ID M3WKC7_FELCA Unreviewed; 477 AA.
AC M3WKC7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Coagulation factor X {ECO:0000256|ARBA:ARBA00040873};
DE EC=3.4.21.6 {ECO:0000256|ARBA:ARBA00012181};
DE AltName: Full=Stuart factor {ECO:0000256|ARBA:ARBA00041550};
GN Name=F10 {ECO:0000313|Ensembl:ENSFCAP00000013217.4,
GN ECO:0000313|VGNC:VGNC:62019};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000013217.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000013217.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013217.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000013217.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013217.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000013217.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013217.4};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037158}.
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 Evidence={ECO:0000256|ARBA:ARBA00001239};
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.
CC {ECO:0000256|ARBA:ARBA00038655}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AANG04001781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003980607.1; XM_003980558.2.
DR AlphaFoldDB; M3WKC7; -.
DR STRING; 9685.ENSFCAP00000013217; -.
DR PaxDb; 9685-ENSFCAP00000013217; -.
DR Ensembl; ENSFCAT00000014248.6; ENSFCAP00000013217.4; ENSFCAG00000014244.6.
DR GeneID; 101098029; -.
DR KEGG; fca:101098029; -.
DR CTD; 2159; -.
DR VGNC; VGNC:62019; F10.
DR eggNOG; ENOG502QS4N; Eukaryota.
DR GeneTree; ENSGT00940000157694; -.
DR HOGENOM; CLU_006842_19_5_1; -.
DR InParanoid; M3WKC7; -.
DR OMA; QKDWAEA; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000011712; Chromosome A1.
DR Bgee; ENSFCAG00000014244; Expressed in liver and 2 other cell types or tissues.
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; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IEA:Ensembl.
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; SSF57196; EGF/Laminin; 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; 1.
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 4: Predicted;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..477
FT /note="Coagulation factor X"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014157758"
FT DOMAIN 40..86
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 86..122
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 238..470
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 181..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 422
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT DISULFID 112..121
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 477 AA; 52576 MW; D9D7C0242F1D64C0 CRC64;
MAGPRCLVLL SASLTCLLLL GDSVFLPTEH ASSVLGRVRR ANSFWEEMKK GNLERECMEE
TCSFEEAREV FEDTAKTTEF WNKYKDGDQC ESNPCQNQGK CMDSLGGYTC TCLEGYEGKN
CELSMRKACS LDNGDCDQFC SEEQGSVVCA CASGYVLADD GKSCVSTGPF PCGKRTLTRR
KRSAETAHGG EGPSETSEAD VQDQHPEDLP PTDSPLYLQP LNKTEASPVE DSSNLIRIVG
GQNCPDGECP WQALLINEEN EGFCGGTILS EYHVLTAAHC LHQAKRFKVR VGERDTGSEE
GDEVAHEVDV IIKHNKFVRE TYDFDIAVIR LRTPITFRRN VAPACLPQKD WAESTLMAQK
TGIVSGFGKT HEKGRPSTIL KMLEVPYVDR NTCKLSSSFT ITQNMFCAGY DTNPEDACQG
DSGGPHVTRF KDTYFVTGIV SWGEGCARKG KYGVYTKVTN FLKWIDKSMR ARAGAQG
//
