ID   FA10_RABIT              Reviewed;         490 AA.
AC   O19045;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-NOV-2023, entry version 161.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9101642; DOI=10.1016/s0049-3848(97)00039-x;
RA   Pendurthi U.R., Anderson K.D., James H.L.;
RT   "Characterization of a full-length cDNA for rabbit factor X.";
RL   Thromb. Res. 85:503-514(1997).
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   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
CC       residues allows the modified protein to bind calcium. {ECO:0000250}.
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   -!- MISCELLANEOUS: Calcium also binds, with stronger affinity to another
CC       site, beyond the GLA domain.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; AF003200; AAB62542.1; -; mRNA.
DR   RefSeq; NP_001075485.1; NM_001082016.1.
DR   AlphaFoldDB; O19045; -.
DR   SMR; O19045; -.
DR   STRING; 9986.ENSOCUP00000025032; -.
DR   BindingDB; O19045; -.
DR   ChEMBL; CHEMBL5062; -.
DR   DrugCentral; O19045; -.
DR   MEROPS; S01.216; -.
DR   GlyCosmos; O19045; 3 sites, No reported glycans.
DR   PaxDb; 9986-ENSOCUP00000025032; -.
DR   GeneID; 100008647; -.
DR   KEGG; ocu:100008647; -.
DR   CTD; 2159; -.
DR   eggNOG; ENOG502QS4N; Eukaryota.
DR   InParanoid; O19045; -.
DR   OrthoDB; 4629979at2759; -.
DR   PRO; PR:O19045; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
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_0000027798"
FT   CHAIN           41..490
FT                   /note="Coagulation factor X"
FT                   /id="PRO_0000027799"
FT   CHAIN           41..180
FT                   /note="Factor X light chain"
FT                   /id="PRO_0000027800"
FT   CHAIN           184..490
FT                   /note="Factor X heavy chain"
FT                   /id="PRO_0000027801"
FT   PROPEP          184..232
FT                   /note="Activation peptide"
FT                   /id="PRO_0000027802"
FT   CHAIN           233..490
FT                   /note="Activated factor Xa heavy chain"
FT                   /id="PRO_0000027803"
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          233..465
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          183..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        274
FT                   /note="Charge relay system"
FT   ACT_SITE        320
FT                   /note="Charge relay system"
FT   ACT_SITE        417
FT                   /note="Charge relay system"
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        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
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        239..244
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   490 AA;  53965 MW;  3A39FA85AF2A6D11 CRC64;
     MANPLHLVLL GAALAGLLLS GSSVFISRRA ANDVLARTRR ANSFLEELKK GNLERECMEE
     NCSYEEALEV FEDREKTNEF WNKYVDGDQC ESNPCQNQGT CKDGLGMYTC SCVEGYEGQD
     CEPVTRKLCS LDNGGCDQFC KEEENSVLCS CASGYTLGDN GKSCISTELF PCGKVTLGRW
     RRSPATNSSE GPPEAPGPEQ QDDGNLTATE NPFNLLDSPE PPPEDDSSSL VRIVGGQDCR
     DGECPWQALL VNEENEGFCG GTILSEYHVL TAAHCLHQAK RFKVRVGDRD TEHEEGNEET
     HEVEVVVKHN RFVKETYDFD IAVLRLKTPI TFRRNVAPAC LPQKDWAEST LMAQKTGIVS
     GFGRTHEMGR LSTTLKMLEV PYVDRNSCKR SSSFTITQNM FCAGYDARPE DACQGDSGGP
     HVTRFRDTYF VTGIVSWGEG CARKGKFGVY TKVSNFLKWI EKSMRARAVP VAEAAGTPGP
     TQPTIKGSPS
//