(data stored in ACNUC3659 zone)

HOVERGEN: PROC_CANFA

ID   PROC_CANFA              Reviewed;         456 AA.
AC   Q28278; Q9TTR0;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   22-SEP-2009, entry version 78.
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   Contains:
DE     RecName: Full=Vitamin K-dependent protein C light chain;
DE   Contains:
DE     RecName: Full=Vitamin K-dependent protein C heavy chain;
DE   Flags: Precursor;
GN   Name=PROC;
OS   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9922393; DOI=10.1007/s003359900958;
RA   Leeb T., Kopp T., Deppe A., Breen M., Matis U., Brunnberg L.,
RA   Brenig B.;
RT   "Molecular characterization and chromosomal assignment of the canine
RT   protein C gene.";
RL   Mamm. Genome 10:134-139(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 273-429.
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   -!- 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 (By similarity).
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.
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CC   -!- GENE_FAMILY: HBG013304 [ FAMILY / ALN / TREE ]
DR   EMBL; AJ001979; CAA05126.1; -; Genomic_DNA.
DR   EMBL; D43751; BAA07808.1; -; Genomic_DNA.
DR   RefSeq; NP_001013871.1; -.
DR   UniGene; Cfa.6331; -.
DR   HSSP; P04070; 1AUT.
DR   SMR; Q28278; 91-186, 211-445.
DR   STRING; Q28278; -.
DR   MEROPS; S01.218; -.
DR   GeneID; 476104; -.
DR   KEGG; cfa:476104; -.
DR   CTD; 476104; -.
DR   HOVERGEN; Q28278; -.
DR   BRENDA; 3.4.21.69; 463.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
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; IPR002383; Coagulation_factor_Gla.
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; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00008; EGF; 2.
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   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;
DR   PRODOM; Q28278.
DR   SWISS-2DPAGE; Q28278.
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid;
KW   Glycoprotein; Hydrolase; Hydroxylation; Protease; Repeat;
KW   Serine protease; Signal; Zymogen.
FT   DOMAIN        1     41       PRODOM:2005.1:PD012340  5
FT   DOMAIN       43     94       PRODOM:2005.1:PD325296  86
FT   DOMAIN      104    132       PRODOM:2005.1:PD007207  861
FT   DOMAIN      210    252       PRODOM:2005.1:PD474467  1445
FT   DOMAIN      262    302       PRODOM:2005.1:PD331626  438
FT   DOMAIN      304    342       PRODOM:2005.1:PD746656  20
FT   DOMAIN      345    393       PRODOM:2005.1:PD860006  8
FT   DOMAIN      396    440       PRODOM:2005.1:PD000068  1525
FT   SIGNAL        1     20       Potential.
FT   PROPEP       21     42       By similarity.
FT                                /FTId=PRO_0000028103.
FT   CHAIN        43    456       Vitamin K-dependent protein C.
FT                                /FTId=PRO_0000028104.
FT   CHAIN        43    197       Vitamin K-dependent protein C light
FT                                chain.
FT                                /FTId=PRO_0000028105.
FT   CHAIN       200    456       Vitamin K-dependent protein C heavy
FT                                chain.
FT                                /FTId=PRO_0000028106.
FT   DOMAIN       47     88       Gla.
FT   DOMAIN       97    132       EGF-like 1.
FT   DOMAIN      136    176       EGF-like 2.
FT   DOMAIN      211    445       Peptidase S1.
FT   ACT_SITE    252    252       Charge relay system (By similarity).
FT   ACT_SITE    298    298       Charge relay system (By similarity).
FT   ACT_SITE    397    397       Charge relay system (By similarity).
FT   MOD_RES      48     48       4-carboxyglutamate (By similarity).
FT   MOD_RES      49     49       4-carboxyglutamate (By similarity).
FT   MOD_RES      56     56       4-carboxyglutamate (By similarity).
FT   MOD_RES      58     58       4-carboxyglutamate (By similarity).
FT   MOD_RES      61     61       4-carboxyglutamate (By similarity).
FT   MOD_RES      62     62       4-carboxyglutamate (By similarity).
FT   MOD_RES      67     67       4-carboxyglutamate (By similarity).
FT   MOD_RES      68     68       4-carboxyglutamate (By similarity).
FT   MOD_RES      71     71       4-carboxyglutamate (By similarity).
FT   MOD_RES     113    113       (3R)-3-hydroxyaspartate (By similarity).
FT   CARBOHYD    139    139       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    202    202       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    289    289       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    350    350       N-linked (GlcNAc...) (Potential).
FT   DISULFID     59     64       By similarity.
FT   DISULFID     92    111       By similarity.
FT   DISULFID    101    106       By similarity.
FT   DISULFID    105    120       By similarity.
FT   DISULFID    122    131       By similarity.
FT   DISULFID    140    151       By similarity.
FT   DISULFID    147    160       By similarity.
FT   DISULFID    162    175       By similarity.
FT   DISULFID    183    318       Interchain (between light and heavy
FT                                chains) (By similarity).
FT   DISULFID    237    253       By similarity.
FT   DISULFID    368    382       By similarity.
FT   DISULFID    393    421       By similarity.
SQ   SEQUENCE   456 AA;  50814 MW;  7AD3A8C1C34E59FF CRC64;
     MWQLASLSLL LTICGTCSTA APPGSVFSSS ESAHQVLRIR KRANSFLEEI RAGSLERECM
     EEICDFEEAK EIFQNVDDTL AYWSKYVDGD QCAALPPEHA CDSPCCGHGS CIDGIGAFHC
     DCGRGWEGRF CQHEVSYINC SLDNGGCSHY CLEEEGGRHC SCAPGYRLGD DHLQCQPAVK
     FPCGRPGKQM EKKRKHLKRD TNQTDQIDPR LVNGKVTRRG ESPWQVVLLD SKKKLACGAV
     LIHTSWVLTA AHCMEDSKKL IVRLGEYDLR RWEKGEMDVD IKEVLIHPNY SKSTTDNDIA
     LLHLAQPAIF SQTIVPICLP DSGLAERELT QVGQETVVTG WGYRSETKRN RTFVLNFINI
     PVAPHNECIQ AMYNMISENM LCAGILGDSR DACEGDSGGP MVTSFRGTWF LVGLVSWGEG
     CGRLHNYGIY TKVSRYLDWI HSHIRGEEAS LENQVP
//

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