ID Q6PAG2_XENLA Unreviewed; 462 AA.
AC Q6PAG2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=coagulation factor Xa {ECO:0000256|ARBA:ARBA00012181};
DE EC=3.4.21.6 {ECO:0000256|ARBA:ARBA00012181};
GN Name=f10.L {ECO:0000313|RefSeq:NP_001083161.1,
GN ECO:0000313|Xenbase:XB-GENE-971438};
GN Synonyms=f10 {ECO:0000313|RefSeq:NP_001083161.1,
GN ECO:0000313|Xenbase:XB-GENE-971438}, MGC68454
GN {ECO:0000313|EMBL:AAH60330.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH60330.1};
RN [1] {ECO:0000313|RefSeq:NP_001083161.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH60330.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver {ECO:0000313|EMBL:AAH60330.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001083161.1}
RP IDENTIFICATION.
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; BC060330; AAH60330.1; -; mRNA.
DR RefSeq; NP_001083161.1; NM_001089692.1.
DR STRING; 8355.Q6PAG2; -.
DR MEROPS; S01.216; -.
DR PaxDb; 8355-Q6PAG2; -.
DR GeneID; 398778; -.
DR KEGG; xla:398778; -.
DR AGR; Xenbase:XB-GENE-971438; -.
DR CTD; 398778; -.
DR Xenbase; XB-GENE-971438; f10.L.
DR OMA; QKDWAEA; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 398778; Expressed in liver and 13 other cell types or tissues.
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:InterPro.
DR GO; GO:0007596; P:blood coagulation; IEA:InterPro.
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; 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 2: Evidence at transcript level;
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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001083161.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..462
FT /note="coagulation factor Xa"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001083161.1"
FT /id="PRO_5033206684"
FT DOMAIN 39..85
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 85..121
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 228..458
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 269
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 313
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 410
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT DISULFID 111..120
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 462 AA; 52039 MW; F54C126849CAAC3C CRC64;
MAGQTCLLIL IALPAVLLQQ ATNVFLKHGN AHNILRAKRA NSGFEEFKKG NLERECYEER
CSFEEAREVF ENEDKTREFW NKYYDDDQCK SNPCQYGGSC KDGINEYTCF CNPGFEGKNC
ETVKLQLCSL NNGDCDQFCK VVDRFIVCSC TNGYVLGENG KSCIPTDKYS CGRRHMRREK
RAAEILKNDT ESHTDNQSEV KLNQTDTLLE SNVTRNNIFD ENEPNVRIVG GRDCDPGECP
WQALLVDDEN EGFCGGTILS RELILTAAHC INQTKSMKVV VGALNTKKTE GAVHNVEKIS
IHPRFVKLTY DYDMAVIKLK QAINFTENII PACIPEPEFA EQVLMNEPDA MVSGFGRLQE
RGRQASYLQM LQVPYIKRHR CKESSTFAIT DNMFCAGFDT EVKDACQGDS GGPHVTPFKG
TYFVTGIVSW GEGCARKGKF GVYTKVSKLN RFLKSVLKKY PL
//
