HGFL_MOUSE
ID HGFL_MOUSE Reviewed; 716 AA.
AC P26928; Q6GTL1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Hepatocyte growth factor-like protein;
DE AltName: Full=Macrophage stimulatory 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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=1832957; DOI=10.1021/bi00104a030;
RA Friezner Degen S.J., Stuart L.A., Han S., Jamison C.S.;
RT "Characterization of the mouse cDNA and gene coding for a hepatocyte growth
RT factor-like protein: expression during development.";
RL Biochemistry 30:9781-9791(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- TISSUE SPECIFICITY: Liver. Lower levels in lung, placenta and adrenal.
CC -!- DEVELOPMENTAL STAGE: Is expressed at low levels during gestation. Just
CC before birth the level increases dramatically and remains stable
CC afterwards.
CC -!- PTM: Cleaved after Arg-488, probably by HPN/Hepsin, to yield the active
CC form consisting of two disulfide-linked chains.
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; M74180; AAA50166.1; -; Genomic_DNA.
DR EMBL; M74181; AAA50167.1; -; mRNA.
DR EMBL; AK040934; BAC30752.1; -; mRNA.
DR EMBL; AK144824; BAE26084.1; -; mRNA.
DR EMBL; CH466560; EDL21265.1; -; Genomic_DNA.
DR EMBL; BC051393; AAH51393.1; -; mRNA.
DR CCDS; CCDS40766.1; -.
DR PIR; A40332; A40332.
DR RefSeq; NP_032269.3; NM_008243.3.
DR AlphaFoldDB; P26928; -.
DR SMR; P26928; -.
DR DIP; DIP-60723N; -.
DR IntAct; P26928; 2.
DR STRING; 10090.ENSMUSP00000035211; -.
DR MEROPS; S01.975; -.
DR GlyGen; P26928; 4 sites.
DR iPTMnet; P26928; -.
DR PhosphoSitePlus; P26928; -.
DR MaxQB; P26928; -.
DR PaxDb; P26928; -.
DR PeptideAtlas; P26928; -.
DR PRIDE; P26928; -.
DR ProteomicsDB; 269785; -.
DR TopDownProteomics; P26928; -.
DR Antibodypedia; 13649; 308 antibodies from 22 providers.
DR DNASU; 15235; -.
DR Ensembl; ENSMUST00000035211; ENSMUSP00000035211; ENSMUSG00000032591.
DR GeneID; 15235; -.
DR KEGG; mmu:15235; -.
DR UCSC; uc009ror.2; mouse.
DR CTD; 4485; -.
DR MGI; MGI:96080; Mst1.
DR VEuPathDB; HostDB:ENSMUSG00000032591; -.
DR eggNOG; ENOG502QRJ0; Eukaryota.
DR GeneTree; ENSGT00940000159461; -.
DR InParanoid; P26928; -.
DR OMA; YQIPRCT; -.
DR OrthoDB; 164039at2759; -.
DR PhylomeDB; P26928; -.
DR TreeFam; TF329901; -.
DR Reactome; R-MMU-8852405; Signaling by MST1.
DR BioGRID-ORCS; 15235; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Mst1; mouse.
DR PRO; PR:P26928; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P26928; protein.
DR Bgee; ENSMUSG00000032591; Expressed in left lobe of liver and 67 other tissues.
DR ExpressionAtlas; P26928; baseline and differential.
DR Genevisible; P26928; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005773; C:vacuole; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
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:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IDA:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; IMP:MGI.
DR GO; GO:0030879; P:mammary gland development; IMP:MGI.
DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IMP:MGI.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IMP:MGI.
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:0010758; P:regulation of macrophage chemotaxis; IMP:MGI.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd00108; KR; 4.
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; IPR043575; MSP_HGFL.
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; 4.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001152; HGF_MST1; 1.
DR PIRSF; PIRSF500185; MSP_HGFL; 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; 4.
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..716
FT /note="Hepatocyte growth factor-like protein"
FT /id="PRO_0000028088"
FT CHAIN 19..488
FT /note="Hepatocyte growth factor-like protein alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028089"
FT CHAIN 489..716
FT /note="Hepatocyte growth factor-like protein beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028090"
FT DOMAIN 19..105
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 110..186
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 191..268
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 292..370
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 379..457
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 489..714
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 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
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 191..268
FT /evidence="ECO:0000250"
FT DISULFID 194..333
FT /evidence="ECO:0000255"
FT DISULFID 212..251
FT /evidence="ECO:0000250"
FT DISULFID 240..263
FT /evidence="ECO:0000250"
FT DISULFID 292..370
FT /evidence="ECO:0000250"
FT DISULFID 313..352
FT /evidence="ECO:0000250"
FT DISULFID 341..364
FT /evidence="ECO:0000250"
FT DISULFID 379..457
FT /evidence="ECO:0000250"
FT DISULFID 400..440
FT /evidence="ECO:0000250"
FT DISULFID 428..452
FT /evidence="ECO:0000250"
FT DISULFID 477..593
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 512..528
FT /evidence="ECO:0000250"
FT DISULFID 607..672
FT /evidence="ECO:0000250"
FT DISULFID 637..651
FT /evidence="ECO:0000250"
FT DISULFID 662..690
FT /evidence="ECO:0000250"
FT CONFLICT 19
FT /note="Q -> P (in Ref. 1; AAA50167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 80619 MW; 15303C4E6105B46D CRC64;
MGWLPLLLLL VQCSRALGQR SPLNDFQLFR GTELRNLLHT AVPGPWQEDV ADAEECARRC
GPLLDCRAFH YNMSSHGCQL LPWTQHSLHT QLYHSSLCHL FQKKDYVRTC IMDNGVSYRG
TVARTAGGLP CQAWSRRFPN DHKYTPTPKN GLEENFCRNP DGDPRGPWCY TTNRSVRFQS
CGIKTCREAV CVLCNGEDYR GEVDVTESGR ECQRWDLQHP HSHPFQPEKF LDKDLKDNYC
RNPDGSERPW CYTTDPNVER EFCDLPSCGP NLPPTVKGSK SQRRNKGKAL NCFRGKGEDY
RGTTNTTSAG VPCQRWDAQS PHQHRFVPEK YACKDLRENF CRNPDGSEAP WCFTSRPGLR
MAFCHQIPRC TEELVPEGCY HGSGEQYRGS VSKTRKGVQC QHWSSETPHK PQFTPTSAPQ
AGLEANFCRN PDGDSHGPWC YTLDPDILFD YCALQRCDDD QPPSILDPPD QVVFEKCGKR
VDKSNKLRVV GGHPGNSPWT VSLRNRQGQH FCGGSLVKEQ WVLTARQCIW SCHEPLTGYE
VWLGTINQNP QPGEANLQRV PVAKAVCGPA GSQLVLLKLE RPVILNHHVA LICLPPEQYV
VPPGTKCEIA GWGESIGTSN NTVLHVASMN VISNQECNTK YRGHIQESEI CTQGLVVPVG
ACEGDYGGPL ACYTHDCWVL QGLIIPNRVC ARPRWPAIFT RVSVFVDWIN KVMQLE
