(data stored in ACNUC19913 zone)

HOGENOM: BOVIN2_6_PE9

ID   BOVIN2_6_PE9                         STANDARD;      PRT;   459 AA.
AC   BOVIN2_6_PE9; P00745;
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; Fragment; (BOVIN2_6.PE9).
GN   Name=PROC;
OS   BOS TAURUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BOVIN2_6.PE9.
CC       Bos taurus chromosome 2 Btau_4.0 partial sequence 4913708..5913707
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:PROC_BOVIN
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   -!- 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:Bos_taurus;ENSBTAG00000003950;ENSBTAT00000005163;ENSBTAP00000005163.
DR   EMBL; K02435; - ;
DR   UniProtKB/Swiss-Prot; P00745; -.
DR   EMBL; K02435; AAA30685.1; -; mRNA.
DR   IPI; IPI00713247; -.
DR   PIR; A26250; KXBO.
DR   UniGene; Bt.49146; -.
DR   ProteinModelPortal; P00745; -.
DR   SMR; P00745; 41-85, 88-183, 211-445.
DR   STRING; P00745; -.
DR   MEROPS; S01.218; -.
DR   PRIDE; P00745; -.
DR   eggNOG; maNOG17466; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; P00745; -.
DR   OrthoDB; EOG43BMNX; -.
DR   PMAP-CutDB; P00745; -.
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:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
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; PF00008; EGF; 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; 2.
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; FALSE_NEG.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   HOGENOMDNA; BOVIN2_6.PE9; -.
KW   ENSBTAG00000003950fold_1320000031; ENSBTAP00000005163fold_1320000031;
KW   K02435;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase;
KW   Hydroxylation; Protease; Reference proteome; Repeat; Serine protease;
KW   Signal; Zymogen.
SQ   SEQUENCE   459 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MWQLTSLLLF VTIWGISSTP APPDSVFSSS QRAHQVLRIR KRANSFLEEL RPGNVERECS
     EEVCEFEEAR EIFQNTEDTM AFWSKYSDGD QCEDRPSGSP CDLPCCGRGK CIDGLGGFRC
     DCAEGWEGRF CLHEVRFSNC SAENGGCAHY CMEEEGRRHC SCAPGYRLED DHQLCVSKVT
     FPCGRLGKRM EKKRKTLKRD TNQVDQKDQL DPRIVDGQEA GWGESPWQAV LLDSKKKLVC
     GAVLIHVSWV LTVAHCLDSR KKLIVRLGEY DMRRWESWEV DLDIKEVIIH PNYTKSTSDN
     DIALLRLAKP ATLSQTIVPI CLPDSGLSER KLTQVGQETV VTGWGYRDET KRNRTFVLSF
     IKVPVVPYNA CVHAMENKIS ENMLCAGILG DPRDACEGDS GGPMVTFFRG TWFLVGLVSW
     GEGCGRLYNY GVYTKVSRYL DWIYGHIKAQ EAPLESQVP
//

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