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Database: UniProt
Entry: A0A1L8HT91_XENLA
LinkDB: A0A1L8HT91_XENLA
Original site: A0A1L8HT91_XENLA 
ID   A0A1L8HT91_XENLA        Unreviewed;       595 AA.
AC   A0A1L8HT91;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Hepatocyte growth factor activator {ECO:0000313|RefSeq:XP_018083875.1};
GN   Name=hgfac.L {ECO:0000313|RefSeq:XP_018083875.1,
GN   ECO:0000313|Xenbase:XB-GENE-6488461};
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|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018083875.1};
RN   [1] {ECO:0000313|RefSeq:XP_018083875.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018083875.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018083875.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:PRU00479}.
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DR   RefSeq; XP_018083875.1; XM_018228386.2.
DR   AlphaFoldDB; A0A1L8HT91; -.
DR   STRING; 8355.A0A1L8HT91; -.
DR   PaxDb; 8355-A0A1L8HT91; -.
DR   GeneID; 108697902; -.
DR   KEGG; xla:108697902; -.
DR   AGR; Xenbase:XB-GENE-6488461; -.
DR   CTD; 108697902; -.
DR   Xenbase; XB-GENE-6488461; hgfac.L.
DR   OMA; ETRYEYF; -.
DR   OrthoDB; 4629979at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 108697902; Expressed in liver and 5 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:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00061; FN1; 1.
DR   CDD; cd00062; FN2; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000083; Fibronectin_type1.
DR   InterPro; IPR000562; FN_type2_dom.
DR   InterPro; IPR036943; FN_type2_sf.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
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; PTHR24264:SF43; HEPATOCYTE GROWTH FACTOR ACTIVATOR; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00039; fn1; 1.
DR   Pfam; PF00040; fn2; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00013; FNTYPEII.
DR   PRINTS; PR00018; KRINGLE.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00058; FN1; 1.
DR   SMART; SM00059; FN2; 1.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF57440; Kringle-like; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01253; FN1_1; 1.
DR   PROSITE; PS51091; FN1_2; 1.
DR   PROSITE; PS00023; FN2_1; 1.
DR   PROSITE; PS51092; FN2_2; 1.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DISULFID        116..133
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        135..144
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        199..216
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        218..227
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   595 AA;  67283 MW;  8D67B31D971B10FE CRC64;
     MDSLSRLSSL LAFLYCLTII AGALNKPRPL NLRPDGSHRF SHRALNLGQR MTEDGKKCKF
     PFRFGGRVYF TCINRPPFYR KWCATTHNYD RDREWGYCSN VDRDVATQNY CAENPCEHGG
     TCYNVAERGT YHCICPEGYT GTDCEKEKCF DHTHYEFYGI GESWPRIHSG RVESCTCFEG
     NNIMCLGGAR YTACIENPCL NGGACRLMIS TGKTVCGCRG QHVGKYCDID IKQGCYDYDN
     ATEYRGIKKN TQSGHSCLPW NSDMLYEEIH TGQEMNFISK GLGSHSYCRS PDDDEIPWCY
     LMKDRLVSWE HCQIPKCSNK GRRVVMQEDA AVPAQPKCGK KHEKRVVARG RILGGNSALP
     GAHPWIAGIY IGNYFCAGSL IHPCWVVSAA HCFADSPPKS KIHVVLGQQF FNQTTDVTQT
     FEVERYIFYD KYSVFKRNEH DIVLIKLKRV NKMCAKKNQF VQTICLPNVN VPFTDDHHCQ
     IAGWGRMHQD STEYAQNLQE AIVPLVPNNK CSSPEIYGAE ISENMFCAGY FDCTIDACQG
     DSGGPLACEK DKISYLWGIV SWGDGCGSFN KPGVYTKVSN YVDWINRKIM PKKTD
//
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