ID F1QLC3_DANRE Unreviewed; 504 AA.
AC F1QLC3; A0A8M1PG13;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=coagulation factor Xa {ECO:0000256|ARBA:ARBA00012181};
DE EC=3.4.21.6 {ECO:0000256|ARBA:ARBA00012181};
GN Name=f10 {ECO:0000313|Ensembl:ENSDARP00000106731,
GN ECO:0000313|RefSeq:NP_958870.3, ECO:0000313|ZFIN:ZDB-GENE-021206-9};
GN Synonyms=fi12c10 {ECO:0000313|RefSeq:NP_958870.3}, wu:fi12c10
GN {ECO:0000313|RefSeq:NP_958870.3};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000106731};
RN [1] {ECO:0000313|RefSeq:NP_958870.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_958870.3};
RX PubMed=19200601;
RA Jima D.D., Shah R.N., Orcutt T.M., Joshi D., Law J.M., Litman G.W.,
RA Trede N.S., Yoder J.A.;
RT "Enhanced transcription of complement and coagulation genes in the absence
RT of adaptive immunity.";
RL Mol. Immunol. 46:1505-1516(2009).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000106731}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000106731};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:NP_958870.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_958870.3};
RX PubMed=22047996;
RA Sukardi H., Zhang X., Lui E.Y., Ung C.Y., Mathavan S., Gong Z., Lam S.H.;
RT "Liver X receptor agonist T0901317 induced liver perturbation in zebrafish:
RT histological, gene set enrichment and expression analyses.";
RL Biochim. Biophys. Acta 1820:33-43(2012).
RN [4] {ECO:0000313|RefSeq:NP_958870.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_958870.3};
RX PubMed=22438865;
RA Gomez G., Lee J.H., Veldman M.B., Lu J., Xiao X., Lin S.;
RT "Identification of vascular and hematopoietic genes downstream of etsrp by
RT deep sequencing in zebrafish.";
RL PLoS ONE 7:E31658-E31658(2012).
RN [5] {ECO:0000313|Ensembl:ENSDARP00000106731, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000106731};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [6] {ECO:0000313|RefSeq:NP_958870.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_958870.3};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [7] {ECO:0000313|RefSeq:NP_958870.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_958870.3};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [8] {ECO:0000313|RefSeq:NP_958870.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_958870.3};
RX PubMed=28576875;
RA Hu Z., Liu Y., Huarng M.C., Menegatti M., Reyon D., Rost M.S., Norris Z.G.,
RA Richter C.E., Stapleton A.N., Chi N.C., Peyvandi F., Joung J.K.,
RA Shavit J.A.;
RT "Genome editing of factor X in zebrafish reveals unexpected tolerance of
RT severe defects in the common pathway.";
RL Blood 130:666-676(2017).
RN [9] {ECO:0000313|RefSeq:NP_958870.3}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_958870.3};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000256|ARBA:ARBA00008850}.
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; FP017167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_958870.3; NM_201462.3.
DR STRING; 7955.ENSDARP00000106731; -.
DR PaxDb; 7955-ENSDARP00000106731; -.
DR Ensembl; ENSDART00000124837; ENSDARP00000106731; ENSDARG00000088581.
DR Ensembl; ENSDART00000124837.3; ENSDARP00000106731.1; ENSDARG00000088581.4.
DR GeneID; 282670; -.
DR KEGG; dre:282670; -.
DR AGR; ZFIN:ZDB-GENE-021206-9; -.
DR CTD; 2159; -.
DR ZFIN; ZDB-GENE-021206-9; f10.
DR eggNOG; ENOG502QS4N; Eukaryota.
DR HOGENOM; CLU_006842_19_5_1; -.
DR OMA; QKDWAEA; -.
DR OrthoDB; 4629979at2759; -.
DR PhylomeDB; F1QLC3; -.
DR TreeFam; TF327329; -.
DR Reactome; R-DRE-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-DRE-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-DRE-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-DRE-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-DRE-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR Proteomes; UP000000437; Chromosome 1.
DR Bgee; ENSDARG00000088581; Expressed in liver and 26 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR GO; GO:0007599; P:hemostasis; IMP:ZFIN.
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; 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; 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 3: Inferred from homology;
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 Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_958870.3}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..504
FT /note="coagulation factor Xa"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_958870.3"
FT /id="PRO_5035035957"
FT DOMAIN 37..83
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 83..119
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 245..477
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 286
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 332
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 429
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT DISULFID 109..118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 504 AA; 56932 MW; 6E47D6650D02D7E2 CRC64;
MSWVFWNFIS LFVTHSVCAE VFLNTRDANQ VLIRQRRANS LFEEMKKGNM ERECIEERCN
YEEAREIFED VKKTDEFWHK YVDGDACLSH PCVNGGQCKD AIGPYTCFCQ QGFKGYNCEI
VIPELCENEN GGCDHFCEVM EKNVVCSCAN GYELAPNGKS CQSQDPFKCG VIYPKKTRSI
FFHTPNITES ENEEETELEA TIEPVYNHSN PLNNQTDSMF GLHELEIIEE EPILPVVSTA
GDGRIVNGVE CPPGDCPWQA LLINENNMGF CGGTILTEHF ILSAAHCMNE SLSIRVVVGE
YDTLVPEGRE ATHDVDEILI HKNYQPDTYH NDIALIKLSK PIKFTKYIIP ACLPEMKFAE
RVLMQQDDGL VSGFGRVREG GLSSTILQKL TVPYVNRAKC IESSNFKISG RMFCAGYDQE
EKDACQGDSG GPHVTRFKNT WFITGVVSWG EGCARKGKYG VYTQVSKYIM WINNAMTKVM
PETGASLKPK AKRELRHKTP IRRV
//
