(data stored in ACNUC19913 zone)

HOGENOM: HS2_PE3273

ID   HS2_PE3273                           STANDARD;      PRT;   461 AA.
AC   HS2_PE3273; P04070; Q15189; Q15190; Q16001; Q53S74; Q9UC55;
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; (HS2.PE3273).
GN   Name=PROC;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS2.PE3273.
CC       Homo sapiens chromosome 2 GRCh37  sequence 1..243189373 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:PROC_HUMAN
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   -!- INTERACTION:
CC       P51511:MMP15; NbExp=2; IntAct=EBI-1383018, EBI-1383043;
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: Partial (70%) N-glycosylation of Asn-371 with an atypical N-
CC       X-C site produces a higher molecular weight form referred to as
CC       alpha. The lower molecular weight form, not glycosylated at Asn-
CC       371, is beta.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC   -!- DISEASE: Defects in PROC are the cause of protein C deficiency
CC       autosomal dominant (ADPROCD) [MIM:176860]. ADPROCD is a cause of
CC       hereditary thrombophilia, a hemostatic disorder characterized by
CC       impaired regulation of blood coagulation and a tendency to
CC       recurrent venous thrombosis. However, many adults with
CC       heterozygous disease may be asymptomatic. Individuals with
CC       decreased amounts of protein C are classically referred to as
CC       having type I protein C deficiency and those with normal amounts
CC       of a functionally defective protein as having type II deficiency.
CC   -!- DISEASE: Defects in PROC are the cause of protein C deficiency
CC       autosomal recessive (ARPROCD) [MIM:612304]. ARPROCD results in a
CC       thrombotic condition that can manifest as a severe neonatal
CC       disorder or as a milder disorder with late-onset thrombophilia.
CC       The severe form leads to neonatal death through massive neonatal
CC       venous thrombosis. Often associated with ecchymotic skin lesions
CC       which can turn necrotic called purpura fulminans, this disorder is
CC       very rare.
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   -!- SEQUENCE CAUTION:
CC       Sequence=S76088; Type=Erroneous termination; Positions=151; Note=Translated as Cys;
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Protein C entry;
CC       URL="http://en.wikipedia.org/wiki/Protein_C";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PROC";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/proc/";
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000115718;ENST00000234071;ENSP00000234071.
DR   EMBL; AB083693; - ;
DR   EMBL; AB083695; - ;
DR   EMBL; AB083696; - ;
DR   EMBL; AB083697; - ;
DR   EMBL; AB083698; - ;
DR   EMBL; AB083699; - ;
DR   EMBL; AB083700; - ;
DR   EMBL; AB086849; - ;
DR   EMBL; AB086850; - ;
DR   EMBL; AB086851; - ;
DR   EMBL; AB086852; - ;
DR   EMBL; AC068282; - ;
DR   EMBL; AF378903; - ;
DR   EMBL; AK298280; - ;
DR   EMBL; AY348553; - ;
DR   EMBL; AY348554; - ;
DR   EMBL; AY454079; - ;
DR   EMBL; BC034377; - ;
DR   EMBL; CH471103; - ;
DR   EMBL; K02059; - ;
DR   EMBL; M11228; - ;
DR   EMBL; M12683; - ;
DR   EMBL; M12684; - ;
DR   EMBL; M12685; - ;
DR   EMBL; M12686; - ;
DR   EMBL; M12687; - ;
DR   EMBL; M12712; - ;
DR   EMBL; S58668; - ;
DR   EMBL; S76088; - ;
DR   EMBL; S76090; - ;
DR   EMBL; X02750; - ;
DR   UniProtKB/Swiss-Prot; P04070; Q15189; Q15190; Q16001; Q53S74; Q9UC55; -.
DR   EMBL; X02750; CAA26528.1; -; mRNA.
DR   EMBL; M11228; AAA60166.1; -; Genomic_DNA.
DR   EMBL; M12712; AAA60165.1; -; Genomic_DNA.
DR   EMBL; M12683; AAA60165.1; JOINED; Genomic_DNA.
DR   EMBL; M12684; AAA60165.1; JOINED; Genomic_DNA.
DR   EMBL; M12685; AAA60165.1; JOINED; Genomic_DNA.
DR   EMBL; M12686; AAA60165.1; JOINED; Genomic_DNA.
DR   EMBL; M12687; AAA60165.1; JOINED; Genomic_DNA.
DR   EMBL; AF378903; AAK56377.1; -; Genomic_DNA.
DR   EMBL; AC068282; AAY15044.1; -; Genomic_DNA.
DR   EMBL; CH471103; EAW95320.1; -; Genomic_DNA.
DR   EMBL; BC034377; AAH34377.1; -; mRNA.
DR   EMBL; S58668; AAB26335.1; -; Genomic_DNA.
DR   EMBL; K02059; AAA60164.1; -; mRNA.
DR   EMBL; S76088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S76090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00021817; -.
DR   PIR; A22331; KXHU.
DR   RefSeq; NP_000303.1; NM_000312.3.
DR   UniGene; Hs.224698; -.
DR   PDB; 1AUT; X-ray; 2.80 A; C=212-461, L=84-197.
DR   PDB; 1LQV; X-ray; 1.60 A; C/D=43-75.
DR   PDB; 1PCU; Model; -; A=175-450.
DR   PDB; 2PCT; Model; -; A=175-450.
DR   PDB; 3F6U; X-ray; 2.80 A; H=212-451, L=91-188.
DR   PDB; 3JTC; X-ray; 1.60 A; C/D=43-75.
DR   PDBsum; 1AUT; -.
DR   PDBsum; 1LQV; -.
DR   PDBsum; 1PCU; -.
DR   PDBsum; 2PCT; -.
DR   PDBsum; 3F6U; -.
DR   PDBsum; 3JTC; -.
DR   ProteinModelPortal; P04070; -.
DR   SMR; P04070; 43-457.
DR   IntAct; P04070; 1.
DR   STRING; P04070; -.
DR   MEROPS; S01.218; -.
DR   GlycoSuiteDB; P04070; -.
DR   PeptideAtlas; P04070; -.
DR   PRIDE; P04070; -.
DR   Ensembl; ENST00000234071; ENSP00000234071; ENSG00000115718.
DR   GeneID; 5624; -.
DR   KEGG; hsa:5624; -.
DR   UCSC; uc002tok.1; human.
DR   CTD; 5624; -.
DR   GeneCards; GC02P120483; -.
DR   H-InvDB; HIX0002434; -.
DR   HGNC; HGNC:9451; PROC.
DR   HPA; CAB016721; -.
DR   HPA; CAB016792; -.
DR   HPA; HPA005550; -.
DR   MIM; 176860; phenotype.
DR   MIM; 188050; phenotype.
DR   MIM; 612283; gene.
DR   MIM; 612304; phenotype.
DR   neXtProt; NX_P04070; -.
DR   Orphanet; 745; Hereditary thrombophilia due to congenital protein C deficiency.
DR   PharmGKB; PA33799; -.
DR   eggNOG; prNOG07393; -.
DR   PhylomeDB; P04070; -.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   Reactome; REACT_604; Hemostasis.
DR   DrugBank; DB00025; Antihemophilic Factor.
DR   DrugBank; DB00055; Drotrecogin alfa.
DR   DrugBank; DB00170; Menadione.
DR   DrugBank; DB00464; Sodium Tetradecyl Sulfate.
DR   NextBio; 21860; -.
DR   PMAP-CutDB; P04070; -.
DR   ArrayExpress; P04070; -.
DR   Bgee; P04070; -.
DR   CleanEx; HS_PROC; -.
DR   Genevestigator; P04070; -.
DR   GermOnline; ENSG00000115718; Homo sapiens.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; EXP:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:UniProtKB.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; TAS:UniProtKB.
DR   GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
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; HS2.PE3273; -.
KW   ENSG000001157181755old_1320000031; ENSP000002340717901old_1320000031;
KW   B4DPC8_HUMAN; Q6SPC0_HUMAN; Q6V7X8_HUMAN; Q6V7X9_HUMAN; Q8IXB4_HUMAN;
KW   Q8IXB6_HUMAN; Q8IXB7_HUMAN; Q8J002_HUMAN; Q8J003_HUMAN; Q8J004_HUMAN;
KW   Q8J006_HUMAN; Q8J007_HUMAN; Q8J008_HUMAN; AB083693; AB083695; AB083696;
KW   AB083698; AB083699; AB083700; AB086849; AB086850; AB086851; AB086852;
KW   AF378903; AK298280; AY348553; AY348554; AY454079; BC034377; CH471103;
KW   M11228; M12683; M12684; M12685; M12686; M12687; M12712; S58668; S76088;
KW   X02750;
KW   3D-structure; Blood coagulation; Calcium;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase;
KW   Hydroxylation; Polymorphism; Protease; Reference proteome; Repeat;
KW   Serine protease; Signal; Thrombophilia; Zymogen.
SQ   SEQUENCE   461 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MWQLTSLLLF VATWGISGTP APLDSVFSSS ERAHQVLRIR KRANSFLEEL RHSSLERECI
     EEICDFEEAK EIFQNVDDTL AFWSKHVDGD QCLVLPLEHP CASLCCGHGT CIDGIGSFSC
     DCRSGWEGRF CQREVSFLNC SLDNGGCTHY CLEEVGWRRC SCAPGYKLGD DLLQCHPAVK
     FPCGRPWKRM EKKRSHLKRD TEDQEDQVDP RLIDGKMTRR GDSPWQVVLL DSKKKLACGA
     VLIHPSWVLT AAHCMDESKK LLVRLGEYDL RRWEKWELDL DIKEVFVHPN YSKSTTDNDI
     ALLHLAQPAT LSQTIVPICL PDSGLAEREL NQAGQETLVT GWGYHSSREK EAKRNRTFVL
     NFIKIPVVPH NECSEVMSNM VSENMLCAGI LGDRQDACEG DSGGPMVASF HGTWFLVGLV
     SWGEGCGLLH NYGVYTKVSR YLDWIHGHIR DKEAPQKSWA P
//

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