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
//