L00_003905 G4L11_003511 G4O33_003194 G4O34_001052 G4O38_002777 G4O43_002653 G4P59_003264 G4P65_002509 G4P71_002341 G4Q33_002605 G4Q34_002222 G4Y16_001057 G4Y74_001950 G4Y75_002585 G9273_003139 G9374_002432 G9375_003558 G9C39_002301 G9G26_004226 G9G29_003563 G9G49_002046 G9W24_002411 G9W26_002811 G9W60_001328 GB008_18185 GB023_19730 GB033_06215 GB073_21190 GB084_15780 GB104_17820 GB108_20855 GB117_12760 GB119_19790 GB125_16930 GB136_14545 GB146_16180 GB163_19015 GB165_16740 GB167_14000 GB172_16190 GB174_14415 GB183_21130 GB184_15005 GB191_20690 GB220_18210 GB222_15290 GB260_14850 GB264_18960 GB267_21450 GB268_17125 GB322_04260 GB328_03375 GB340_20380 GB350_18005 GB366_20965 GB382_13880 GB384_17705 GB389_17130 GB395_14155 GB398_19660 GB400_17165 GB410_19810 GB411_20290 GB424_18050 GB444_15320 GB453_02390 GB458_14190 GB471_14430 GB474_15350 GB512_06355 GB517_16250 GB521_21110 GB522_13565 GB528_15755 GB536_16845 GB545_21125 GB552_05380 GB596_11600 GB605_13600 GB608_14220 GB611_21255 GB617_20665 GB638_12945 GBR90_15875 GBR92_06005 GBR96_18020 GBS02_10665 GBS31_18015 GBS51_18015 GBV48_20440 GBV49_21290 GBV51_16940 GBV59_05205 GBW10_15355 GBW37_21300 GBW40_14450 GBW61_14955 GBW81_14525 GBW91_19925 GBW93_16210 GBW94_20475 GBX02_18175 GBX28_03500 GBX30_16305 GBX44_07655 GBX50_18975 GBX65_09510 GBX79_02640 GBY10_21110 GBY16_20595 GBY22_15800 GBY30_14000 GBY40_12305 GBY43_19015 GBY51_02640 GBY55_13045 GBY69_02100 GBY71_13275 GBY80_15315 GBY98_15310 GBZ02_20775 GBZ07_05340 GBZ09_19665 GBZ19_06355 GBZ20_16245 GBZ21_20920 GBZ57_15255 GBZ88_16205 GBZ96_10620 GCS50_17180 GCY20_17660 GDA07_18585 GDH40_18035 GDI37_18915 GDI50_10605 GDN42_04680 GI500_18260 GI569_18355 GI571_19455 GI574_15255 GI576_17370 GI587_15930 GI598_19450 GI602_19455 GI603_18270 GI605_16665 GI606_17755 GI607_18225 GI610_19850 GI613_18970 GI616_19915 GI617_18250 GI618_19650 GI619_18185 GI623_19925 GI627_19930 GI628_20335 GI635_19450 GI641_19620 GI643_19215 GI648_16180 GI652_19115 GI653_18965 GI656_10830 GI657_16195 GI658_10970 GI661_14545 GI664_14465 GI666_14865 GI667_19440 GI672_16195 GI673_19155 GI678_16820 GI679_18005 GI681_20130 GI682_19670 GI684_16950 GJE23_19345 GJE52_20320 GJE53_18800 GJE57_19140 GJE58_18480 GJE61_19460 GJE63_19120 GJE66_17975 GJE68_19380 GJE69_16935 GJE75_19455 GJE76_19455 GJE78_19465 GJE80_18250 GJE81_19525 GJE83_18265 GJE85_18895 GJE87_17205 GJE88_18245 GJE91_18740 GJE97_17405 GJE99_16230 GJF01_19455 GJF04_19450 GJF05_19445 GJF06_19145 GJF07_16855 GJF11_14795 GJF12_19000 GJF15_18775 GJF17_18765 GJF18_19035 GJF25_18900 GJF26_19420 GJF28_19175 GJF31_18790 GJF33_18960 GJF41_19610 GJF44_19235 GJF47_19445 GJF49_19145 GJF51_20105 GJF54_19450 GJF59_18550 GJF61_19930 GJF63_18475 GJF64_19455 GJF68_18410 GJF69_18870 GJF75_19785 GJF76_19450 GJF77_19140 GJF78_19925 GJF81_16490 GJF83_18960 GJF85_19920 GJF86_18955 GJF88_19445 GJF90_20340 GJF91_20505 GJF93_19465 GJF95_18650 GJF99_17980 GJG01_19920 GJG02_19360 GJG03_14565 GJG05_14715 GJG07_11790 GJG10_16200 GJG11_15865 GJG13_13795 GJG14_16105 GJG15_14705 GJG16_17040 GJG17_14795 GJG18_23365 GJG24_15060 GJG25_15325 GJG26_16315 GJG28_16415 GJG29_14235 GJG30_16180 GJG35_16225 GJG37_15715 GJG38_18655 GJG39_18260 GJG40_14820 GJG45_19440 GJG48_17440 GJG49_18945 GJG51_19455 GJG54_21345 GJG57_19125 GJG58_19175 GJG60_18005 GJG63_17960 GJG66_18105 GJG70_17990 GJG71_16195 GJG76_18470 GJG77_18995 GJG81_16360 GJG84_18715 GNA67_003852 GNA68_003740 GNA89_003109 GNA90_003610 GNA94_003248 GNA95_003605 GNB01_003578 GNB24_003575 GNB30_003635 GNB32_003570 GNB39_003909 GNB51_003077 GNB52_003552 GNB53_003749 GNB87_003935 GNB90_003879 GYI57_002966 GYK12_04750 GYK13_17425 OB33_18235 R841_07660 ZQ07_09565 ZR89_19430 ZW25_11665] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[F10 FX] Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Virus-activating protease) (VAP) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]
[PROS1 PROS] Vitamin K-dependent protein S
[F8 F8C] Coagulation factor VIII (Antihemophilic factor) (AHF) (Procoagulant component) [Cleaved into: Factor VIIIa heavy chain, 200 kDa isoform; Factor VIIIa heavy chain, 92 kDa isoform; Factor VIII B chain; Factor VIIIa light chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[F12] Coagulation factor XII (EC 3.4.21.38) (Hageman factor) (HAF) [Cleaved into: Coagulation factor XIIa heavy chain; Beta-factor XIIa part 1; Coagulation factor XIIa light chain (Beta-factor XIIa part 2)]
[Cfi If] Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain]
[VKORC1 VKOR MSTP134 MSTP576 UNQ308/PRO351] Vitamin K epoxide reductase complex subunit 1 (EC 1.17.4.4) (Vitamin K1 2,3-epoxide reductase subunit 1)
[Masp1 Crarf Masp3] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[CFI IF] Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[F11] Coagulation factor XI (FXI) (EC 3.4.21.27) (Plasma thromboplastin antecedent) (PTA) [Cleaved into: Coagulation factor XIa heavy chain; Coagulation factor XIa light chain]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

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