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Coagulation factor X (EC 3.4.21.6) (Stuart factor) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]

 FA10_MOUSE              Reviewed;         481 AA.
O88947; O54740; Q99L32;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
07-JUN-2017, entry version 158.
RecName: Full=Coagulation factor X;
EC=3.4.21.6;
AltName: Full=Stuart factor;
Contains:
RecName: Full=Factor X light chain;
Contains:
RecName: Full=Factor X heavy chain;
Contains:
RecName: Full=Activated factor Xa heavy chain;
Flags: Precursor;
Name=F10;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X CBA; TISSUE=Liver;
PubMed=9684791;
Liang Z., Cooper A., DeFord M.E., Carmeliet P., Collen D.,
Castellino F.J., Rosen E.D.;
"Cloning and characterization of a cDNA encoding murine coagulation
factor X.";
Thromb. Haemost. 80:87-91(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=9783672; DOI=10.1016/S0049-3848(98)00110-8;
Heidtmann H.H., Kontermann R.E.;
"Cloning and recombinant expression of mouse coagulation factor X.";
Thromb. Res. 92:33-41(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=10823271;
Cooper A., Liang Z., Castellino F.J., Rosen E.D.;
"Cloning and characterization of the murine coagulation factor X
gene.";
Thromb. Haemost. 83:732-735(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Liver, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that
converts prothrombin to thrombin in the presence of factor Va,
calcium and phospholipid during blood clotting.
-!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Thr and then
Arg-|-Ile bonds in prothrombin to form thrombin.
-!- ENZYME REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
-!- SUBUNIT: The two chains are formed from a single-chain precursor
by the excision of two Arg residues and are held together by 1 or
more disulfide bonds. Forms a heterodimer with SERPINA5 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
-!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
glutamate residues allows the modified protein to bind calcium.
-!- PTM: N- and O-glycosylated. {ECO:0000250}.
-!- PTM: The activation peptide is cleaved by factor IXa (in the
intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; AF087644; AAC36345.1; -; mRNA.
EMBL; AJ222677; CAA10933.1; -; mRNA.
EMBL; AF211347; AAF22980.1; -; Genomic_DNA.
EMBL; BC003877; AAH03877.1; -; mRNA.
CCDS; CCDS40226.1; -.
RefSeq; NP_031998.3; NM_007972.4.
UniGene; Mm.262589; -.
ProteinModelPortal; O88947; -.
SMR; O88947; -.
IntAct; O88947; 2.
MINT; MINT-6597397; -.
STRING; 10090.ENSMUSP00000033821; -.
MEROPS; S01.216; -.
iPTMnet; O88947; -.
PhosphoSitePlus; O88947; -.
PaxDb; O88947; -.
PeptideAtlas; O88947; -.
PRIDE; O88947; -.
Ensembl; ENSMUST00000063820; ENSMUSP00000068389; ENSMUSG00000031444.
GeneID; 14058; -.
KEGG; mmu:14058; -.
UCSC; uc009kws.2; mouse.
CTD; 2159; -.
MGI; MGI:103107; F10.
eggNOG; ENOG410IGPV; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118890; -.
HOGENOM; HOG000251821; -.
HOVERGEN; HBG013304; -.
InParanoid; O88947; -.
KO; K01314; -.
TreeFam; TF327329; -.
Reactome; R-MMU-140834; Extrinsic Pathway of Fibrin Clot Formation.
Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
PRO; PR:O88947; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031444; -.
CleanEx; MM_F10; -.
ExpressionAtlas; O88947; baseline and differential.
Genevisible; O88947; MM.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005543; F:phospholipid binding; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR000294; GLA_domain.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00008; EGF; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00069; GLA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 2.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Blood coagulation; Calcium; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; EGF-like domain;
Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
Hydroxylation; Protease; Reference proteome; Repeat; Secreted;
Serine protease; Signal; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 40 {ECO:0000250}.
/FTId=PRO_0000027792.
CHAIN 41 481 Coagulation factor X.
/FTId=PRO_0000027793.
CHAIN 41 180 Factor X light chain. {ECO:0000250}.
/FTId=PRO_0000027794.
CHAIN 184 481 Factor X heavy chain. {ECO:0000250}.
/FTId=PRO_0000027795.
PROPEP 184 231 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000027796.
CHAIN 232 481 Activated factor Xa heavy chain.
{ECO:0000250}.
/FTId=PRO_0000027797.
DOMAIN 41 85 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 86 122 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 125 165 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 232 464 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 273 273 Charge relay system. {ECO:0000250}.
ACT_SITE 319 319 Charge relay system. {ECO:0000250}.
ACT_SITE 416 416 Charge relay system. {ECO:0000250}.
MOD_RES 46 46 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 47 47 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 54 54 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 56 56 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 59 59 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 60 60 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 65 65 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 66 66 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 69 69 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 72 72 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 75 75 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 79 79 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00743,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 103 103 (3R)-3-hydroxyaspartate. {ECO:0000250}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
CARBOHYD 218 218 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 62 {ECO:0000250}.
DISULFID 90 101 {ECO:0000250}.
DISULFID 95 110 {ECO:0000250}.
DISULFID 112 121 {ECO:0000250}.
DISULFID 129 140 {ECO:0000250}.
DISULFID 136 149 {ECO:0000250}.
DISULFID 151 164 {ECO:0000250}.
DISULFID 172 339 Interchain (between light and heavy
chains). {ECO:0000255|PROSITE-
ProRule:PRU00076, ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00463}.
DISULFID 238 243 {ECO:0000250}.
DISULFID 258 274 {ECO:0000250}.
DISULFID 387 401 {ECO:0000250}.
DISULFID 412 440 {ECO:0000250}.
CONFLICT 250 250 I -> V (in Ref. 4; AAH03877).
{ECO:0000305}.
CONFLICT 294 294 E -> D (in Ref. 2; CAA10933).
{ECO:0000305}.
CONFLICT 298 298 M -> L (in Ref. 2; CAA10933).
{ECO:0000305}.
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


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