(data stored in ACNUC19913 zone)

HOGENOM: MOUSE18_PE294

ID   MOUSE18_PE294                        STANDARD;      PRT;   460 AA.
AC   MOUSE18_PE294; P33587; O35498; Q91WN8; Q99PC6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Vitamin K-dependent protein C; EC=3.4.21 69;AltName:
DE   Full=Anticoagulant protein C;AltName: Full=Autoprothrombin IIA;AltName:
DE   Full=Blood coagulation factor XIV;Contains: RecName: Full=Vitamin
DE   K-dependent protein C light chain;Contains: RecName: Full=Vitamin
DE   K-dependent protein C heavy chain;Contains: RecName: Full=Activation
DE   peptide;Flags: Precursor; (MOUSE18.PE294).
GN   Name=Proc;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE18.PE294.
CC       Mus musculus chromosome 18 NCBIM37  sequence 1..90772031 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:PROC_MOUSE
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   -!- 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   -!- 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       (By similarity).
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   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000024386;ENSMUST00000025245;ENSMUSP00000025245.
DR   EMBL; AF034569; - ;
DR   EMBL; AF318182; - ;
DR   EMBL; BC013896; - ;
DR   EMBL; D10445; - ;
DR   EMBL; D43755; - ;
DR   UniProtKB/Swiss-Prot; P33587; O35498; Q91WN8; Q99PC6; -.
DR   EMBL; D10445; BAA01235.1; -; mRNA.
DR   EMBL; AF034569; AAC33795.1; -; Genomic_DNA.
DR   EMBL; AF318182; AAK07918.1; -; mRNA.
DR   EMBL; BC013896; AAH13896.1; -; mRNA.
DR   EMBL; D43755; BAA07812.1; -; Genomic_DNA.
DR   IPI; IPI00113750; -.
DR   PIR; JX0210; JX0210.
DR   RefSeq; NP_001036232.1; NM_001042767.1.
DR   RefSeq; NP_001036233.1; NM_001042768.1.
DR   RefSeq; NP_032960.2; NM_008934.2.
DR   UniGene; Mm.2786; -.
DR   ProteinModelPortal; P33587; -.
DR   SMR; P33587; 46-87, 90-184, 212-448.
DR   STRING; P33587; -.
DR   MEROPS; S01.218; -.
DR   PRIDE; P33587; -.
DR   Ensembl; ENSMUST00000025245; ENSMUSP00000025245; ENSMUSG00000024386.
DR   Ensembl; ENSMUST00000171765; ENSMUSP00000132226; ENSMUSG00000024386.
DR   GeneID; 19123; -.
DR   KEGG; mmu:19123; -.
DR   NMPDR; fig|10090.3.peg.3736; -.
DR   UCSC; uc008eiz.1; mouse.
DR   CTD; 5624; -.
DR   MGI; MGI:97771; Proc.
DR   eggNOG; roNOG10647; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; P33587; -.
DR   OMA; GDSPWQV; -.
DR   OrthoDB; EOG43BMNX; -.
DR   PhylomeDB; P33587; -.
DR   NextBio; 295718; -.
DR   ArrayExpress; P33587; -.
DR   Bgee; P33587; -.
DR   CleanEx; MM_PROC; -.
DR   Genevestigator; P33587; -.
DR   GermOnline; ENSMUSG00000024386; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; IDA:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Gene3D; G3DSA:4.10.740.10; Coagulation_factor_Gla; 1.
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; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR   SUPFAM; SSF57630; VitK_dep_GLA; 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.
DR   HOGENOMDNA; MOUSE18.PE294; -.
KW   ENSMUSG000000243865old_1320000031; ENSMUSP000000252451old_1320000031;
KW   AF034569; AF318182; BC013896; D10445; D43755;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation;
KW   Protease; Reference proteome; Repeat; Serine protease; Signal;
KW   Zymogen.
SQ   SEQUENCE   460 AA;  UNKNOWN MW;  UNKNOWN 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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