HGFL_BOVIN
ID HGFL_BOVIN Reviewed; 712 AA.
AC Q24K22;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Hepatocyte growth factor-like protein;
DE AltName: Full=Macrophage stimulatory protein;
DE AltName: Full=Macrophage-stimulating protein;
DE Short=MSP;
DE Contains:
DE RecName: Full=Hepatocyte growth factor-like protein alpha chain;
DE Contains:
DE RecName: Full=Hepatocyte growth factor-like protein beta chain;
DE Flags: Precursor;
GN Name=MST1; Synonyms=HGFL;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Dimer of an alpha chain and a beta chain linked by a disulfide
CC bond. Interacts (via beta chain) with MST1R (via SEMA domain).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- PTM: Cleaved after Arg-484, probably by HPN/Hepsin, to yield the active
CC form consisting of two disulfide-linked chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: The active site residues characteristic of serine proteases
CC appear to be absent from this protein, which may therefore lack
CC catalytic activity. {ECO:0000305}.
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DR EMBL; BC114002; AAI14003.1; -; mRNA.
DR RefSeq; NP_001069145.1; NM_001075677.2.
DR AlphaFoldDB; Q24K22; -.
DR SMR; Q24K22; -.
DR STRING; 9913.ENSBTAP00000030635; -.
DR MEROPS; S01.975; -.
DR PaxDb; Q24K22; -.
DR PRIDE; Q24K22; -.
DR GeneID; 514667; -.
DR KEGG; bta:514667; -.
DR CTD; 4485; -.
DR eggNOG; ENOG502QRJ0; Eukaryota.
DR InParanoid; Q24K22; -.
DR OrthoDB; 164039at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:2000479; P:regulation of cAMP-dependent protein kinase activity; ISS:UniProtKB.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR CDD; cd00108; KR; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.20.10; -; 4.
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 Pfam; PF00051; Kringle; 3.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001152; HGF_MST1; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00130; KR; 4.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 4.
DR PROSITE; PS00021; KRINGLE_1; 3.
DR PROSITE; PS50070; KRINGLE_2; 4.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Kringle; Reference proteome; Repeat;
KW Secreted; Serine protease homolog; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..712
FT /note="Hepatocyte growth factor-like protein"
FT /id="PRO_0000285888"
FT CHAIN 19..484
FT /note="Hepatocyte growth factor-like protein alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000285889"
FT CHAIN 485..712
FT /note="Hepatocyte growth factor-like protein beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000285890"
FT DOMAIN 21..105
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 109..186
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 190..268
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 283..362
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 370..449
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 485..710
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..78
FT /evidence="ECO:0000250"
FT DISULFID 60..66
FT /evidence="ECO:0000250"
FT DISULFID 110..186
FT /evidence="ECO:0000250"
FT DISULFID 131..169
FT /evidence="ECO:0000250"
FT DISULFID 157..181
FT /evidence="ECO:0000250"
FT DISULFID 284..362
FT /evidence="ECO:0000250"
FT DISULFID 305..344
FT /evidence="ECO:0000250"
FT DISULFID 333..356
FT /evidence="ECO:0000250"
FT DISULFID 371..449
FT /evidence="ECO:0000250"
FT DISULFID 392..432
FT /evidence="ECO:0000250"
FT DISULFID 420..444
FT /evidence="ECO:0000250"
FT DISULFID 469..589
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00315"
FT DISULFID 508..524
FT /evidence="ECO:0000250"
FT DISULFID 603..668
FT /evidence="ECO:0000250"
FT DISULFID 633..647
FT /evidence="ECO:0000250"
FT DISULFID 658..686
FT /evidence="ECO:0000250"
SQ SEQUENCE 712 AA; 79973 MW; 3BA3B1F750B36EFC CRC64;
MGWLPLLLLL IWFSGAPGQR SPLNDFQVLR GTELQHLLHS VGPGPWQEDV ANAEECAGLC
GPLLDCRAFH YNLSSHGCQL LPWTQHSPHT RLQRSGRCDL FQKKNYVRTC IVDNGVEYRG
TVAITVGGLP CQRWSHRFPN DHKFTPTLRN GLEENFCRNP DRDPGGPWCY TTDPAVRFQS
CGIKSCREAT CLWCNGEDYR GSVDSTESGR ECQRWDLQHP HPHPFEPGFW TKIWTTTIAG
IRTARSGPGA IPPTRRWRES SATYPAAVQR SEAQPSQEAT TLNCFRGKGE GYRGTVNTTA
AGVPCQRWDA QLPHQHRFAP EKYACKDLRE NFCRNPDGSE APWCFTSRPG MRMAFCYQIR
RCTDDVRPED CYHGAGELYR GSVSKTRKGI RCQNWSAETP HKPQFKHTSA PHTPLEENFC
RNPDGDSHGP WCYTTDPGTP FDYCALRRCD DDQQPSILET AHQVLFDKCG KRVTRVDPLH
SKLRVVGGQP GNSPWTVSLR NRQGQHFCGG SLVKEQWVLT ARQCFSSCHM SLVGYEVWLG
TLFQDPQPGE PDLQHIPMAK MVCGPSGSQL VLLKLERPVI LNQRVALICL PPERYVVPPG
TRCEIAGWGE TKGTGDDTVL NIALLSVISN QECNVKHRGR VRESEMCTAG LLAPVGACEG
DYGGPLACFT HDCWVLQGII IPNRVCARPR WPAVFMRVSV FVDWIHKVMR LG
