GenomeNet

Database: UniProt
Entry: Q63207
LinkDB: Q63207
Original site: Q63207 
ID   FA10_RAT                Reviewed;         482 AA.
AC   Q63207;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JAN-2019, entry version 160.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=8578539; DOI=10.1016/0049-3848(95)00151-G;
RA   Stanton C., Ross R.P., Hutson S., Wallin R.;
RT   "Evidence for competition between vitamin K-dependent clotting factors
RT   for intracellular processing by the vitamin K-dependent gamma-
RT   carboxylase.";
RL   Thromb. Res. 80:63-73(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that
CC       converts prothrombin to thrombin in the presence of factor Va,
CC       calcium and phospholipid during blood clotting.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds
CC         in 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
CC       by the excision of two Arg residues and are held together by 1 or
CC       more disulfide bonds. Forms a heterodimer with SERPINA5 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium.
CC   -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC   -!- PTM: The activation peptide is cleaved by factor IXa (in the
CC       intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
CC       {ECO:0000250}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; X79807; CAA56202.1; -; mRNA.
DR   EMBL; BC088151; AAH88151.1; -; mRNA.
DR   PIR; S49075; EXRT.
DR   RefSeq; NP_058839.1; NM_017143.2.
DR   UniGene; Rn.21393; -.
DR   ProteinModelPortal; Q63207; -.
DR   SMR; Q63207; -.
DR   STRING; 10116.ENSRNOP00000026677; -.
DR   BindingDB; Q63207; -.
DR   ChEMBL; CHEMBL3755; -.
DR   MEROPS; S01.216; -.
DR   iPTMnet; Q63207; -.
DR   PhosphoSitePlus; Q63207; -.
DR   PaxDb; Q63207; -.
DR   PRIDE; Q63207; -.
DR   GeneID; 29243; -.
DR   KEGG; rno:29243; -.
DR   UCSC; RGD:61850; rat.
DR   CTD; 2159; -.
DR   RGD; 61850; F10.
DR   eggNOG; ENOG410IGPV; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; Q63207; -.
DR   KO; K01314; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q63207; -.
DR   TreeFam; TF327329; -.
DR   PRO; PR:Q63207; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; Q63207; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IDA:RGD.
DR   CDD; cd00190; Tryp_SPc; 1.
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; IPR013032; EGF-like_CS.
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; 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   2: Evidence at transcript level;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW   Hydroxylation; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   PROPEP       21     40       {ECO:0000250}.
FT                                /FTId=PRO_0000027804.
FT   CHAIN        41    482       Coagulation factor X.
FT                                /FTId=PRO_0000027805.
FT   CHAIN        41    180       Factor X light chain. {ECO:0000250}.
FT                                /FTId=PRO_0000027806.
FT   CHAIN       184    482       Factor X heavy chain. {ECO:0000250}.
FT                                /FTId=PRO_0000027807.
FT   PROPEP      184    231       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000027808.
FT   CHAIN       232    482       Activated factor Xa heavy chain.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000027809.
FT   DOMAIN       41     85       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       86    122       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      125    165       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      232    465       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    274    274       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    320    320       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    417    417       Charge relay system. {ECO:0000250}.
FT   MOD_RES      46     46       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      47     47       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      54     54       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      56     56       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      59     59       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      60     60       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      65     65       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      66     66       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      69     69       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      72     72       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      75     75       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      79     79       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00743,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES     103    103       (3R)-3-hydroxyaspartate. {ECO:0000250}.
FT   CARBOHYD    187    187       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    218    218       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     57     62       {ECO:0000250}.
FT   DISULFID     90    101       {ECO:0000250}.
FT   DISULFID     95    110       {ECO:0000250}.
FT   DISULFID    112    121       {ECO:0000250}.
FT   DISULFID    129    140       {ECO:0000250}.
FT   DISULFID    136    149       {ECO:0000250}.
FT   DISULFID    151    164       {ECO:0000250}.
FT   DISULFID    172    340       Interchain (between light and heavy
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DISULFID    238    243       {ECO:0000250}.
FT   DISULFID    259    275       {ECO:0000250}.
FT   DISULFID    388    402       {ECO:0000250}.
FT   DISULFID    413    441       {ECO:0000250}.
SQ   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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