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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_RAT                Reviewed;         482 AA.
Q63207;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 157.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
PubMed=8578539; DOI=10.1016/0049-3848(95)00151-G;
Stanton C., Ross R.P., Hutson S., Wallin R.;
"Evidence for competition between vitamin K-dependent clotting factors
for intracellular processing by the vitamin K-dependent gamma-
carboxylase.";
Thromb. Res. 80:63-73(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
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).
-!- 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.
-!- 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 {ECO:0000250}.
-!- 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}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; X79807; CAA56202.1; -; mRNA.
EMBL; BC088151; AAH88151.1; -; mRNA.
PIR; S49075; EXRT.
RefSeq; NP_058839.1; NM_017143.2.
UniGene; Rn.21393; -.
ProteinModelPortal; Q63207; -.
SMR; Q63207; -.
STRING; 10116.ENSRNOP00000026677; -.
BindingDB; Q63207; -.
ChEMBL; CHEMBL3755; -.
MEROPS; S01.216; -.
iPTMnet; Q63207; -.
PhosphoSitePlus; Q63207; -.
PaxDb; Q63207; -.
PRIDE; Q63207; -.
GeneID; 29243; -.
KEGG; rno:29243; -.
UCSC; RGD:61850; rat.
CTD; 2159; -.
RGD; 61850; F10.
eggNOG; ENOG410IGPV; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000251821; -.
HOVERGEN; HBG013304; -.
InParanoid; Q63207; -.
KO; K01314; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; Q63207; -.
TreeFam; TF327329; -.
PRO; PR:Q63207; -.
Proteomes; UP000002494; Unplaced.
Genevisible; Q63207; RN.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; IDA:RGD.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac-like_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; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR012224; Pept_S1A_FX.
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.
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; 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.
2: Evidence at transcript 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_0000027804.
CHAIN 41 482 Coagulation factor X.
/FTId=PRO_0000027805.
CHAIN 41 180 Factor X light chain. {ECO:0000250}.
/FTId=PRO_0000027806.
CHAIN 184 482 Factor X heavy chain. {ECO:0000250}.
/FTId=PRO_0000027807.
PROPEP 184 231 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000027808.
CHAIN 232 482 Activated factor Xa heavy chain.
{ECO:0000250}.
/FTId=PRO_0000027809.
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 232 465 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 274 274 Charge relay system. {ECO:0000250}.
ACT_SITE 320 320 Charge relay system. {ECO:0000250}.
ACT_SITE 417 417 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:0000255}.
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 172 340 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 259 275 {ECO:0000250}.
DISULFID 388 402 {ECO:0000250}.
DISULFID 413 441 {ECO:0000250}.
SEQUENCE 482 AA; 54265 MW; 0284678E3954A698 CRC64;
MESPVRLSLL YVVLASLLLP GRSVFINRER ANNVLQRIRR ANSFFEEIKK GNLERECVEE
ICSFEEAREV FEDNEKTTEF WNKYEDGDQC ESSPCQNQGE CRDGLGSYTC TCTEGFEGKN
CELFVRKLCS LDNGDCDQFC REEQNSVVCS CAKGYFLGND GKSCLSTAPF PCGKTNKGRA
KRSVALNTSN SEPDPEDLMP DADILYPTES PSELLNLNKT EPEANSDDVI RIVGGQECKR
GECPWQALLF SDEETDGFCG GTILNEFYIL TAAHCLHQAK RFKVRVGDLN TEQEDGGEMV
HEVDMIIKHN KFQRDTYDFD IAMLRLKTPI TFRENVAPAC LPQKDWAEAT LMTQKTGIVS
GFGRTHEKGR QSKVLKMMEV PYVDRNTCRL STSFSITQNM FCAGYDAKQE DACQGDSGGP
HVTRFKDTYF VTGIVSWGEG CARKGKYGIY TKVTAFLKWI DRSMKARVGP TSETPRLTHP
PY


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