HGF_HUMAN
ID HGF_HUMAN Reviewed; 728 AA.
AC P14210; A1L3U6; Q02935; Q13494; Q14519; Q3KRB2; Q8TCE2; Q9BYL9; Q9BYM0;
AC Q9UDU6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 247.
DE RecName: Full=Hepatocyte growth factor;
DE AltName: Full=Hepatopoietin-A;
DE AltName: Full=Scatter factor;
DE Short=SF;
DE Contains:
DE RecName: Full=Hepatocyte growth factor alpha chain;
DE Contains:
DE RecName: Full=Hepatocyte growth factor beta chain;
DE Flags: Precursor;
GN Name=HGF; Synonyms=HPTA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=2528952; DOI=10.1016/0006-291x(89)92316-4;
RA Miyazawa K., Tsubouchi H., Naka D., Takahashi K., Okigaki M., Arakaki N.,
RA Nakayama H., Hirono S., Sakiyama O., Takahashi K., Gohda E., Daikuhara Y.,
RA Kitamura N.;
RT "Molecular cloning and sequence analysis of cDNA for human hepatocyte
RT growth factor.";
RL Biochem. Biophys. Res. Commun. 163:967-973(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 55-73 AND
RP 495-520.
RC TISSUE=Liver;
RX PubMed=2531289; DOI=10.1038/342440a0;
RA Nakamura T., Nishizawa T., Hagiya M., Seki T., Shimonishi M., Sugimura A.,
RA Tashiro K., Shimizu S.;
RT "Molecular cloning and expression of human hepatocyte growth factor.";
RL Nature 342:440-443(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Leukocyte;
RX PubMed=2145836; DOI=10.1016/s0006-291x(05)80212-8;
RA Seki T., Ihara I., Sugimura A., Shimonishi M., Nishizawa T., Asami O.,
RA Hagiya M., Nakamura T., Shimizu S.;
RT "Isolation and expression of cDNA for different forms of hepatocyte growth
RT factor from human leukocyte.";
RL Biochem. Biophys. Res. Commun. 172:321-327(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=1831432; DOI=10.1016/0378-1119(91)90080-u;
RA Seki T., Hagiya M., Shimonishi M., Nakamura T., Shimizu S.;
RT "Organization of the human hepatocyte growth factor-encoding gene.";
RL Gene 102:213-219(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=1826653; DOI=10.1111/j.1432-1033.1991.tb15876.x;
RA Miyazawa K., Kitamura A., Naka D., Kitamura N.;
RT "An alternatively processed mRNA generated from human hepatocyte growth
RT factor gene.";
RL Eur. J. Biochem. 197:15-22(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND PROTEIN SEQUENCE OF 583-592.
RC TISSUE=Lung fibroblast;
RX PubMed=1824873; DOI=10.1073/pnas.88.2.415;
RA Rubin J.S., Chan A.M.-L., Bottaro D.P., Burgess W.H., Taylor W.G.,
RA Cech A.C., Hirschfield D.W., Wong J., Miki T., Finch P.W., Aaronson S.A.;
RT "A broad-spectrum human lung fibroblast-derived mitogen is a variant of
RT hepatocyte growth factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:415-419(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Embryonic fibroblast;
RX PubMed=1831266; DOI=10.1073/pnas.88.16.7001;
RA Weidner K.M., Arakaki N., Hartmann G., Vandekerckhove J., Weingart S.,
RA Rieder H., Fonatsch C., Tsubouchi H., Hishida T., Daikuhara Y.,
RA Birchmeier W.;
RT "Evidence for the identity of human scatter factor and human hepatocyte
RT growth factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7001-7005(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=1720571; DOI=10.1126/science.1720571;
RA Chan A.M.-L., Rubin J.S., Bottaro D.P., Hirschfield D.W., Chedid M.,
RA Aaronson S.A.;
RT "Identification of a competitive HGF antagonist encoded by an alternative
RT transcript.";
RL Science 254:1382-1385(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND MUTAGENESIS OF ARG-494.
RX PubMed=1280830; DOI=10.1073/pnas.89.23.11574;
RA Hartmann G., Naldini L., Weidner K.M., Sachs M., Vigna E., Comoglio P.M.,
RA Birchmeier W.;
RT "A functional domain in the heavy chain of scatter factor/hepatocyte growth
RT factor binds the c-Met receptor and induces cell dissociation but not
RT mitogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11574-11578(1992).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RX PubMed=8662798; DOI=10.1074/jbc.271.22.13110;
RA Cioce V., Csaky K.G., Chan A.M.-L., Bottaro D.P., Taylor W.G., Jensen R.,
RA Aaronson S.A., Rubin J.S.;
RT "Hepatocyte growth factor (HGF)/NK1 is a naturally occurring HGF/scatter
RT factor variant with partial agonist/antagonist activity.";
RL J. Biol. Chem. 271:13110-13115(1996).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-304 AND TYR-330.
RG NIEHS SNPs program;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6).
RC TISSUE=Brain;
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).
RN [15]
RP NUCLEOTIDE SEQUENCE OF 1-208 AND 249-695 (ISOFORM 1).
RX PubMed=1832556; DOI=10.1021/bi00102a007;
RA Miyazawa K., Kitamura A., Kitamura N.;
RT "Structural organization and the transcription initiation site of the human
RT hepatocyte growth factor gene.";
RL Biochemistry 30:9170-9176(1991).
RN [16]
RP SIGNAL SEQUENCE CLEAVAGE SITE, AND PYROGLUTAMATE FORMATION AT GLN-32.
RX PubMed=1826837; DOI=10.1016/0006-291x(91)91616-k;
RA Yoshiyama Y., Arakaki N., Naka D., Takahashi K., Hirono S., Kondo J.,
RA Nakayama H., Gohda E., Kitamura N., Tsubouchi H., Ishii T., Hishida T.,
RA Daikuhara Y.;
RT "Identification of the N-terminal residue of the heavy chain of both native
RT and recombinant human hepatocyte growth factor.";
RL Biochem. Biophys. Res. Commun. 175:660-667(1991).
RN [17]
RP GLYCOSYLATION AT THR-476.
RX PubMed=1482348; DOI=10.1016/0006-291x(92)90219-b;
RA Shimizu N., Hara H., Sogabe T., Sakai H., Ihara I., Inoue H., Nakamura T.,
RA Shimizu S.;
RT "Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on
RT the alpha chain.";
RL Biochem. Biophys. Res. Commun. 189:1329-1335(1992).
RN [18]
RP MUTAGENESIS.
RX PubMed=1321034; DOI=10.1002/j.1460-2075.1992.tb05315.x;
RA Lokker N.A., Mark M.R., Luis E.A., Bennett G.L., Robbins K.A., Baker J.B.,
RA Godowski P.J.;
RT "Structure-function analysis of hepatocyte growth factor: identification of
RT variants that lack mitogenic activity yet retain high affinity receptor
RT binding.";
RL EMBO J. 11:2503-2510(1992).
RN [19]
RP INVOLVEMENT IN DFNB39.
RX PubMed=19576567; DOI=10.1016/j.ajhg.2009.06.003;
RA Schultz J.M., Khan S.N., Ahmed Z.M., Riazuddin S., Waryah A.M., Chhatre D.,
RA Starost M.F., Ploplis B., Buckley S., Velasquez D., Kabra M., Lee K.,
RA Hassan M.J., Ali G., Ansar M., Ghosh M., Wilcox E.R., Ahmad W., Merlino G.,
RA Leal S.M., Riazuddin S., Friedman T.B., Morell R.J.;
RT "Noncoding mutations of HGF are associated with nonsyndromic hearing loss,
RT DFNB39.";
RL Am. J. Hum. Genet. 85:25-39(2009).
RN [20]
RP INTERACTION WITH SRPX2.
RX PubMed=22242148; DOI=10.1371/journal.pone.0027922;
RA Tanaka K., Arao T., Tamura D., Aomatsu K., Furuta K., Matsumoto K.,
RA Kaneda H., Kudo K., Fujita Y., Kimura H., Yanagihara K., Yamada Y.,
RA Okamoto I., Nakagawa K., Nishio K.;
RT "SRPX2 is a novel chondroitin sulfate proteoglycan that is overexpressed in
RT gastrointestinal cancer.";
RL PLoS ONE 7:E27922-E27922(2012).
RN [21]
RP STRUCTURE BY NMR OF 31-127.
RX PubMed=9493272; DOI=10.1016/s0969-2126(98)00012-4;
RA Zhou H., Mazzulla M.J., Kaufman J.D., Stahl S.J., Wingfield P.T.,
RA Rubin J.S., Bottaro D.P., Byrd R.A.;
RT "The solution structure of the N-terminal domain of hepatocyte growth
RT factor reveals a potential heparin-binding site.";
RL Structure 6:109-116(1998).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 35-210.
RX PubMed=9817840; DOI=10.1016/s0969-2126(98)00138-5;
RA Ultsch M., Lokker N.A., Godowski P.J., de Vos A.M.;
RT "Crystal structure of the NK1 fragment of human hepatocyte growth factor at
RT 2.0-A resolution.";
RL Structure 6:1383-1393(1998).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.22 ANGSTROMS) OF 495-728 IN COMPLEX WITH MET,
RP FUNCTION, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=15167892; DOI=10.1038/sj.emboj.7600243;
RA Stamos J., Lazarus R.A., Yao X., Kirchhofer D., Wiesmann C.;
RT "Crystal structure of the HGF beta-chain in complex with the Sema domain of
RT the Met receptor.";
RL EMBO J. 23:2325-2335(2004).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 28-289, DISULFIDE BONDS, AND
RP FUNCTION.
RX PubMed=20624990; DOI=10.1073/pnas.1005183107;
RA Tolbert W.D., Daugherty-Holtrop J., Gherardi E., Vande Woude G., Xu H.E.;
RT "Structural basis for agonism and antagonism of hepatocyte growth factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13264-13269(2010).
CC -!- FUNCTION: Potent mitogen for mature parenchymal hepatocyte cells, seems
CC to be a hepatotrophic factor, and acts as a growth factor for a broad
CC spectrum of tissues and cell types. Activating ligand for the receptor
CC tyrosine kinase MET by binding to it and promoting its dimerization.
CC {ECO:0000269|PubMed:15167892, ECO:0000269|PubMed:20624990}.
CC -!- SUBUNIT: Dimer of an alpha chain and a beta chain linked by a disulfide
CC bond. Interacts with SRPX2; the interaction increases HGF mitogenic
CC activity. {ECO:0000269|PubMed:15167892, ECO:0000269|PubMed:22242148}.
CC -!- INTERACTION:
CC P14210; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1039104, EBI-10173507;
CC P14210; P14210: HGF; NbExp=2; IntAct=EBI-1039104, EBI-1039104;
CC P14210; P50222: MEOX2; NbExp=3; IntAct=EBI-1039104, EBI-748397;
CC P14210; P08581: MET; NbExp=7; IntAct=EBI-1039104, EBI-1039152;
CC P14210; P16056: Met; Xeno; NbExp=2; IntAct=EBI-1039104, EBI-1798780;
CC P14210-6; P14210-6: HGF; NbExp=3; IntAct=EBI-6280319, EBI-6280319;
CC P14210-6; P08581: MET; NbExp=3; IntAct=EBI-6280319, EBI-1039152;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P14210-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P14210-2; Sequence=VSP_009622, VSP_009623;
CC Name=3;
CC IsoId=P14210-3; Sequence=VSP_009617;
CC Name=4; Synonyms=HGF/NK2;
CC IsoId=P14210-4; Sequence=VSP_009620, VSP_009621;
CC Name=5;
CC IsoId=P14210-5; Sequence=VSP_009617, VSP_009622, VSP_009623;
CC Name=6; Synonyms=HGF/NK1;
CC IsoId=P14210-6; Sequence=VSP_009618, VSP_009619;
CC -!- DISEASE: Deafness, autosomal recessive, 39 (DFNB39) [MIM:608265]: A
CC form of profound prelingual sensorineural hearing loss. Sensorineural
CC deafness results from damage to the neural receptors of the inner ear,
CC the nerve pathways to the brain, or the area of the brain that receives
CC sound information. {ECO:0000269|PubMed:19576567}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 4]: Acts as a competitive antagonist in MET-
CC signaling. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: Has lost two of the three essential catalytic residues and so
CC probably has no enzymatic activity. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hgf/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hepatocyte growth factor entry;
CC URL="https://en.wikipedia.org/wiki/Hepatocyte_growth_factor";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HGFID385ch7q21.html";
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DR EMBL; M29145; AAA52650.1; -; mRNA.
DR EMBL; X16323; CAA34387.1; -; mRNA.
DR EMBL; M60718; AAA52648.1; -; mRNA.
DR EMBL; D90334; BAA14348.1; -; Genomic_DNA.
DR EMBL; X57574; CAA40802.1; -; mRNA.
DR EMBL; M55379; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M73239; AAA64239.1; -; mRNA.
DR EMBL; M73240; AAA64297.1; -; mRNA.
DR EMBL; M77227; AAA35980.1; -; mRNA.
DR EMBL; L02931; AAA52649.1; -; mRNA.
DR EMBL; U46010; AAC50539.1; -; mRNA.
DR EMBL; AY246560; AAO61091.1; -; Genomic_DNA.
DR EMBL; AC004960; AAC71655.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24189.1; -; Genomic_DNA.
DR EMBL; BC022308; AAH22308.1; -; mRNA.
DR EMBL; BC063485; AAH63485.1; -; mRNA.
DR EMBL; BC105797; AAI05798.1; -; mRNA.
DR EMBL; BC130284; AAI30285.1; -; mRNA.
DR EMBL; BC130286; AAI30287.1; -; mRNA.
DR EMBL; M75971; AAG53459.1; -; Genomic_DNA.
DR EMBL; M75967; AAG53459.1; JOINED; Genomic_DNA.
DR EMBL; M75966; AAG53459.1; JOINED; Genomic_DNA.
DR EMBL; M75968; AAG53459.1; JOINED; Genomic_DNA.
DR EMBL; M75969; AAG53459.1; JOINED; Genomic_DNA.
DR EMBL; M75983; AAG53460.1; -; Genomic_DNA.
DR EMBL; M75972; AAG53460.1; JOINED; Genomic_DNA.
DR EMBL; M75973; AAG53460.1; JOINED; Genomic_DNA.
DR EMBL; M75974; AAG53460.1; JOINED; Genomic_DNA.
DR EMBL; M75975; AAG53460.1; JOINED; Genomic_DNA.
DR EMBL; M75976; AAG53460.1; JOINED; Genomic_DNA.
DR EMBL; M75977; AAG53460.1; JOINED; Genomic_DNA.
DR EMBL; M75978; AAG53460.1; JOINED; Genomic_DNA.
DR EMBL; M75979; AAG53460.1; JOINED; Genomic_DNA.
DR EMBL; M75980; AAG53460.1; JOINED; Genomic_DNA.
DR EMBL; M75981; AAG53460.1; JOINED; Genomic_DNA.
DR EMBL; M75982; AAG53460.1; JOINED; Genomic_DNA.
DR CCDS; CCDS47626.1; -. [P14210-3]
DR CCDS; CCDS47627.1; -. [P14210-2]
DR CCDS; CCDS47628.1; -. [P14210-5]
DR CCDS; CCDS47629.1; -. [P14210-6]
DR CCDS; CCDS5597.1; -. [P14210-1]
DR PIR; JH0579; JH0579.
DR RefSeq; NP_000592.3; NM_000601.5. [P14210-1]
DR RefSeq; NP_001010931.1; NM_001010931.2. [P14210-2]
DR RefSeq; NP_001010932.1; NM_001010932.2. [P14210-3]
DR RefSeq; NP_001010933.1; NM_001010933.2. [P14210-5]
DR RefSeq; NP_001010934.1; NM_001010934.2. [P14210-6]
DR RefSeq; XP_006716019.1; XM_006715956.2. [P14210-1]
DR RefSeq; XP_011514417.1; XM_011516115.2. [P14210-3]
DR RefSeq; XP_016867586.1; XM_017012097.1. [P14210-2]
DR RefSeq; XP_016867587.1; XM_017012098.1. [P14210-5]
DR PDB; 1BHT; X-ray; 2.00 A; A/B=35-210.
DR PDB; 1GMN; X-ray; 2.30 A; A/B=28-210.
DR PDB; 1GMO; X-ray; 3.00 A; A/B/C/D/E/F/G/H=28-210.
DR PDB; 1GP9; X-ray; 2.50 A; A/B/C/D=40-210.
DR PDB; 1NK1; X-ray; 2.50 A; A/B=28-210.
DR PDB; 1SHY; X-ray; 3.22 A; A=495-728.
DR PDB; 1SI5; X-ray; 2.53 A; H=495-728.
DR PDB; 2HGF; NMR; -; A=31-127.
DR PDB; 2QJ2; X-ray; 1.81 A; A/B=28-209.
DR PDB; 3HMS; X-ray; 1.70 A; A=28-126.
DR PDB; 3HMT; X-ray; 2.00 A; A/B=28-126.
DR PDB; 3HN4; X-ray; 2.60 A; A=28-289.
DR PDB; 3MKP; X-ray; 2.81 A; A/B/C/D=28-210.
DR PDB; 3SP8; X-ray; 1.86 A; A/B=28-288.
DR PDB; 4D3C; X-ray; 2.62 A; A=32-210.
DR PDB; 4K3J; X-ray; 2.80 A; A=495-721.
DR PDB; 4O3T; X-ray; 2.99 A; A=495-728.
DR PDB; 4O3U; X-ray; 3.04 A; A=495-728.
DR PDB; 5COE; X-ray; 2.18 A; A/B=28-210.
DR PDB; 5CP9; X-ray; 1.90 A; A/B=28-210.
DR PDB; 5CS1; X-ray; 2.00 A; A/B=28-210.
DR PDB; 5CS3; X-ray; 2.50 A; A/B=28-210.
DR PDB; 5CS5; X-ray; 1.90 A; A/B=28-210.
DR PDB; 5CS9; X-ray; 2.00 A; A/B=28-210.
DR PDB; 5CSQ; X-ray; 1.95 A; A/B=28-210.
DR PDB; 5CT1; X-ray; 2.00 A; A/B=28-210.
DR PDB; 5CT2; X-ray; 2.00 A; A/B=28-210.
DR PDB; 5CT3; X-ray; 2.00 A; A/B=28-210.
DR PDB; 7MO7; EM; 4.80 A; A/D=1-728.
DR PDB; 7MO8; EM; 4.50 A; A=1-728.
DR PDB; 7MO9; EM; 4.00 A; A/D=1-728.
DR PDB; 7MOA; EM; 4.90 A; A/D=1-728.
DR PDB; 7MOB; EM; 5.00 A; A/B=1-210.
DR PDB; 7OCL; X-ray; 1.80 A; A/B=125-290.
DR PDB; 7OCM; X-ray; 1.70 A; A=125-290.
DR PDBsum; 1BHT; -.
DR PDBsum; 1GMN; -.
DR PDBsum; 1GMO; -.
DR PDBsum; 1GP9; -.
DR PDBsum; 1NK1; -.
DR PDBsum; 1SHY; -.
DR PDBsum; 1SI5; -.
DR PDBsum; 2HGF; -.
DR PDBsum; 2QJ2; -.
DR PDBsum; 3HMS; -.
DR PDBsum; 3HMT; -.
DR PDBsum; 3HN4; -.
DR PDBsum; 3MKP; -.
DR PDBsum; 3SP8; -.
DR PDBsum; 4D3C; -.
DR PDBsum; 4K3J; -.
DR PDBsum; 4O3T; -.
DR PDBsum; 4O3U; -.
DR PDBsum; 5COE; -.
DR PDBsum; 5CP9; -.
DR PDBsum; 5CS1; -.
DR PDBsum; 5CS3; -.
DR PDBsum; 5CS5; -.
DR PDBsum; 5CS9; -.
DR PDBsum; 5CSQ; -.
DR PDBsum; 5CT1; -.
DR PDBsum; 5CT2; -.
DR PDBsum; 5CT3; -.
DR PDBsum; 7MO7; -.
DR PDBsum; 7MO8; -.
DR PDBsum; 7MO9; -.
DR PDBsum; 7MOA; -.
DR PDBsum; 7MOB; -.
DR PDBsum; 7OCL; -.
DR PDBsum; 7OCM; -.
DR AlphaFoldDB; P14210; -.
DR SASBDB; P14210; -.
DR SMR; P14210; -.
DR BioGRID; 109330; 40.
DR CORUM; P14210; -.
DR DIP; DIP-37535N; -.
DR IntAct; P14210; 9.
DR MINT; P14210; -.
DR STRING; 9606.ENSP00000222390; -.
DR BindingDB; P14210; -.
DR ChEMBL; CHEMBL5479; -.
DR DrugBank; DB05434; ABT-510.
DR DrugBank; DB12307; Foretinib.
DR DrugBank; DB01109; Heparin.
DR DrugBank; DB03959; N,O6-Disulfo-Glucosamine.
DR DrugBank; DB02264; O2-Sulfo-Glucuronic Acid.
DR MEROPS; S01.976; -.
DR GlyConnect; 219; 8 N-Linked glycans (4 sites), 1 O-Linked glycan (1 site).
DR GlyGen; P14210; 5 sites, 14 N-linked glycans (4 sites), 2 O-linked glycans (1 site).
DR iPTMnet; P14210; -.
DR PhosphoSitePlus; P14210; -.
DR BioMuta; HGF; -.
DR DMDM; 123116; -.
DR EPD; P14210; -.
DR MassIVE; P14210; -.
DR MaxQB; P14210; -.
DR PaxDb; P14210; -.
DR PeptideAtlas; P14210; -.
DR PRIDE; P14210; -.
DR ProteomicsDB; 53034; -. [P14210-1]
DR ProteomicsDB; 53035; -. [P14210-2]
DR ProteomicsDB; 53036; -. [P14210-3]
DR ProteomicsDB; 53037; -. [P14210-4]
DR ProteomicsDB; 53038; -. [P14210-5]
DR ProteomicsDB; 53039; -. [P14210-6]
DR ABCD; P14210; 13 sequenced antibodies.
DR Antibodypedia; 4150; 1068 antibodies from 43 providers.
DR DNASU; 3082; -.
DR Ensembl; ENST00000222390.11; ENSP00000222390.5; ENSG00000019991.18. [P14210-1]
DR Ensembl; ENST00000423064.7; ENSP00000413829.2; ENSG00000019991.18. [P14210-6]
DR Ensembl; ENST00000444829.7; ENSP00000389854.2; ENSG00000019991.18. [P14210-2]
DR Ensembl; ENST00000453411.6; ENSP00000408270.1; ENSG00000019991.18. [P14210-5]
DR Ensembl; ENST00000457544.7; ENSP00000391238.2; ENSG00000019991.18. [P14210-3]
DR GeneID; 3082; -.
DR KEGG; hsa:3082; -.
DR MANE-Select; ENST00000222390.11; ENSP00000222390.5; NM_000601.6; NP_000592.3.
DR UCSC; uc003uhl.4; human. [P14210-1]
DR CTD; 3082; -.
DR DisGeNET; 3082; -.
DR GeneCards; HGF; -.
DR GeneReviews; HGF; -.
DR HGNC; HGNC:4893; HGF.
DR HPA; ENSG00000019991; Tissue enriched (placenta).
DR MalaCards; HGF; -.
DR MIM; 142409; gene.
DR MIM; 608265; phenotype.
DR neXtProt; NX_P14210; -.
DR OpenTargets; ENSG00000019991; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA29269; -.
DR VEuPathDB; HostDB:ENSG00000019991; -.
DR eggNOG; ENOG502QR40; Eukaryota.
DR GeneTree; ENSGT00940000156019; -.
DR HOGENOM; CLU_017565_1_0_1; -.
DR InParanoid; P14210; -.
DR OMA; CNIKVCE; -.
DR OrthoDB; 164039at2759; -.
DR PhylomeDB; P14210; -.
DR TreeFam; TF329901; -.
DR PathwayCommons; P14210; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-1266695; Interleukin-7 signaling.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-6806942; MET Receptor Activation.
DR Reactome; R-HSA-6807004; Negative regulation of MET activity.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8851805; MET activates RAS signaling.
DR Reactome; R-HSA-8851907; MET activates PI3K/AKT signaling.
DR Reactome; R-HSA-8865999; MET activates PTPN11.
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR Reactome; R-HSA-8875513; MET interacts with TNS proteins.
DR Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-HSA-8875656; MET receptor recycling.
DR Reactome; R-HSA-8875791; MET activates STAT3.
DR Reactome; R-HSA-9734091; Drug-mediated inhibition of MET activation.
DR SignaLink; P14210; -.
DR SIGNOR; P14210; -.
DR BioGRID-ORCS; 3082; 40 hits in 1079 CRISPR screens.
DR ChiTaRS; HGF; human.
DR EvolutionaryTrace; P14210; -.
DR GeneWiki; Hepatocyte_growth_factor; -.
DR GenomeRNAi; 3082; -.
DR Pharos; P14210; Tchem.
DR PRO; PR:P14210; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P14210; protein.
DR Bgee; ENSG00000019991; Expressed in placenta and 150 other tissues.
DR ExpressionAtlas; P14210; baseline and differential.
DR Genevisible; P14210; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0042056; F:chemoattractant activity; IDA:BHF-UCL.
DR GO; GO:0008083; F:growth factor activity; NAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0060326; P:cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; TAS:HGNC-UCL.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; NAS:UniProtKB.
DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; IDA:BHF-UCL.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
DR GO; GO:0070572; P:positive regulation of neuron projection regeneration; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; NAS:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:BHF-UCL.
DR GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; IDA:MGI.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; IEA:Ensembl.
DR GO; GO:1902947; P:regulation of tau-protein kinase activity; IEA:Ensembl.
DR GO; GO:0014856; P:skeletal muscle cell proliferation; 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; IPR027284; Hepatocyte_GF.
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; 4.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF500183; Hepatocyte_GF; 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; 4.
DR PROSITE; PS50070; KRINGLE_2; 4.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Deafness; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor; Kringle;
KW Non-syndromic deafness; Pyrrolidone carboxylic acid; Reference proteome;
KW Repeat; Serine protease homolog; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:1826837"
FT CHAIN 32..494
FT /note="Hepatocyte growth factor alpha chain"
FT /id="PRO_0000028091"
FT CHAIN 495..728
FT /note="Hepatocyte growth factor beta chain"
FT /id="PRO_0000028092"
FT DOMAIN 37..123
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 128..206
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 211..288
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 305..383
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 391..469
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 495..721
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOD_RES 32
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1826837"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /id="CAR_000021"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /id="CAR_000022"
FT CARBOHYD 476
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1482348"
FT /id="CAR_000023"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /id="CAR_000024"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /id="CAR_000025"
FT DISULFID 70..96
FT DISULFID 74..84
FT DISULFID 128..206
FT DISULFID 149..189
FT DISULFID 177..201
FT DISULFID 211..288
FT /evidence="ECO:0000250"
FT DISULFID 232..271
FT /evidence="ECO:0000250"
FT DISULFID 260..283
FT /evidence="ECO:0000250"
FT DISULFID 305..383
FT /evidence="ECO:0000250"
FT DISULFID 326..365
FT /evidence="ECO:0000250"
FT DISULFID 354..377
FT /evidence="ECO:0000250"
FT DISULFID 391..469
FT /evidence="ECO:0000250"
FT DISULFID 412..452
FT /evidence="ECO:0000250"
FT DISULFID 440..464
FT /evidence="ECO:0000250"
FT DISULFID 487..604
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 519..535
FT /evidence="ECO:0000250"
FT DISULFID 612..679
FT /evidence="ECO:0000250"
FT DISULFID 642..658
FT /evidence="ECO:0000250"
FT DISULFID 669..697
FT /evidence="ECO:0000250"
FT VAR_SEQ 161..165
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1824873"
FT /id="VSP_009617"
FT VAR_SEQ 209..210
FT /note="VE -> GK (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8662798"
FT /id="VSP_009618"
FT VAR_SEQ 211..728
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8662798"
FT /id="VSP_009619"
FT VAR_SEQ 287..296
FT /note="TCADNTMNDT -> NMRDITWALN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1720571"
FT /id="VSP_009620"
FT VAR_SEQ 289..290
FT /note="AD -> ET (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:1280830,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1826653"
FT /id="VSP_009622"
FT VAR_SEQ 291..728
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:1280830,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1826653"
FT /id="VSP_009623"
FT VAR_SEQ 297..728
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1720571"
FT /id="VSP_009621"
FT VARIANT 304
FT /note="E -> K (in dbSNP:rs5745687)"
FT /evidence="ECO:0000269|Ref.11"
FT /id="VAR_019199"
FT VARIANT 330
FT /note="D -> Y (in dbSNP:rs5745688)"
FT /evidence="ECO:0000269|Ref.11"
FT /id="VAR_019200"
FT MUTAGEN 494
FT /note="R->Q: Loss of activity due to absence of proteolytic
FT cleavage."
FT /evidence="ECO:0000269|PubMed:1280830"
FT CONFLICT 32..33
FT /note="QR -> HK (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="K -> N (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="P -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="M -> V (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="L -> M (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="V -> A (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="E -> K (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="H -> N (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="D -> N (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="I -> V (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="V -> I (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="D -> E (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="C -> R (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="D -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="S -> N (in Ref. 2; CAA34387)"
FT /evidence="ECO:0000305"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3HMS"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:3HMS"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1NK1"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3HMS"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:3HMS"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5CP9"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3SP8"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:3HMS"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:3HMS"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:3HMS"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1GP9"
FT STRAND 108..121
FT /evidence="ECO:0007829|PDB:3HMS"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3HMS"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:7OCM"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5CSQ"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:7OCL"
FT TURN 164..169
FT /evidence="ECO:0007829|PDB:7OCM"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:7OCM"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:7OCM"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:3SP8"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3SP8"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3SP8"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:7OCM"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:3HN4"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:7OCM"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:7OCM"
FT STRAND 508..525
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:1SI5"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:1SI5"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 544..549
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:1SI5"
FT TURN 557..561
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 563..572
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 579..586
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 611..618
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 630..637
FT /evidence="ECO:0007829|PDB:1SI5"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:1SI5"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:4K3J"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:1SI5"
FT TURN 670..674
FT /evidence="ECO:0007829|PDB:4O3U"
FT STRAND 676..680
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 682..691
FT /evidence="ECO:0007829|PDB:1SI5"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:4O3T"
FT STRAND 704..708
FT /evidence="ECO:0007829|PDB:1SI5"
FT HELIX 709..712
FT /evidence="ECO:0007829|PDB:1SI5"
FT HELIX 713..720
FT /evidence="ECO:0007829|PDB:1SI5"
SQ SEQUENCE 728 AA; 83134 MW; 2D997938295ADD2F CRC64;
MWVTKLLPAL LLQHVLLHLL LLPIAIPYAE GQRKRRNTIH EFKKSAKTTL IKIDPALKIK
TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE
NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SFLPSSYRGK DLQENYCRNP
RGEEGGPWCF TSNPEVRYEV CDIPQCSEVE CMTCNGESYR GLMDHTESGK ICQRWDHQTP
HRHKFLPERY PDKGFDDNYC RNPDGQPRPW CYTLDPHTRW EYCAIKTCAD NTMNDTDVPL
ETTECIQGQG EGYRGTVNTI WNGIPCQRWD SQYPHEHDMT PENFKCKDLR ENYCRNPDGS
ESPWCFTTDP NIRVGYCSQI PNCDMSHGQD CYRGNGKNYM GNLSQTRSGL TCSMWDKNME
DLHRHIFWEP DASKLNENYC RNPDDDAHGP WCYTGNPLIP WDYCPISRCE GDTTPTIVNL
DHPVISCAKT KQLRVVNGIP TRTNIGWMVS LRYRNKHICG GSLIKESWVL TARQCFPSRD
LKDYEAWLGI HDVHGRGDEK CKQVLNVSQL VYGPEGSDLV LMKLARPAVL DDFVSTIDLP
NYGCTIPEKT SCSVYGWGYT GLINYDGLLR VAHLYIMGNE KCSQHHRGKV TLNESEICAG
AEKIGSGPCE GDYGGPLVCE QHKMRMVLGV IVPGRGCAIP NRPGIFVRVA YYAKWIHKII
LTYKVPQS
