位置:首页 > 蛋白库 > FA10_MOUSE
FA10_MOUSE
ID   FA10_MOUSE              Reviewed;         481 AA.
AC   O88947; O54740; Q99L32;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Coagulation factor X;
DE            EC=3.4.21.6;
DE   AltName: Full=Stuart factor;
DE   Contains:
DE     RecName: Full=Factor X light chain;
DE   Contains:
DE     RecName: Full=Factor X heavy chain;
DE   Contains:
DE     RecName: Full=Activated factor Xa heavy chain;
DE   Flags: Precursor;
GN   Name=F10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX   PubMed=9684791;
RA   Liang Z., Cooper A., DeFord M.E., Carmeliet P., Collen D., Castellino F.J.,
RA   Rosen E.D.;
RT   "Cloning and characterization of a cDNA encoding murine coagulation factor
RT   X.";
RL   Thromb. Haemost. 80:87-91(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9783672; DOI=10.1016/s0049-3848(98)00110-8;
RA   Heidtmann H.H., Kontermann R.E.;
RT   "Cloning and recombinant expression of mouse coagulation factor X.";
RL   Thromb. Res. 92:33-41(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=10823271;
RA   Cooper A., Liang Z., Castellino F.J., Rosen E.D.;
RT   "Cloning and characterization of the murine coagulation factor X gene.";
RL   Thromb. Haemost. 83:732-735(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Liver, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts
CC       prothrombin to thrombin in the presence of factor Va, calcium and
CC       phospholipid during blood clotting.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in
CC         prothrombin to form thrombin.; EC=3.4.21.6;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC   -!- SUBUNIT: The two chains are formed from a single-chain precursor by the
CC       excision of two Arg residues and are held together by 1 or more
CC       disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
CC       residues allows the modified protein to bind calcium.
CC   -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC   -!- PTM: Proteolytically cleaved and activated by cathepsin CTSG (By
CC       similarity). The activation peptide is cleaved by factor IXa (in the
CC       intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By
CC       similarity). {ECO:0000250|UniProtKB:P00742,
CC       ECO:0000250|UniProtKB:P00743}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF087644; AAC36345.1; -; mRNA.
DR   EMBL; AJ222677; CAA10933.1; -; mRNA.
DR   EMBL; AF211347; AAF22980.1; -; Genomic_DNA.
DR   EMBL; BC003877; AAH03877.1; -; mRNA.
DR   CCDS; CCDS40226.1; -.
DR   RefSeq; NP_031998.3; NM_007972.4.
DR   AlphaFoldDB; O88947; -.
DR   SMR; O88947; -.
DR   BioGRID; 199566; 10.
DR   IntAct; O88947; 2.
DR   STRING; 10090.ENSMUSP00000068389; -.
DR   MEROPS; S01.216; -.
DR   GlyGen; O88947; 2 sites.
DR   iPTMnet; O88947; -.
DR   PhosphoSitePlus; O88947; -.
DR   CPTAC; non-CPTAC-3413; -.
DR   jPOST; O88947; -.
DR   PaxDb; O88947; -.
DR   PeptideAtlas; O88947; -.
DR   PRIDE; O88947; -.
DR   ProteomicsDB; 275832; -.
DR   Antibodypedia; 11687; 688 antibodies from 35 providers.
DR   DNASU; 14058; -.
DR   Ensembl; ENSMUST00000063820; ENSMUSP00000068389; ENSMUSG00000031444.
DR   GeneID; 14058; -.
DR   KEGG; mmu:14058; -.
DR   UCSC; uc009kws.2; mouse.
DR   CTD; 2159; -.
DR   MGI; MGI:103107; F10.
DR   VEuPathDB; HostDB:ENSMUSG00000031444; -.
DR   eggNOG; ENOG502QS4N; Eukaryota.
DR   GeneTree; ENSGT00940000157694; -.
DR   HOGENOM; CLU_006842_19_5_1; -.
DR   InParanoid; O88947; -.
DR   TreeFam; TF327329; -.
DR   Reactome; R-MMU-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
DR   Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   BioGRID-ORCS; 14058; 4 hits in 73 CRISPR screens.
DR   ChiTaRS; F10; mouse.
DR   PRO; PR:O88947; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; O88947; protein.
DR   Bgee; ENSMUSG00000031444; Expressed in left lobe of liver and 66 other tissues.
DR   ExpressionAtlas; O88947; baseline and differential.
DR   Genevisible; O88947; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:1905370; C:serine-type endopeptidase complex; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR   GO; GO:0007596; P:blood coagulation; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; ISO:MGI.
DR   GO; GO:0031638; P:zymogen activation; ISO:MGI.
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; 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; 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   1: Evidence at protein level;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
KW   Hemostasis; Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..40
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027792"
FT   CHAIN           41..481
FT                   /note="Coagulation factor X"
FT                   /id="PRO_0000027793"
FT   CHAIN           41..180
FT                   /note="Factor X light chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027794"
FT   CHAIN           184..481
FT                   /note="Factor X heavy chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027795"
FT   PROPEP          184..231
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027796"
FT   CHAIN           232..481
FT                   /note="Activated factor Xa heavy chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027797"
FT   DOMAIN          41..85
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DOMAIN          86..122
FT                   /note="EGF-like 1; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          125..165
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          232..464
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        273
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        319
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        416
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         46
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         47
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         54
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         56
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         59
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         60
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         65
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         66
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         69
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         72
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         75
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         79
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P00743,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         103
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16944957"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        90..101
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        112..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        129..140
FT                   /evidence="ECO:0000250"
FT   DISULFID        136..149
FT                   /evidence="ECO:0000250"
FT   DISULFID        151..164
FT                   /evidence="ECO:0000250"
FT   DISULFID        172..339
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        238..243
FT                   /evidence="ECO:0000250"
FT   DISULFID        258..274
FT                   /evidence="ECO:0000250"
FT   DISULFID        387..401
FT                   /evidence="ECO:0000250"
FT   DISULFID        412..440
FT                   /evidence="ECO:0000250"
FT   CONFLICT        250
FT                   /note="I -> V (in Ref. 4; AAH03877)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        294
FT                   /note="E -> D (in Ref. 2; CAA10933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="M -> L (in Ref. 2; CAA10933)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   481 AA;  54018 MW;  8AC09DE5EF9D271E CRC64;
     MGSPVQLSLL CVVLASLLLP GKGVFINRER ANNVLARTRR ANSFFEEFKK GNLERECMEE
     ICSYEEVREI FEDDEKTKEY WTKYKDGDQC ESSPCQNQGA CRDGIGGYTC TCSEGFEGKN
     CELFVRKLCR LDNGDCDQFC REEQNSVVCS CASGYFLGND GKSCISTAPF PCGKITTGRR
     KRSVALNTSD SELDLEDALL DEDFLSPTEN PIELLNLNET QPERSSDDLV RIVGGRECKD
     GECPWQALLI NEDNEGFCGG TILNEFYILT AAHCLHQARR FKVRVGDRNT EKEEGNEMVH
     EVDVVIKHNK FQRDTYDYDI AVLRLKTPIT FRMNVAPACL PQKDWAESTL MTQKTGIVSG
     FGRTHEKGRQ SNILKMLEVP YVDRNTCKLS TSFSITQNMF CAGYEAKLED ACQGDSGGPH
     VTRFKNTYYV TGIVSWGEGC ARKGKYGIYT KVTTFLKWID RSMKARVGPT AETPRTAGPP
     N
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024