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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] (Fragment)

 PROC_BOVIN              Reviewed;         456 AA.
P00745;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
28-MAR-2018, entry version 156.
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; Fragment;
Name=PROC;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6091100; DOI=10.1073/pnas.81.18.5653;
Long G.L., Balagaje R.M., McGillivray R.T.A.;
"Cloning and sequencing of liver cDNA coding for bovine protein C.";
Proc. Natl. Acad. Sci. U.S.A. 81:5653-5656(1984).
[2]
PROTEIN SEQUENCE OF 40-194, GLYCOSYLATION AT ASN-136, HYDROXYLATION AT
ASP-110, AND GAMMA-CARBOXYGLUTAMATION AT GLU-45; GLU-46; GLU-53;
GLU-55; GLU-58; GLU-59; GLU-62; GLU-64; GLU-65; GLU-68 AND GLU-74.
PubMed=6896876;
Fernlund P., Stenflo J.;
"Amino acid sequence of the light chain of bovine protein C.";
J. Biol. Chem. 257:12170-12179(1982).
[3]
SEQUENCE REVISION TO 110.
PubMed=6572939; DOI=10.1073/pnas.80.7.1802;
Drakenberg T., Fernlund P., Roepstorff P., Stenflo J.;
"Beta-hydroxyaspartic acid in vitamin K-dependent protein C.";
Proc. Natl. Acad. Sci. U.S.A. 80:1802-1806(1983).
[4]
PROTEIN SEQUENCE OF 197-456, AND GLYCOSYLATION AT ASN-289; ASN-350 AND
ASN-366.
PubMed=6896877;
Stenflo J., Fernlund P.;
"Amino acid sequence of the heavy chain of bovine protein C.";
J. Biol. Chem. 257:12180-12190(1982).
[5]
PROTEOLYTIC PROCESSING, AND CALCIUM-BINDING.
PubMed=6304092;
Esmon N.L., Debault L.E., Esmon C.T.;
"Proteolytic formation and properties of gamma-carboxyglutamic acid-
domainless protein C.";
J. Biol. Chem. 258:5548-5553(1983).
[6]
PROTEOLYTIC PROCESSING, AND CALCIUM-BINDING DATA.
PubMed=6406503;
Johnson A.E., Esmon N.L., Laue T.M., Esmon C.T.;
"Structural changes required for activation of protein C are induced
by Ca2+ binding to a high affinity site that does not contain gamma-
carboxyglutamic acid.";
J. Biol. Chem. 258:5554-5560(1983).
-!- 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. Exerts a
protective effect on the endothelial cell barrier function.
{ECO:0000250|UniProtKB:P04070}.
-!- CATALYTIC ACTIVITY: Degradation of blood coagulation factors Va
and VIIIa.
-!- 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.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04070}.
Golgi apparatus {ECO:0000250|UniProtKB:P04070}. Endoplasmic
reticulum {ECO:0000250|UniProtKB:P04070}.
-!- 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: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000269|PubMed:6896876}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; K02435; AAA30685.1; -; mRNA.
PIR; A26250; KXBO.
UniGene; Bt.49146; -.
ProteinModelPortal; P00745; -.
STRING; 9913.ENSBTAP00000005163; -.
MEROPS; S01.218; -.
iPTMnet; P00745; -.
PaxDb; P00745; -.
PRIDE; P00745; -.
eggNOG; ENOG410IJRM; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000251821; -.
HOVERGEN; HBG013304; -.
InParanoid; P00745; -.
SABIO-RK; P00745; -.
PMAP-CutDB; P00745; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0030195; P:negative regulation of blood coagulation; IBA:GO_Central.
GO; GO:0050819; P:negative regulation of coagulation; ISS:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISS:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR012224; Pept_S1A_FX.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; 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; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Blood coagulation; Calcium; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Disulfide bond;
EGF-like domain; Endoplasmic reticulum; Gamma-carboxyglutamic acid;
Glycoprotein; Golgi apparatus; Hemostasis; Hydrolase; Hydroxylation;
Protease; Reference proteome; Repeat; Secreted; Serine protease;
Signal; Zymogen.
SIGNAL <1 15 {ECO:0000255}.
PROPEP 16 39 {ECO:0000269|PubMed:6896876}.
/FTId=PRO_0000028098.
CHAIN 40 456 Vitamin K-dependent protein C.
/FTId=PRO_0000028099.
CHAIN 40 194 Vitamin K-dependent protein C light
chain.
/FTId=PRO_0000028100.
CHAIN 197 456 Vitamin K-dependent protein C heavy
chain.
/FTId=PRO_0000028101.
PEPTIDE 197 210 Activation peptide.
/FTId=PRO_0000028102.
DOMAIN 40 85 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 94 129 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 133 173 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 211 445 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 252 252 Charge relay system.
ACT_SITE 298 298 Charge relay system.
ACT_SITE 397 397 Charge relay system.
MOD_RES 45 45 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 46 46 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 53 53 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 55 55 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 58 58 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 59 59 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 62 62 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 64 64 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 65 65 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 68 68 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 74 74 4-carboxyglutamate. {ECO:0000255|PROSITE-
ProRule:PRU00463,
ECO:0000269|PubMed:6896876}.
MOD_RES 110 110 (3R)-3-hydroxyaspartate.
{ECO:0000269|PubMed:6896876}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:6896876}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:6896877}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:6896877}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine;
atypical; partial.
{ECO:0000269|PubMed:6896877}.
DISULFID 56 61 {ECO:0000250}.
DISULFID 89 108 {ECO:0000250}.
DISULFID 98 103 {ECO:0000250}.
DISULFID 102 117 {ECO:0000250}.
DISULFID 119 128 {ECO:0000250}.
DISULFID 137 148 {ECO:0000250}.
DISULFID 144 157 {ECO:0000250}.
DISULFID 159 172 {ECO:0000250}.
DISULFID 180 318 Interchain (between light and heavy
chains).
DISULFID 237 253
DISULFID 368 382
DISULFID 393 421
VARIANT 82 82 F -> K.
CONFLICT 455 456 VP -> PV (in Ref. 4; AA sequence).
{ECO:0000305}.
NON_TER 1 1
SEQUENCE 456 AA; 51409 MW; CAAF6833F894C209 CRC64;
XTSLLLFVTI WGISSTPAPP DSVFSSSQRA HQVLRIRKRA NSFLEELRPG NVERECSEEV
CEFEEAREIF QNTEDTMAFW SFYSDGDQCE DRPSGSPCDL PCCGRGKCID GLGGFRCDCA
EGWEGRFCLH EVRFSNCSAE NGGCAHYCME EEGRRHCSCA PGYRLEDDHQ LCVSKVTFPC
GRLGKRMEKK RKTLKRDTNQ VDQKDQLDPR IVDGQEAGWG ESPWQAVLLD SKKKLVCGAV
LIHVSWVLTV AHCLDSRKKL IVRLGEYDMR RWESWEVDLD IKEVIIHPNY TKSTSDNDIA
LLRLAKPATL SQTIVPICLP DSGLSERKLT QVGQETVVTG WGYRDETKRN RTFVLSFIKV
PVVPYNACVH AMENKISENM LCAGILGDPR DACEGDSGGP MVTFFRGTWF LVGLVSWGEG
CGRLYNYGVY TKVSRYLDWI YGHIKAQEAP LESQVP


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