ID A0A3Q3MWE6_9TELE Unreviewed; 700 AA.
AC A0A3Q3MWE6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Macrophage stimulating 1 {ECO:0000313|Ensembl:ENSMAMP00000024619.1};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000024619.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000024619.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q3MWE6; -.
DR Ensembl; ENSMAMT00000025252.2; ENSMAMP00000024619.1; ENSMAMG00000016554.2.
DR GeneTree; ENSGT00940000159461; -.
DR Proteomes; UP000261640; 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: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; 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:UP000261640};
KW Serine protease homolog {ECO:0000256|PIRNR:PIRNR001152};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..700
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018784993"
FT DOMAIN 7..104
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 108..185
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 189..267
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 283..362
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 370..449
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 473..698
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 190..267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 211..250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 239..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 305..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 333..356
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 700 AA; 80347 MW; 5BD230CF7AB162E3 CRC64;
MEQFLSCVLL TVGLVTGYRS PLNDFQRSEG RELVPTSWNS ARVLLLPGLN LEDCATRCSQ
SLDCRAFNYE TRPTVTCKHL PWVGDGSNAE VKRNVNCDLY EKKVYVRKCI VGKGEDYRGK
VFTTKSALTC QQWWSKFPHD HRWTPTATNG LELNYCRNPD GDRIGPWCYT TDPERRYESC
NIPQCKDEVC ITCNGEEYRG QVDHTVSGRE CQRWDQQYPH QHIYQPEKYP DKSLDDNYCR
NPDASPVPWC YTTDPEMERE NCDIRKCTEV HVEKRQRSSF TTNCFRGRGE DYRGKVNETT
SGIPCQRWDA QYPHEHPFYP NTYECKGLEE NYCRNPDGSE APWCFTSVPE MRTALCLQIK
RCADDIEAED CYQENGKNYK GMVRKTRKGI TCQKWNVNTP HQTKINPRTH PEANLTENYC
RNPDGDQHGP WCYTTDPKTE FDYCAIKQCE KVEFSECGKR DDRQASQSPR LRIVNGIPGN
SPWTVSLRDR KGNHFCGGSL VNPRWVISTK QCFSSCYVDL PGYSAMMGTL FRDPQEGEPG
VQTIPLTKIV CGPSESQLVM LQLEYPAQFN ERVSQICLPP ERYIVAEETT CEIAGWGETR
GTGDETVLNV AHVPVINNKE CNKYFRGRVR ENEMCTSSFQ GGVGACERDY GGPLACQNRD
CWVLEGVIIP MRRCGHPGQP NIFIRVSVYV DWIKKVMEMA
//
