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Database: UniProt
Entry: P31394
LinkDB: P31394
Original site: P31394 
ID   PROC_RAT                Reviewed;         461 AA.
AC   P31394;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   16-JAN-2019, entry version 162.
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   Contains:
DE     RecName: Full=Vitamin K-dependent protein C light chain;
DE   Contains:
DE     RecName: Full=Vitamin K-dependent protein C heavy chain;
DE   Contains:
DE     RecName: Full=Activation peptide;
DE   Flags: Precursor;
GN   Name=Proc;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=1627650; DOI=10.1016/0167-4781(92)90035-X;
RA   Okafuji T., Maekawa K., Nawa K., Marumoto Y.;
RT   "The cDNA cloning and mRNA expression of rat protein C.";
RL   Biochim. Biophys. Acta 1131:329-332(1992).
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. Exerts a
CC       protective effect 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   -!- SUBUNIT: Synthesized as a single chain precursor, which is cleaved
CC       into a light chain and a heavy chain held together by a disulfide
CC       bond. The enzyme is then activated by thrombin, which cleaves a
CC       tetradecapeptide from the amino end of the heavy chain; this
CC       reaction, which occurs at the surface of endothelial cells, is
CC       strongly promoted by thrombomodulin.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04070}.
CC       Golgi apparatus {ECO:0000250|UniProtKB:P04070}. Endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:P04070}.
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some Glu
CC       residues allows the modified protein to bind calcium.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Calcium also binds, with stronger affinity to
CC       another site, beyond the GLA domain. This GLA-independent binding
CC       site is necessary for the recognition of the thrombin-
CC       thrombomodulin complex.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; X64336; CAA45617.1; -; mRNA.
DR   PIR; S18994; S18994.
DR   RefSeq; NP_036935.1; NM_012803.1.
DR   UniGene; Rn.91064; -.
DR   ProteinModelPortal; P31394; -.
DR   SMR; P31394; -.
DR   STRING; 10116.ENSRNOP00000019596; -.
DR   MEROPS; S01.218; -.
DR   PhosphoSitePlus; P31394; -.
DR   PaxDb; P31394; -.
DR   PRIDE; P31394; -.
DR   GeneID; 25268; -.
DR   KEGG; rno:25268; -.
DR   UCSC; RGD:3411; rat.
DR   CTD; 5624; -.
DR   RGD; 3411; Proc.
DR   eggNOG; ENOG410IJRM; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P31394; -.
DR   KO; K01344; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P31394; -.
DR   PRO; PR:P31394; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0070012; F:oligopeptidase activity; IDA:RGD.
DR   GO; GO:0043621; F:protein self-association; IDA:RGD.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; IDA:RGD.
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; IDA:RGD.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Gamma-carboxyglutamic acid; Glycoprotein;
KW   Golgi apparatus; Hemostasis; Hydrolase; Hydroxylation; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   PROPEP       19     41       {ECO:0000250}.
FT                                /FTId=PRO_0000028127.
FT   CHAIN        42    461       Vitamin K-dependent protein C.
FT                                /FTId=PRO_0000028128.
FT   CHAIN        42    196       Vitamin K-dependent protein C light
FT                                chain. {ECO:0000250}.
FT                                /FTId=PRO_0000028129.
FT   CHAIN       199    461       Vitamin K-dependent protein C heavy
FT                                chain. {ECO:0000250}.
FT                                /FTId=PRO_0000028130.
FT   PEPTIDE     199    212       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000028131.
FT   DOMAIN       42     87       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       96    131       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      135    175       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      213    450       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    254    254       Charge relay system.
FT   ACT_SITE    300    300       Charge relay system.
FT   ACT_SITE    402    402       Charge relay system.
FT   SITE        212    213       Cleavage; by thrombin. {ECO:0000250}.
FT   MOD_RES      47     47       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00745,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      48     48       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00745,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      55     55       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00745,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      57     57       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00745,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      60     60       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00745,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      61     61       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00745,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      66     66       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00745,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      67     67       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00745,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      70     70       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00745,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      76     76       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00745,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES     112    112       (3R)-3-hydroxyaspartate. {ECO:0000250}.
FT   CARBOHYD    215    215       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    291    291       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    355    355       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     58     63       {ECO:0000250}.
FT   DISULFID     91    110       {ECO:0000250}.
FT   DISULFID    100    105       {ECO:0000250}.
FT   DISULFID    104    119       {ECO:0000250}.
FT   DISULFID    121    130       {ECO:0000250}.
FT   DISULFID    139    150       {ECO:0000250}.
FT   DISULFID    146    159       {ECO:0000250}.
FT   DISULFID    161    174       {ECO:0000250}.
FT   DISULFID    182    320       Interchain (between light and heavy
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DISULFID    239    255       {ECO:0000250}.
FT   DISULFID    373    387       {ECO:0000250}.
FT   DISULFID    398    426       {ECO:0000250}.
SQ   SEQUENCE   461 AA;  51912 MW;  8A4CF93664EDACD5 CRC64;
     MWQFRIFLLF ASTWGISGVS AHPDPVFSSS EGAHQVLRVR RANSFLEEVR AGSLERECME
     EICDFEEAQE IFQNVEDTLA FWIKYFDGDQ CSTPPLDHQC DSPCCGHGTC IDGLGGFSCS
     CDKGWEGRFC QQEMGFQDCR VKNGGCYHYC LEETRGRRCR CAPGYELADD HMHCRPTVNF
     PCGKLWKRTD KKRKNFKRDI DPEDEELELG PRIVNGTLTK QGDSPWQAIL LDSKKKLACG
     GVLIHTSWVL TAAHCLESSK KLTVRLGEYD LRRRDPWELD LDIKEVLVHP NYTRSNSDND
     IALLRLSQPA TLSKTIVPIC LPNSGLAQEL SQAGQETVVT GWGYQSDKVK DGRRNRTFIL
     TFIRIPLAAR NDCMQVMNNV VSENMLCAGI IGDTRDACDG DSGGPMVVFF RGTWFLVGLV
     SWGEGCGHLN NYGVYTKVGS YLKWIHSYIG ERDVSLKSPK L
//
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