ID A0A401T147_CHIPU Unreviewed; 812 AA.
AC A0A401T147;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Hepatocyte growth factor activator {ECO:0008006|Google:ProtNLM};
GN ORFNames=chiPu_0014870 {ECO:0000313|EMBL:GCC36376.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC36376.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC36376.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC36376.1}.
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DR EMBL; BEZZ01000820; GCC36376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401T147; -.
DR STRING; 137246.A0A401T147; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
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:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00108; KR; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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:SF54; HEPATOCYTE GROWTH FACTOR ACTIVATOR-LIKE; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00008; EGF; 4.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00051; Kringle; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00013; FNTYPEII.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00058; FN1; 2.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00130; KR; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57440; Kringle-like; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01253; FN1_1; 1.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS00021; KRINGLE_1; 2.
DR PROSITE; PS50070; KRINGLE_2; 2.
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, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..812
FT /note="Hepatocyte growth factor activator"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019240535"
FT DOMAIN 57..104
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 109..147
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 190..228
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 234..316
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 318..356
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 399..437
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 443..525
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 565..803
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 21..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 118..135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 137..146
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"
FT DISULFID 327..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 346..355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 408..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 427..436
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 812 AA; 91820 MW; E9FA64C763A881B3 CRC64;
MLAQYSIILS WCCLAGGLTQ KSPSDSAWRL KSGIPRHGDE QREPPHPLQH PRQVFTDNGW
PCVFPFRFAS KLHRTCIPHR MTNRKWCATT PNFDKDEQWG YCEWIQPLTH DYCESDPCWH
GAACVNIPRH NSYQCICKDP FTGRHCEKEK CFERQHLKYY DFGKTWMRSL HGDIEKCICT
EGGIHSEIVR SKACEINPCL HGGTCHEVED SGESVCECSE NYVGEFCEID TAANCYENNG
SSYRGAVAQT ASGTDCLAWT SNFISPEFNI KDVEEPLRLG LGDHPYCRNT DNEQEPWCYT
LTDDHISWDF CDIPQCPKED PCTSHPCKNG GTCIRDPLLN SYHCRCHDEF TGVNCQEVKC
FDSSHYRYFL IGERWVRIVG DEVENCVCTG SGPECDSVQY EECRVNQCLH DGQCRAVQDA
EEIICQCRAG FAGKYCDIDK NATCYEGNGM SYKGPEDESA LGIECLPWNE DFLHDQLNIS
SLEGALQLGL GDHSYCRNPD GDEKPWCYIM LDNHVSWEHC NIPKCGTMSF WSKRIPPIAR
FTVSIFPQQS PSCGKQAQKG PKPRIVGGSS ALPGSHPWLA AIYIGRNFCT GSLIFSCWVV
SAAHCFIDSP LTSSIRVVLG QHHFNKTSKN TQVFEIEKYI LHSKYNVFDE TIHDIALLKL
KKENKRCATK TRFVQTLCLP SVTDSFPDCT KCQIAGWGHT HENATTYPCT LQEATVRLIP
QELCSSNFLY GTEVTPNMIC AGEMMKSVDA CQGDSGGPLV CYKGDTAYLY GIVSWGEGCA
KMNKPGVYTR VTKYINWIYR KIKHRPKYNQ KG
//
