ID   PROC_HORSE              Reviewed;         157 AA.
AC   Q28380;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Vitamin K-dependent protein C;
DE            EC=3.4.21.69;
DE   AltName: Full=Autoprothrombin IIA;
DE   AltName: Full=Anticoagulant protein C;
DE   AltName: Full=Blood coagulation factor XIV;
DE   Flags: Fragment;
GN   Name=PROC;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94318474; PubMed=8043441;
RX   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
RT   region 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
CC       in the presence of calcium ions and phospholipids.
CC   -!- CATALYTIC ACTIVITY: Degradation of blood coagulation factors Va
CC       and VIIIa.
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR   EMBL; D43753; BAA07810.1; -; Genomic_DNA.
DR   HSSP; P04070; 1AUT.
DR   SMR; Q28380; 1-157.
DR   MEROPS; S01.218; -.
DR   Ensembl; ENSECAG00000016570; Equus caballus.
DR   HOVERGEN; Q28380; -.
DR   BRENDA; 3.4.21.69; 1464.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; PARTIAL.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Serine protease.
FT   CHAIN        <1   >157       Vitamin K-dependent protein C.
FT                                /FTId=PRO_0000088710.
FT   DOMAIN       <1   >157       Peptidase S1.
FT   ACT_SITE     26     26       Charge relay system.
FT   ACT_SITE    125    125       Charge relay system.
FT   CARBOHYD     17     17       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   DISULFID     96    110       By similarity.
FT   DISULFID    121    149       By similarity.
FT   NON_TER       1      1
FT   NON_TER     157    157
SQ   SEQUENCE   157 AA;  17200 MW;  BFAA6EA045C3C580 CRC64;
     ENGEVDLDIQ EVIMHPNYSK SSSDNDIALL RLARPATFSQ TIVPICLPDS GLSERELTQA
     GQETVVTGWG YRSETKRNRT FVLNFIKVPV VPHSECVRTM HNLVSENMLC AGILGDTRDA
     CEGDSGGPMV ASFRGTWFLV GLVSWGEGCG RLHNYGV
//