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Database: UniProt
Entry: A0A2K5WCZ4_MACFA
LinkDB: A0A2K5WCZ4_MACFA
Original site: A0A2K5WCZ4_MACFA 
ID   A0A2K5WCZ4_MACFA        Unreviewed;       650 AA.
AC   A0A2K5WCZ4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Macrophage stimulating 1 {ECO:0000313|Ensembl:ENSMFAP00000034994.2};
GN   Name=MST1 {ECO:0000313|Ensembl:ENSMFAP00000034994.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000034994.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000034994.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000034994.2}
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   RefSeq; XP_015301398.1; XM_015445912.1.
DR   AlphaFoldDB; A0A2K5WCZ4; -.
DR   STRING; 9541.ENSMFAP00000034994; -.
DR   Ensembl; ENSMFAT00000009227.2; ENSMFAP00000034994.2; ENSMFAG00000003952.2.
DR   GeneID; 102121457; -.
DR   KEGG; mcf:102121457; -.
DR   CTD; 4485; -.
DR   VEuPathDB; HostDB:ENSMFAG00000003952; -.
DR   GeneTree; ENSGT00940000159461; -.
DR   OrthoDB; 211181at2759; -.
DR   Proteomes; UP000233100; Chromosome 2.
DR   Bgee; ENSMFAG00000003952; Expressed in liver and 13 other cell types or tissues.
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; 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; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
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; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001152; HGF_MST1; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00018; KRINGLE.
DR   SMART; SM00130; KR; 4.
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; 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:UP000233100};
KW   Serine protease homolog {ECO:0000256|PIRNR:PIRNR001152}.
FT   DOMAIN          48..125
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          129..207
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          221..300
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          308..387
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          423..648
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        130..207
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        151..190
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        179..202
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        243..282
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        271..294
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ   SEQUENCE   650 AA;  73728 MW;  5BAB8D87889BED01 CRC64;
     MLRGPWAFHY NVSSHGCQLL PWTQHSPHTR LRHSGRCDLF QKKDYIRTCI MDNGVGYRGT
     VATTVDGLPC QAWSHKFPND HRYTPTLRNG LEENFCRNPD GDPGGPWCYT TNPAVRFQSC
     GIKSCREAAC VWCNGEDYRG AVDRTESGRE CQRWDLQHPH QHPFEPGKFL DQGLDDNYCR
     NPDGSERPWC YTTDPQLERE FCDLPRCGSE AQPRHEATTV SCFRGKGEGY RGTANTTTAG
     VPCQRWDAQI PHQHRFTPEK YACKDLRENF CRNPDGSEAP WCFTLRPGMR MAFCYQIRRC
     ADDVRPQDCY HGTGEQYRGT VSKTRKGVQC QRWSAETPHK PQFTFTPEPH AQLEENFCRN
     PDGDSHGPWC YTMDPGTPFD YCALRRCADD QPPSILDPPD QVQFEKCGKR VDRLDQRRSK
     LRVVGGHPGN SPWTVSLRNR QGQHFCGGSL VKEQWILTAR QCFSSCHMPL MGYEVWLGTL
     FQNPQHGEPG LQRVPVAKMV CGPSGSQLVL LKLERSVTLN QRVALICLPP EWYVVPPGTK
     CEIAGWGETK GTGNDTVLNV ALLNVISNQE CNIKHRGRVR ESEMCTDGLL APVGACEGDY
     GGPLACFTHN CWVLEGIIIP NRVCARSRWP AVFTRVSVFV DWIHKVMRLA
//
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