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 27-MAR-2024, entry version 98.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D43752; BAA07809.1; -; Genomic_DNA.
DR AlphaFoldDB; Q28315; -.
DR SMR; Q28315; -.
DR STRING; 9925.ENSCHIP00000019993; -.
DR MEROPS; S01.218; -.
DR GlyCosmos; Q28315; 2 sites, No reported glycans.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR Proteomes; UP000694566; Unplaced.
DR Proteomes; UP000694900; Genome assembly.
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; Trypsin-like serine proteases; 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 PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR PANTHER; PTHR24278:SF0; VITAMIN K-DEPENDENT PROTEIN C; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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
//
