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PROC_RABIT
ID   PROC_RABIT              Reviewed;         458 AA.
AC   Q28661;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 142.
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; Fragment;
GN   Name=PROC;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Shen L., He X., Dahlback B.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein C is a vitamin K-dependent serine protease that
CC       regulates blood coagulation by inactivating factors Va and VIIIa in the
CC       presence of calcium ions and phospholipids. Exerts a protective effect
CC       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 into
CC       a light chain and a heavy chain held together by a disulfide bond. The
CC       enzyme is then activated by thrombin, which cleaves a tetradecapeptide
CC       from the amino end of the heavy chain; this reaction, which occurs at
CC       the surface of endothelial cells, is strongly promoted by
CC       thrombomodulin.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04070}. Golgi
CC       apparatus {ECO:0000250|UniProtKB:P04070}. Endoplasmic reticulum
CC       {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 aspartate
CC       and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Calcium also binds, with stronger affinity to another
CC       site, beyond the GLA domain. This GLA-independent binding site is
CC       necessary for the recognition of the thrombin-thrombomodulin complex.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; U49933; AAA92956.1; -; mRNA.
DR   AlphaFoldDB; Q28661; -.
DR   SMR; Q28661; -.
DR   STRING; 9986.ENSOCUP00000013608; -.
DR   MEROPS; S01.218; -.
DR   eggNOG; ENOG502QQ3W; Eukaryota.
DR   InParanoid; Q28661; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
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; 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; IPR043504; Peptidase_S1_PA_chymotrypsin.
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   Disulfide bond; EGF-like domain; Endoplasmic reticulum;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Golgi apparatus; Hemostasis;
KW   Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          <1..27
FT                   /evidence="ECO:0000250"
FT   PROPEP          28..36
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028122"
FT   CHAIN           37..458
FT                   /note="Vitamin K-dependent protein C"
FT                   /id="PRO_0000028123"
FT   CHAIN           37..192
FT                   /note="Vitamin K-dependent protein C light chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028124"
FT   CHAIN           195..458
FT                   /note="Vitamin K-dependent protein C heavy chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028125"
FT   PEPTIDE         195..209
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000028126"
FT   DOMAIN          37..82
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DOMAIN          91..126
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          130..170
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          210..447
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        250
FT                   /note="Charge relay system"
FT   ACT_SITE        296
FT                   /note="Charge relay system"
FT   ACT_SITE        399
FT                   /note="Charge relay system"
FT   SITE            209..210
FT                   /note="Cleavage; by thrombin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         42
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00745,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         43
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00745,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         50
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00745,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         52
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00745,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         55
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00745,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         56
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00745,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         61
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00745,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         62
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00745,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         65
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00745,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         107
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000250"
FT   DISULFID        99..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        116..125
FT                   /evidence="ECO:0000250"
FT   DISULFID        134..145
FT                   /evidence="ECO:0000250"
FT   DISULFID        141..154
FT                   /evidence="ECO:0000250"
FT   DISULFID        156..169
FT                   /evidence="ECO:0000250"
FT   DISULFID        177..316
FT                   /note="Interchain (between light and heavy chains)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT                   ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT                   ProRule:PRU00463"
FT   DISULFID        235..251
FT                   /evidence="ECO:0000250"
FT   DISULFID        370..384
FT                   /evidence="ECO:0000250"
FT   DISULFID        395..423
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   458 AA;  51088 MW;  D75A5F990C8F29D7 CRC64;
     IPDDVGYRNQ KTASKEGVCV VSKCQDGPNT LPRAKRANSF LEELRPSSLE RECVEEVCDL
     EEAKEIFQSV DDTLAFWYKY VDGDQCAALP SEHPCSSQCC GHGTCADSIG GFSCQCHGGW
     EGSFCQYEVR FSNCSVDNGG CAHYCLEEEA GRSCSCAPGY ELADDHLQCE PAVRFPCGRL
     GWKRIEKKRG NVKRDLEQVD EMDEVDPRLI DGKLTRRGDS PWQVILLDSK KKLACGAVLI
     HVSWVLTAAH CMEEPKKLFV RLGEYDLRRK ERWELDLNIQ EVLIHPNYSR STTDNDIALL
     RLAQPATLSQ TIVPICLPDN GLAERELMQA GQETVVTGWG YHSSREKEAK RNRTFILNFI
     TVPVAPQNEC EQVMSNIISE NMLCAGILGD RRDACDGDSG GPMVASFRGT WFLVGLVSWG
     EGCGDLNNYG VYTKVSRYLD WIHSHIEEKE AAPESPAP
 
 
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