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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_MOUSE              Reviewed;         460 AA.
P33587; O35498; Q91WN8; Q99PC6;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 2.
12-SEP-2018, entry version 181.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=1618739;
Tada N., Sato M., Tsujimura A., Iwase R., Hashimoto-Gotoh T.;
"Isolation and characterization of a mouse protein C cDNA.";
J. Biochem. 111:491-495(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=9493582;
Jalbert L.R., Rosen E.D., Lissens A., Carmeliet P., Collen D.,
Castellino F.J.;
"Nucleotide structure and characterization of the murine gene encoding
anticoagulant protein C.";
Thromb. Haemost. 79:310-316(1998).
[3]
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6J;
Korf I.;
"Complete sequence of UC72A01.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 274-433.
STRAIN=BALB/cJ;
PubMed=8043441; DOI=10.1111/j.1365-2141.1994.tb04791.x;
Murakawa M., Okamura T., Kamura T., Kuroiwa M., Harada M., Niho Y.;
"A comparative study of partial primary structures of the catalytic
region of mammalian protein C.";
Br. J. Haematol. 86:590-600(1994).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-214.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
-!- 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:0000250}.
-!- 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; D10445; BAA01235.1; -; mRNA.
EMBL; AF034569; AAC33795.1; -; Genomic_DNA.
EMBL; AF318182; AAK07918.1; -; mRNA.
EMBL; BC013896; AAH13896.1; -; mRNA.
EMBL; D43755; BAA07812.1; -; Genomic_DNA.
CCDS; CCDS29116.1; -.
PIR; JX0210; JX0210.
RefSeq; NP_001036232.1; NM_001042767.3.
RefSeq; NP_001300867.1; NM_001313938.1.
RefSeq; XP_011245159.1; XM_011246857.2.
UniGene; Mm.2786; -.
UniGene; Mm.489734; -.
ProteinModelPortal; P33587; -.
STRING; 10090.ENSMUSP00000132226; -.
MEROPS; S01.218; -.
iPTMnet; P33587; -.
PhosphoSitePlus; P33587; -.
MaxQB; P33587; -.
PaxDb; P33587; -.
PeptideAtlas; P33587; -.
PRIDE; P33587; -.
Ensembl; ENSMUST00000171765; ENSMUSP00000132226; ENSMUSG00000024386.
GeneID; 19123; -.
KEGG; mmu:19123; -.
UCSC; uc008eiz.1; mouse.
CTD; 5624; -.
MGI; MGI:97771; Proc.
eggNOG; ENOG410IJRM; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118890; -.
HOGENOM; HOG000251821; -.
HOVERGEN; HBG013304; -.
InParanoid; P33587; -.
KO; K01344; -.
OMA; HTSWVLT; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P33587; -.
TreeFam; TF327329; -.
Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
ChiTaRS; Proc; mouse.
PRO; PR:P33587; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024386; Expressed in 85 organ(s), highest expression level in liver.
CleanEx; MM_PROC; -.
Genevisible; P33587; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0070012; F:oligopeptidase activity; ISO:MGI.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0043621; F:protein self-association; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0007596; P:blood coagulation; IMP:MGI.
GO; GO:0001889; P:liver development; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0030195; P:negative regulation of blood coagulation; IDA:MGI.
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.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0044537; P:regulation of circulating fibrinogen levels; IMP:MGI.
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; 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; 2.
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;
Blood coagulation; Calcium; Cleavage on pair of basic residues;
Complete proteome; 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 18 {ECO:0000255}.
PROPEP 19 41 {ECO:0000250}.
/FTId=PRO_0000028112.
CHAIN 42 460 Vitamin K-dependent protein C.
/FTId=PRO_0000028113.
CHAIN 42 196 Vitamin K-dependent protein C light
chain. {ECO:0000250}.
/FTId=PRO_0000028114.
CHAIN 199 460 Vitamin K-dependent protein C heavy
chain. {ECO:0000250}.
/FTId=PRO_0000028115.
PEPTIDE 199 212 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000028116.
DOMAIN 42 87 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 96 131 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 135 175 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 213 449 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 253 253 Charge relay system.
ACT_SITE 299 299 Charge relay system.
ACT_SITE 401 401 Charge relay system.
SITE 212 213 Cleavage; by thrombin. {ECO:0000250}.
MOD_RES 47 47 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 48 48 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 55 55 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 57 57 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 60 60 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 61 61 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 66 66 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 67 67 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 70 70 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 76 76 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 112 112 (3R)-3-hydroxyaspartate. {ECO:0000250}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 58 63 {ECO:0000250}.
DISULFID 91 110 {ECO:0000250}.
DISULFID 100 105 {ECO:0000250}.
DISULFID 104 119 {ECO:0000250}.
DISULFID 121 130 {ECO:0000250}.
DISULFID 139 150 {ECO:0000250}.
DISULFID 146 159 {ECO:0000250}.
DISULFID 161 174 {ECO:0000250}.
DISULFID 182 319 Interchain (between light and heavy
chains). {ECO:0000255|PROSITE-
ProRule:PRU00076, ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00463}.
DISULFID 238 254 {ECO:0000250}.
DISULFID 372 386 {ECO:0000250}.
DISULFID 397 425 {ECO:0000250}.
VARIANT 327 327 Q -> QQ (in strain: BALB/c).
VARIANT 392 392 D -> N (in strain: BALB/c).
CONFLICT 65 65 F -> L (in Ref. 3; AAK07918).
{ECO:0000305}.
SEQUENCE 460 AA; 51818 MW; 0117F26E68FCC274 CRC64;
MWQFRVFLLL MSTWGISSIP AHPDPVFSSS EHAHQVLRVR RANSFLEEMR PGSLERECME
EICDFEEAQE IFQNVEDTLA FWIKYFDGDQ CSAPPLDHQC DSPCCGHGTC IDGIGSFSCS
CDKGWEGKFC QQELRFQDCR VNNGGCLHYC LEESNGRRCA CAPGYELADD HMRCKSTVNF
PCGKLGRWIE KKRKILKRDT DLEDELEPDP RIVNGTLTKQ GDSPWQAILL DSKKKLACGG
VLIHTSWVLT AAHCVEGTKK LTVRLGEYDL RRRDHWELDL DIKEILVHPN YTRSSSDNDI
ALLRLAQPAT LSKTIVPICL PNNGLAQELT QAGQETVVTG WGYQSDRIKD GRRNRTFILT
FIRIPLVARN ECVEVMKNVV SENMLCAGII GDTRDACDGD SGGPMVVFFR GTWFLVGLVS
WGEGCGHTNN YGIYTKVGSY LKWIHSYIGE KGVSLKSQKL


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