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Database: UniProt
Entry: A0A1S3G699_DIPOR
LinkDB: A0A1S3G699_DIPOR
Original site: A0A1S3G699_DIPOR 
ID   A0A1S3G699_DIPOR        Unreviewed;       723 AA.
AC   A0A1S3G699;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Hepatocyte growth factor-like protein isoform X2 {ECO:0000313|RefSeq:XP_012883547.1};
GN   Name=Mst1 {ECO:0000313|RefSeq:XP_012883547.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012883547.1};
RN   [1] {ECO:0000313|RefSeq:XP_012883547.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012883547.1};
RG   RefSeq;
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   RefSeq; XP_012883547.1; XM_013028093.1.
DR   AlphaFoldDB; A0A1S3G699; -.
DR   GeneID; 105994542; -.
DR   CTD; 4485; -.
DR   InParanoid; A0A1S3G699; -.
DR   OrthoDB; 211181at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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:SF7; KRINGLE DOMAIN-CONTAINING PROTEIN; 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; 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:UP000081671};
KW   Serine protease homolog {ECO:0000256|PIRNR:PIRNR001152};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..723
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010359981"
FT   DOMAIN          13..105
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          109..186
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          190..268
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          296..375
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          383..460
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          496..721
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        191..268
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        212..251
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        240..263
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        318..357
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        346..369
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ   SEQUENCE   723 AA;  81224 MW;  0422CFAA69EFCA58 CRC64;
     MGWLALLLLL MQCLGPLGQR SPLNDFQLLR GTQLQNLLHA VVPGPWQEDV ANAEECARLC
     GPLLDCRAFH YNRSSHGCQL LPWTQNSPNT QIHHSGCCDL FQKKDYIRTC IMDKGVGYRG
     TVATTAGGLT CQSWNHRFPN DHRYTPTLQN GLEENFCRNP DGDSGGPWCY TTNPSVRFQS
     CGIKSCQEAA CVWCNGEDYR GSVDHTESGR ECQRWDLQYP HQHPFHPGKF MERGLDDNYC
     RNPDGSERPW CYTTDPQLER EFCAIPSCAP PLTKQFQSRF ISGSKAPPDQ VATTFNCFRG
     KGEGYRGTAN TTTAGVPCQR WDSQSPHQHG FSPEKYACKD LRENFCRNPD GSEAPWCFTT
     RPGMRVAFCY QIPRCTDEIL PEDCYQGSGK QYRGSVNKTR KGIPCQHWSA ETPHKPQFTP
     ASAPQLEKNF CRNPDGDSHG PWCYTTDPGT LFDYCALKHC NKDQLPSILK PPVPVQFEKC
     GKRVDRMDRW RSMMRVVGGQ PGNSPWTVSL RNRKGEHFCG GSLVKEKWVL TARQCFSSCH
     EPLTGYEVWS GTLFQNPQPG EPDLQRVPIA KMVCGPSSSQ LVLLKLARSV TLNQRVALIC
     LPPERYVVPP RTKCEIAGWG EGKGSSGASV LHVASMNVIS NQECNVKHRG RVHENEMCTE
     GLLVPTGACE GDYGGPLACF THDCWVLQGI IIPNRVCARP RWPAIFMRVS VFVDWIQKVM
     QLE
//
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