ID   PROC_CAPHI              Reviewed;         157 AA.
AC   Q28315;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Vitamin K-dependent protein C;
DE            EC=3.4.21.69;
DE   AltName: Full=Anticoagulant protein C;
DE   AltName: Full=Autoprothrombin IIA;
DE   AltName: Full=Blood coagulation factor XIV;
DE   Flags: Fragment;
GN   Name=PROC;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8043441; DOI=10.1111/j.1365-2141.1994.tb04791.x;
RA   Murakawa M., Okamura T., Kamura T., Kuroiwa M., Harada M., Niho Y.;
RT   "A comparative study of partial primary structures of the catalytic region
RT   of mammalian protein C.";
RL   Br. J. Haematol. 86:590-600(1994).
CC   -!- FUNCTION: Protein C is a vitamin K-dependent serine protease that
CC       regulates blood coagulation by inactivating factors Va and VIIIa in the
CC       presence of calcium ions and phospholipids. Exerts a protective effect
CC       on the endothelial cell barrier function.
CC       {ECO:0000250|UniProtKB:P04070}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Degradation of blood coagulation factors Va and VIIIa.;
CC         EC=3.4.21.69;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04070}. Golgi
CC       apparatus {ECO:0000250|UniProtKB:P04070}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P04070}.
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; D43752; BAA07809.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q28315; -.
DR   SMR; Q28315; -.
DR   STRING; 9925.ENSCHIP00000019993; -.
DR   MEROPS; S01.218; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0050819; P:negative regulation of coagulation; ISS:UniProtKB.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   Golgi apparatus; Hemostasis; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease.
FT   CHAIN           <1..>157
FT                   /note="Vitamin K-dependent protein C"
FT                   /id="PRO_0000088708"
FT   DOMAIN          <1..>157
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        26
FT                   /note="Charge relay system"
FT   ACT_SITE        125
FT                   /note="Charge relay system"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        96..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        121..149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         1
FT   NON_TER         157
SQ   SEQUENCE   157 AA;  17251 MW;  B89790F9954B610A CRC64;
     ESWEVDLDIK EVIVRPNYTK STSDNDIALL HLAKPATLSQ TIVPICLPDS GLSERKLTQV
     GQETVVTGWG YRDETKKNRT SILNFIKIPV VSYNACVHAM ENKVSENMLC AGILGNPRDA
     CEGDSGGPMV TFFRGTWFLV GLVSWGEGCG RLNNYGI