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 27-MAR-2024, entry version 176.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 for
RT intracellular processing by the vitamin K-dependent gamma-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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 {ECO:0000250}.
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 -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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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 AlphaFoldDB; Q63207; -.
DR SMR; Q63207; -.
DR STRING; 10116.ENSRNOP00000026677; -.
DR BindingDB; Q63207; -.
DR ChEMBL; CHEMBL3755; -.
DR MEROPS; S01.216; -.
DR GlyCosmos; Q63207; 2 sites, No reported glycans.
DR GlyGen; Q63207; 2 sites.
DR iPTMnet; Q63207; -.
DR PhosphoSitePlus; Q63207; -.
DR PaxDb; 10116-ENSRNOP00000026677; -.
DR GeneID; 29243; -.
DR KEGG; rno:29243; -.
DR UCSC; RGD:61850; rat.
DR AGR; RGD:61850; -.
DR CTD; 2159; -.
DR RGD; 61850; F10.
DR eggNOG; ENOG502QS4N; Eukaryota.
DR HOGENOM; CLU_006842_19_5_1; -.
DR InParanoid; Q63207; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; Q63207; -.
DR TreeFam; TF327329; -.
DR Reactome; R-RNO-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-159740; Gamma-carboxylation of protein precursors.
DR Reactome; R-RNO-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-RNO-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR PRO; PR:Q63207; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q63207; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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 PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR PANTHER; PTHR24278:SF28; COAGULATION FACTOR X; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00010; EGFBLOOD.
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; SSF57630; GLA-domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 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_0000027804"
FT CHAIN 41..482
FT /note="Coagulation factor X"
FT /id="PRO_0000027805"
FT CHAIN 41..180
FT /note="Factor X light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027806"
FT CHAIN 184..482
FT /note="Factor X heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027807"
FT PROPEP 184..231
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027808"
FT CHAIN 232..482
FT /note="Activated factor Xa heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027809"
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..465
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 320
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 417
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:0000255"
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..340
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 259..275
FT /evidence="ECO:0000250"
FT DISULFID 388..402
FT /evidence="ECO:0000250"
FT DISULFID 413..441
FT /evidence="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
//
