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Database: UniProt
Entry: F7CM56_ORNAN
LinkDB: F7CM56_ORNAN
Original site: F7CM56_ORNAN 
ID   F7CM56_ORNAN            Unreviewed;       724 AA.
AC   F7CM56;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Macrophage stimulating 1 {ECO:0000313|Ensembl:ENSOANP00000011368.2};
GN   Name=MST1 {ECO:0000313|Ensembl:ENSOANP00000011368.2};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000011368.2, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000011368.2, ECO:0000313|Proteomes:UP000002279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000011368.2,
RC   ECO:0000313|Proteomes:UP000002279};
RX   PubMed=18464734; DOI=10.1038/nature06936;
RA   Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA   Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA   Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA   Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA   Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA   Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA   Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA   Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA   Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA   Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA   Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA   Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA   Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA   Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA   Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA   Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA   Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA   Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA   de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT   "Genome analysis of the platypus reveals unique signatures of evolution.";
RL   Nature 453:175-183(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOANP00000011368.2}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000011368.2};
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; F7CM56; -.
DR   STRING; 9258.ENSOANP00000011368; -.
DR   Ensembl; ENSOANT00000011370.3; ENSOANP00000011368.2; ENSOANG00000007143.3.
DR   eggNOG; ENOG502QRJ0; Eukaryota.
DR   GeneTree; ENSGT00940000159461; -.
DR   TreeFam; TF329901; -.
DR   Proteomes; UP000002279; Chromosome X1.
DR   Bgee; ENSOANG00000007143; Expressed in liver and 1 other cell type or tissue.
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; 4.
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:UP000002279};
KW   Serine protease homolog {ECO:0000256|PIRNR:PIRNR001152};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..724
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5028189114"
FT   DOMAIN          20..106
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          110..187
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          191..269
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          298..377
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          385..464
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          497..722
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        192..269
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        213..252
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        241..264
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        320..359
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        348..371
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ   SEQUENCE   724 AA;  82350 MW;  BB8359F6AD16A08B CRC64;
     MWRRVLALLV LPLVSPRTSV QRSPLNDFQL LKATELRFLS QQAPEPWQEN TVSLEECARR
     CVRARTCRAF HYNLVSETCQ LLSQTQNSAH TLLQRNIHYD LFQKKDYVRE CIVERGATYR
     GTVATTIEGH PCQPWKEKYP FDHKFVPTAH NGLEENYCRN PDGAQGGPWC YTQNPAVRSQ
     VCGIKTCEEA TCLSCNGEDY RGSVDRTESG RECQRWDLQR PHKHPYDPNT YPDKNLDDNY
     CRNPDGSERP WCYTTDREHP REFCHIPRCR SLPDYRSPAA AREKGARRWQ PPEDTTLTCF
     RGKGEGYRGT ANTTVSGIPC QRWDAQTPHR HHFLPEKYQC KDLRENYCRN PDGSEGPWCF
     TSRSSLHMGF CFQIKRCPDD VKVEDCYPGN GAQYRGRVNK TRKGIICQRW ADKTPHQPQF
     SPTTAPHAHL EGNFCRNPDD DSHGPWCYTT DPNTPFDYCA LKPCDSNRKP SILETPDQVL
     FEKCGKRDDR RQEKLRVIGG QPGNSPWTVS LRNRQGQHFC GGTLVSEQWV ISARQCFSSC
     EATVRGYEAW LGTLFKNPGP NDPDLQVIPV VHLVCGPSNS QLVMLKLERP VTPSPRVAVI
     CLPPEKYVVP KGTKCEIAGW GETQGTGNPN VLNVATLHVM SNRDCNVKHR GRVQETEMCT
     EGLLAPAGAC EGDYGGPLAC FTHDCWVLEG IIIPNRVCAR PGWPAIFTRV SVYVDWIKKV
     MKLT
//
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