ID G3XAK1_HUMAN Unreviewed; 725 AA. AC G3XAK1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 13-FEB-2019, entry version 82. DE SubName: Full=Hepatocyte growth factor-like protein {ECO:0000313|Ensembl:ENSP00000414287}; DE SubName: Full=Macrophage stimulating 1 (Hepatocyte growth factor-like), isoform CRA_b {ECO:0000313|EMBL:EAW65000.1}; GN Name=MST1 {ECO:0000313|EMBL:EAW65000.1, GN ECO:0000313|Ensembl:ENSP00000414287}; GN ORFNames=hCG_2001992 {ECO:0000313|EMBL:EAW65000.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000414287, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|EMBL:EAW65000.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., RA Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., RA Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G., RA Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., RA Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., RA Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., RA Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., RA Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., RA Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., RA Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., RA Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., RA Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., RA Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., RA Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., RA Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., RA Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., RA Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., RA Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., RA Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., RA Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., RA Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., RA Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., RA Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., RA Kline L., Koduru S., Love A., Mann F., May D., McCawley S., RA McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., RA Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., RA Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., RA Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., RA Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., RA Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., RA Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., RA Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., RA Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., RA Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., RA Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., RA Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., RA Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., RA Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., RA McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., RA Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|EMBL:EAW65000.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSP00000414287, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] {ECO:0000313|Ensembl:ENSP00000414287} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen CC subfamily. {ECO:0000256|PIRNR:PIRNR001152}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC099668; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW65000.1; -; Genomic_DNA. DR RefSeq; NP_066278.3; NM_020998.3. DR UniGene; Hs.349110; -. DR UniGene; Hs.512587; -. DR jPOST; G3XAK1; -. DR MaxQB; G3XAK1; -. DR Ensembl; ENST00000449682; ENSP00000414287; ENSG00000173531. DR GeneID; 4485; -. DR KEGG; hsa:4485; -. DR UCSC; uc003cxg.4; human. DR CTD; 4485; -. DR EuPathDB; HostDB:ENSG00000173531.15; -. DR HGNC; HGNC:7380; MST1. DR OpenTargets; ENSG00000173531; -. DR eggNOG; ENOG410IDXR; Eukaryota. DR eggNOG; COG5640; LUCA. DR GeneTree; ENSGT00940000159461; -. DR OMA; FHYNVSS; -. DR OrthoDB; 164039at2759; -. DR TreeFam; TF329901; -. DR ChiTaRS; MST1; human. DR GenomeRNAi; 4485; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000173531; Expressed in 88 organ(s), highest expression level in right lobe of liver. DR ExpressionAtlas; G3XAK1; baseline and differential. DR GO; GO:0005773; C:vacuole; IEA:Ensembl. DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl. DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl. DR GO; GO:0060763; P:mammary duct terminal end bud growth; IEA:Ensembl. DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0010758; P:regulation of macrophage chemotaxis; IEA:Ensembl. DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR CDD; cd00108; KR; 4. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.20.10; -; 4. DR InterPro; IPR024174; HGF-like. 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; 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 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 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00121, KW ECO:0000256|SAAS:SAAS00045912}; KW Kringle {ECO:0000256|PROSITE-ProRule:PRU00121, KW ECO:0000256|SAAS:SAAS00045973}; KW Proteomics identification {ECO:0000213|MaxQB:G3XAK1, KW ECO:0000213|PeptideAtlas:G3XAK1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Serine protease homolog {ECO:0000256|PIRNR:PIRNR001152}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 725 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015091868. FT DOMAIN 27 119 Apple. {ECO:0000259|PROSITE:PS50948}. FT DOMAIN 123 200 Kringle. {ECO:0000259|PROSITE:PS50070}. FT DOMAIN 204 282 Kringle. {ECO:0000259|PROSITE:PS50070}. FT DOMAIN 296 375 Kringle. {ECO:0000259|PROSITE:PS50070}. FT DOMAIN 383 462 Kringle. {ECO:0000259|PROSITE:PS50070}. FT DOMAIN 498 723 Peptidase S1. FT {ECO:0000259|PROSITE:PS50240}. FT DISULFID 205 282 {ECO:0000256|PROSITE-ProRule:PRU00121}. FT DISULFID 226 265 {ECO:0000256|PROSITE-ProRule:PRU00121}. FT DISULFID 254 277 {ECO:0000256|PROSITE-ProRule:PRU00121}. FT DISULFID 318 357 {ECO:0000256|PROSITE-ProRule:PRU00121}. FT DISULFID 346 369 {ECO:0000256|PROSITE-ProRule:PRU00121}. SQ SEQUENCE 725 AA; 81999 MW; B222E0BDAC020D03 CRC64; MGLWWVTVQP PARRMGWLPL LLLLTQCLGV PGQRSPLNDF QVLRGTELQH LLHAVVPGPW QEDVADAEEC AGRCGPLMDC RAFHYNVSSH GCQLLPWTQH SPHTRLRRSG RCDLFQKKDY VRTCIMNNGV GYRGTMATTV GGLPCQAWSH KFPNDHKYTP TLRNGLEENF CRNPDGDPGG PWCYTTDPAV RFQSCGIKSC REAACVWCNG EEYRGAVDRT ESGRECQRWD LQHPHQHPFE PGKFLDQGLD DNYCRNPDGS ERPWCYTTDP QIEREFCDLP RCGSEAQPRQ EATTVSCFRG KGEGYRGTAN TTTAGVPCQR WDAQIPHQHR FTPEKYACKD LRENFCRNPD GSEAPWCFTL RPGMRAAFCY QIRRCTDDVR PQDCYHGAGE QYRGTVSKTR KGVQCQRWSA ETPHKPQFTF TSEPHAQLEE NFCRNPDGDS HGPWCYTMDP RTPFDYCALR RCADDQPPSI LDPPDQVQFE KCGKRVDRLD QRRSKLRVVG GHPGNSPWTV SLRNRQGQHF CGGSLVKEQW ILTARQCFSS CHMPLTGYEV WLGTLFQNPQ HGEPSLQRVP VAKMVCGPSG SQLVLLKLER SVTLNQRVAL ICLPPEWYVV PPGTKCEIAG WGETKGTGND TVLNVALLNV ISNQECNIKH RGRVRESEMC TEGLLAPVGA CEGDYGGPLA CFTHNCWVLE GIIIPNRVCA RSRWPAVFTR VSVFVDWIHK VMRLG //