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FA10_BOVIN Reviewed; 492 AA.
P00743;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
23-FEB-2022, entry version 224.
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;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-487.
PubMed=6330671; DOI=10.1093/nar/12.11.4481;
Fung M.R., Campbell R.M., McGillivray R.T.A.;
"Blood coagulation factor X mRNA encodes a single polypeptide chain
containing a prepro leader sequence.";
Nucleic Acids Res. 12:4481-4492(1984).
[2]
PROTEIN SEQUENCE OF 41-180, AND GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47;
GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-72; GLU-75 AND
GLU-79.
PubMed=6766735; DOI=10.1021/bi00545a009;
Enfield D.L., Ericsson L.H., Fujikawa K., Walsh K.A., Neurath H.,
Titani K.;
"Amino acid sequence of the light chain of bovine factor X1 (Stuart
factor).";
Biochemistry 19:659-667(1980).
[3]
HYDROXYLATION AT ASP-103.
PubMed=6688526; DOI=10.1016/0006-291x(83)90961-0;
McMullen B.A., Fujikawa K., Kisiel W.;
"The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent
blood coagulation zymogens.";
Biochem. Biophys. Res. Commun. 115:8-14(1983).
[4]
PROTEIN SEQUENCE OF 183-492, GLYCOSYLATION AT ASN-218 AND THR-485, AND
DISULFIDE BONDS.
PubMed=1059093; DOI=10.1073/pnas.72.8.3082;
Titani K., Fujikawa K., Enfield D.L., Ericsson L.H., Walsh K.A.,
Neurath H.;
"Bovine factor X1 (Stuart factor): amino-acid sequence of heavey chain.";
Proc. Natl. Acad. Sci. U.S.A. 72:3082-3086(1975).
[5]
PROTEIN SEQUENCE OF 183-233, AND GLYCOSYLATION AT THR-208.
PubMed=8243461; DOI=10.1111/j.1432-1033.1993.tb18361.x;
Inoue K., Morita T.;
"Identification of O-linked oligosaccharide chains in the activation
peptides of blood coagulation factor X. The role of the carbohydrate
moieties in the activation of factor X.";
Eur. J. Biochem. 218:153-163(1993).
[6]
ACTIVE SITE.
PubMed=4264286; DOI=10.1021/bi00776a004;
Titani K., Hermodson M.A., Fujikawa K., Ericsson L.H., Walsh K.A.,
Neurath H., Davie E.W.;
"Bovine factor X 1a (activated Stuart factor). Evidence of homology with
mammalian serine proteases.";
Biochemistry 11:4899-4903(1972).
[7]
PROTEOLYTIC PROCESSING.
PubMed=1059122; DOI=10.1073/pnas.72.9.3359;
Fujikawa K., Titani K., Davie E.W.;
"Activation of bovine factor X (Stuart factor): conversion of factor Xa-
alpha to factor Xa-beta.";
Proc. Natl. Acad. Sci. U.S.A. 72:3359-3363(1975).
[8]
CALCIUM-BINDING.
PubMed=6546930;
Sugo T., Bjoerk I., Holmgren A., Stenflo J.;
"Calcium-binding properties of bovine factor X lacking the gamma-
carboxyglutamic acid-containing region.";
J. Biol. Chem. 259:5705-5710(1984).
[9]
SULFATION AT TYR-200.
PubMed=3949800;
Morita T., Jackson C.M.;
"Localization of the structural difference between bovine blood coagulation
factors X1 and X2 to tyrosine 18 in the activation peptide.";
J. Biol. Chem. 261:4008-4014(1986).
[10]
STRUCTURE BY NMR OF 85-126.
PubMed=2261466; DOI=10.1021/bi00487a018;
Selander M., Persson E., Stenflo J., Drakenberg T.;
"1H NMR assignment and secondary structure of the Ca2(+)-free form of the
amino-terminal epidermal growth factor like domain in coagulation factor
X.";
Biochemistry 29:8111-8118(1990).
[11]
STRUCTURE BY NMR OF 85-126.
PubMed=1627540; DOI=10.1021/bi00141a004;
Ullner M., Selander M., Persson E., Stenflo J., Drakenberg T., Teleman O.;
"Three-dimensional structure of the apo form of the N-terminal EGF-like
module of blood coagulation factor X as determined by NMR spectroscopy and
simulated folding.";
Biochemistry 31:5974-5983(1992).
[12]
STRUCTURE BY NMR OF 85-126.
PubMed=1527084; DOI=10.2210/pdb1ccf/pdb;
Selander-Sunnerhagen M., Ullner M., Persson E., Teleman O., Stenflo J.,
Drakenberg T.;
"How an epidermal growth factor (EGF)-like domain binds calcium. High
resolution NMR structure of the calcium form of the NH2-terminal EGF-like
domain in coagulation factor X.";
J. Biol. Chem. 267:19642-19649(1992).
[13]
STRUCTURE BY NMR OF 41-126.
PubMed=8794734; DOI=10.1021/bi960633j;
Sunnerhagen M., Olah G.A., Stenflo J., Forsen S., Drakenberg T.,
Trewhella J.;
"The relative orientation of Gla and EGF domains in coagulation factor X is
altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle
X-ray scattering study.";
Biochemistry 35:11547-11559(1996).
-!- 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:
Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in
prothrombin to form thrombin.; EC=3.4.21.6;
-!- ACTIVITY 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.
-!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
residues allows the modified protein to bind calcium.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:1059093,
ECO:0000269|PubMed:8243461}.
-!- PTM: Proteolytically cleaved and activated by cathepsin CTSG (By
similarity). The activation peptide is cleaved by factor IXa (in the
intrinsic pathway), or by factor VIIa (in the extrinsic pathway)
(PubMed:1059122). {ECO:0000250|UniProtKB:P00742,
ECO:0000269|PubMed:1059122}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
and asparagine is (R) stereospecific within EGF domains.
{ECO:0000269|PubMed:6688526}.
-!- MISCELLANEOUS: Calcium also binds, with stronger affinity to another
site, beyond the GLA domain.
-!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
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EMBL; X00673; CAA25286.1; -; mRNA.
PIR; A22867; EXBO.
RefSeq; NP_001073682.1; NM_001080213.1.
PDB; 1APO; NMR; -; A=85-126.
PDB; 1CCF; NMR; -; A=85-126.
PDB; 1IOD; X-ray; 2.30 A; G=41-84.
PDB; 1KIG; X-ray; 3.00 A; H=234-474, L=129-179.
PDB; 1WHE; NMR; -; A=41-126.
PDB; 1WHF; NMR; -; A=41-126.
PDBsum; 1APO; -.
PDBsum; 1CCF; -.
PDBsum; 1IOD; -.
PDBsum; 1KIG; -.
PDBsum; 1WHE; -.
PDBsum; 1WHF; -.
BMRB; P00743; -.
SMR; P00743; -.
ELM; P00743; -.
IntAct; P00743; 1.
STRING; 9913.ENSBTAP00000021789; -.
BindingDB; P00743; -.
ChEMBL; CHEMBL3656; -.
MEROPS; S01.216; -.
GlyConnect; 101; 2 N-Linked glycans (1 site), 9 O-Linked glycans.
iPTMnet; P00743; -.
PaxDb; P00743; -.
GeneID; 280787; -.
KEGG; bta:280787; -.
CTD; 2159; -.
eggNOG; ENOG502QS4N; Eukaryota.
HOGENOM; CLU_006842_19_5_1; -.
InParanoid; P00743; -.
OMA; HITRYND; -.
OrthoDB; 1314811at2759; -.
TreeFam; TF327329; -.
SABIO-RK; P00743; -.
EvolutionaryTrace; P00743; -.
PRO; PR:P00743; -.
Proteomes; UP000009136; Unplaced.
Bgee; ENSBTAG00000016385; Expressed in liver and 61 other tissues.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 2.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR012224; Pept_S1A_FX.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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.
PIRSF; PIRSF001143; Factor_X; 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; 1.
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;
3D-structure; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Direct protein sequencing;
Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
Hemostasis; Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
Secreted; Serine protease; Signal; Sulfation; Zymogen.
SIGNAL 1..23
/evidence="ECO:0000255"
PROPEP 24..40
/evidence="ECO:0000269|PubMed:6766735"
/id="PRO_0000027779"
CHAIN 41..492
/note="Coagulation factor X"
/id="PRO_0000027780"
CHAIN 41..180
/note="Factor X light chain"
/id="PRO_0000027781"
CHAIN 183..492
/note="Factor X heavy chain"
/id="PRO_0000027782"
PROPEP 183..233
/note="Activation peptide"
/id="PRO_0000027783"
CHAIN 234..492
/note="Activated factor Xa heavy chain"
/id="PRO_0000027784"
PROPEP 476..492
/note="May be removed but is not necessary for activation"
/id="PRO_0000027785"
DOMAIN 41..85
/note="Gla"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
DOMAIN 86..122
/note="EGF-like 1; calcium-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 125..165
/note="EGF-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 234..466
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
REGION 472..492
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 275
/note="Charge relay system"
/evidence="ECO:0000269|PubMed:4264286"
ACT_SITE 321
/note="Charge relay system"
/evidence="ECO:0000269|PubMed:4264286"
ACT_SITE 418
/note="Charge relay system"
/evidence="ECO:0000269|PubMed:4264286"
SITE 233..234
/note="Cleavage; by coagulation factor IXa and coagulation
factor VIIa"
MOD_RES 46
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 47
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 54
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 56
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 59
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 60
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 65
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 66
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 69
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 72
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 75
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 79
/note="4-carboxyglutamate"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
ECO:0000269|PubMed:6766735"
MOD_RES 103
/note="(3R)-3-hydroxyaspartate"
/evidence="ECO:0000269|PubMed:6688526"
MOD_RES 200
/note="Sulfotyrosine"
/evidence="ECO:0000269|PubMed:3949800"
CARBOHYD 208
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:8243461"
CARBOHYD 218
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:1059093"
/id="CAR_000011"
CARBOHYD 485
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 57..62
/evidence="ECO:0000250"
DISULFID 90..101
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 95..110
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 112..121
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 129..140
/evidence="ECO:0000250"
DISULFID 136..149
/evidence="ECO:0000250"
DISULFID 151..164
/evidence="ECO:0000250"
DISULFID 172..341
/note="Interchain (between light and heavy chains)"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00463, ECO:0000269|PubMed:1059093"
DISULFID 240..245
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 260..276
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 389..403
/evidence="ECO:0000269|PubMed:1059093"
DISULFID 414..442
/evidence="ECO:0000269|PubMed:1059093"
CONFLICT 103
/note="D -> N (in Ref. 2; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 293
/note="Missing (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 296..298
/note="EGN -> GDE (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 335
/note="Missing (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 349..350
/note="EA -> AE (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 355
/note="Missing (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 442..445
/note="CARK -> GKFG (in Ref. 4; AA sequence)"
/evidence="ECO:0000305"
HELIX 46..48
/evidence="ECO:0007829|PDB:1IOD"
HELIX 53..57
/evidence="ECO:0007829|PDB:1IOD"
STRAND 58..61
/evidence="ECO:0007829|PDB:1WHE"
HELIX 64..71
/evidence="ECO:0007829|PDB:1IOD"
HELIX 74..82
/evidence="ECO:0007829|PDB:1IOD"
TURN 86..90
/evidence="ECO:0007829|PDB:1WHE"
STRAND 100..102
/evidence="ECO:0007829|PDB:1CCF"
STRAND 105..107
/evidence="ECO:0007829|PDB:1APO"
STRAND 109..111
/evidence="ECO:0007829|PDB:1CCF"
STRAND 116..118
/evidence="ECO:0007829|PDB:1APO"
STRAND 121..123
/evidence="ECO:0007829|PDB:1WHF"
TURN 131..134
/evidence="ECO:0007829|PDB:1KIG"
STRAND 135..138
/evidence="ECO:0007829|PDB:1KIG"
STRAND 155..157
/evidence="ECO:0007829|PDB:1KIG"
STRAND 164..166
/evidence="ECO:0007829|PDB:1KIG"
STRAND 168..170
/evidence="ECO:0007829|PDB:1KIG"
STRAND 235..237
/evidence="ECO:0007829|PDB:1KIG"
TURN 242..244
/evidence="ECO:0007829|PDB:1KIG"
STRAND 248..252
/evidence="ECO:0007829|PDB:1KIG"
STRAND 254..256
/evidence="ECO:0007829|PDB:1KIG"
STRAND 258..264
/evidence="ECO:0007829|PDB:1KIG"
STRAND 266..272
/evidence="ECO:0007829|PDB:1KIG"
STRAND 304..309
/evidence="ECO:0007829|PDB:1KIG"
TURN 315..317
/evidence="ECO:0007829|PDB:1KIG"
STRAND 323..329
/evidence="ECO:0007829|PDB:1KIG"
HELIX 345..350
/evidence="ECO:0007829|PDB:1KIG"
TURN 351..354
/evidence="ECO:0007829|PDB:1KIG"
STRAND 355..363
/evidence="ECO:0007829|PDB:1KIG"
STRAND 365..367
/evidence="ECO:0007829|PDB:1KIG"
STRAND 370..372
/evidence="ECO:0007829|PDB:1KIG"
STRAND 377..383
/evidence="ECO:0007829|PDB:1KIG"
HELIX 386..392
/evidence="ECO:0007829|PDB:1KIG"
STRAND 401..407
/evidence="ECO:0007829|PDB:1KIG"
STRAND 421..426
/evidence="ECO:0007829|PDB:1KIG"
STRAND 429..443
/evidence="ECO:0007829|PDB:1KIG"
STRAND 447..454
/evidence="ECO:0007829|PDB:1KIG"
HELIX 455..457
/evidence="ECO:0007829|PDB:1KIG"
HELIX 458..464
/evidence="ECO:0007829|PDB:1KIG"
SEQUENCE 492 AA; 54510 MW; D5BD911FB72F1D30 CRC64;
MAGLLHLVLL STALGGLLRP AGSVFLPRDQ AHRVLQRARR ANSFLEEVKQ GNLERECLEE
ACSLEEAREV FEDAEQTDEF WSKYKDGDQC EGHPCLNQGH CKDGIGDYTC TCAEGFEGKN
CEFSTREICS LDNGGCDQFC REERSEVRCS CAHGYVLGDD SKSCVSTERF PCGKFTQGRS
RRWAIHTSED ALDASELEHY DPADLSPTES SLDLLGLNRT EPSAGEDGSQ VVRIVGGRDC
AEGECPWQAL LVNEENEGFC GGTILNEFYV LTAAHCLHQA KRFTVRVGDR NTEQEEGNEM
AHEVEMTVKH SRFVKETYDF DIAVLRLKTP IRFRRNVAPA CLPEKDWAEA TLMTQKTGIV
SGFGRTHEKG RLSSTLKMLE VPYVDRSTCK LSSSFTITPN MFCAGYDTQP EDACQGDSGG
PHVTRFKDTY FVTGIVSWGE GCARKGKFGV YTKVSNFLKW IDKIMKARAG AAGSRGHSEA
PATWTVPPPL PL