ID A0A3P8QWI7_ASTCA Unreviewed; 712 AA.
AC A0A3P8QWI7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Hepatocyte growth factor-like {ECO:0000313|Ensembl:ENSACLP00000033908.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000033908.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000033908.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000033908.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000256|PIRNR:PIRNR001152}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR AlphaFoldDB; A0A3P8QWI7; -.
DR STRING; 8154.ENSACLP00000033908; -.
DR Ensembl; ENSACLT00000034715.1; ENSACLP00000033908.1; ENSACLG00000022967.1.
DR GeneTree; ENSGT00940000156019; -.
DR OMA; NSVTMPM; -.
DR Proteomes; UP000265100; Chromosome 17.
DR Bgee; ENSACLG00000022967; Expressed in zone of skin and 1 other cell type or tissue.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IEA:Ensembl.
DR GO; GO:0021603; P:cranial nerve formation; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00108; KR; 4.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR024174; HGF/MST1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24261:SF8; HEPATOCYTE GROWTH FACTOR; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
DR Pfam; PF00051; Kringle; 4.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001152; HGF_MST1; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 4.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF57440; Kringle-like; 4.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00021; KRINGLE_1; 4.
DR PROSITE; PS50070; KRINGLE_2; 4.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Serine protease homolog {ECO:0000256|ARBA:ARBA00022542,
KW ECO:0000256|PIRNR:PIRNR001152}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..712
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017997640"
FT DOMAIN 24..113
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 117..196
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 200..278
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 293..372
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 381..459
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 486..707
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 201..278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 222..261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 250..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 315..354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 343..366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 382..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 712 AA; 81619 MW; 5C5412ACC92D6B61 CRC64;
MRTYVWIYQA LLCVLLTIVD TGCCRKSRQL LQRYEKTESH MLVCTDCPQL PLIRTSNSEE
RCARKCKVKK NFNCRAFNFQ RHSKKCHLLP FDRFTNNVQK QASINFTLYE KKDYIRECIT
GTMDNYRGRR SWTKSNITCQ AWSDNNINEH TFYPDRYPTQ DLRHNFCRNP NNDPGGPWCY
TTDPNVRAEE CGIPQCSEDV CMTCNGEDYR GKMDHTESGK ECQRWDSARP HKHPFQPKKY
RDKDLKDNYC RNPNNRLRPW CYTMDPKTPW EYCNITVCGS DPTEDSDVEV TTSCVQGKGT
DYQGTMNVTP EGVTCQRWDS QFPHSHSFLP QNYKCKDLRE NYCRNPDGAD YPWCFTTNPN
QRIANCTHIP RCGAEATQKA ECYEENGETY RGTLSITRSG IPCADWSHHI NSGDSHSTVS
HVGLEKNYCR NPDRDRHGAW CYTSPNNRLA WDYCKLKHCD SATKAPQTNI QTRPKISCFV
HINTRIVGGH QVRGTDGSWV VSIQRQKVHL CGGSLIRENW VLTDQQCFTS CVPDLRDYSV
QVGLHHLDES KNRPRLRVSR LICGPDGSNL VMLKLADPAP VSEGASTIHL PVKDCRIPEG
TNCTMYGWGE TKNTGHDEAL NSVIMPMVDN DMCSHIKEDA GESRICAGGK RGEGVCDRDY
GGPLVCQEHE RKVIIGVSIQ RTKCASSQPA LFVNVAFYSE WIYKVFRLYP NV
//
