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Database: UniProt
Entry: L5KUG3_PTEAL
LinkDB: L5KUG3_PTEAL
Original site: L5KUG3_PTEAL 
ID   L5KUG3_PTEAL            Unreviewed;       686 AA.
AC   L5KUG3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Hepatocyte growth factor-like protein {ECO:0000313|EMBL:ELK15104.1};
GN   ORFNames=PAL_GLEAN10009191 {ECO:0000313|EMBL:ELK15104.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK15104.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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   EMBL; KB030552; ELK15104.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5KUG3; -.
DR   STRING; 9402.L5KUG3; -.
DR   InParanoid; L5KUG3; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00108; KR; 3.
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; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24261:SF12; HEPATOCYTE GROWTH FACTOR-LIKE PROTEIN-RELATED; 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; 3.
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; 3.
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}; Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Serine protease homolog {ECO:0000256|PIRNR:PIRNR001152}.
FT   DOMAIN          65..149
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          153..230
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          234..312
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          329..365
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          373..452
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          488..684
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        235..312
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        256..295
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        284..307
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        336..359
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ   SEQUENCE   686 AA;  77700 MW;  00E28437A7D66D89 CRC64;
     MTAAPLTPEQ VQGRSDMVIR VMGKPSGYPL CQALRTREGV SSRPILLFKP GASSLFYWAW
     RRQRSPLNDF QVLRGAELQH LLHARRPEPW QEDVADAEEC AGRCKPLLDC RAFHYNVSSH
     GCQLLPWTQN SPHTQLQRSG RCDLFQKKDY VRTCIVDNGV EYRGTVAITT GGLPCQRWSH
     RFPNDHRYLP TLRNGLENNF CRNPDGDAGG PWCYTTDPAV RFQSCGIKSC REATCFWCNG
     EDYRGAVDRT ESGRECQRWD LQRPHPHPFE PGKFLDKHLD DNYCRNPDGS ERPWCYTTDP
     QVEREFCDLP RCGRTRGPGL GDAWKMWGAD LRENFCRNPD GSEAPWCFTS RPGMRVAFCY
     QIRRCTDDVR PKECYHGAGE KYRGSISKTR KGIPCQRWSA ETPHKSLFTP ISAPHAQLEE
     NFCRNPDGDS HGPWCYTTDP GTPFDYCALR RCDDDHPPSI LEPPDKVLFE KCGKRVPHLD
     QHGSKLRVVG GQPGNSPWTV SLRNRHMSLL GYEVWLGTMF QNPQPGEPGL QRVSVAKMVC
     GPSGSQLALL KLERPVTLNQ YVALICLPPE RYVVPPETKC EIAGWGESKA NSVLNVALLN
     VISNQECNIK HRGRVRESEM CTKALLAPAG ACEGDYGGPL ACFTHDCWVL EGIIIPNRVC
     ARPRWPAVFT RVSVFVDWIH KVMRLS
//
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