FGF7_HUMAN
ID FGF7_HUMAN Reviewed; 194 AA.
AC P21781; H0YNY5; Q6FGV5; Q96FG5;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Fibroblast growth factor 7;
DE Short=FGF-7;
DE AltName: Full=Heparin-binding growth factor 7;
DE Short=HBGF-7;
DE AltName: Full=Keratinocyte growth factor;
DE Flags: Precursor;
GN Name=FGF7; Synonyms=KGF;
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), AND PROTEIN SEQUENCE OF 32-50.
RX PubMed=2475908; DOI=10.1126/science.2475908;
RA Finch P.W., Rubin J.S., Miki T., Ron D., Aaronson S.A.;
RT "Human KGF is FGF-related with properties of a paracrine effector of
RT epithelial cell growth.";
RL Science 245:752-755(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1664700; DOI=10.1111/j.1749-6632.1991.tb49018.x;
RA Aaronson S.A., Bottaro D.P., Miki T., Ron D., Finch P.W., Fleming T.P.,
RA Ahn J., Taylor W.G., Rubin J.S.;
RT "Keratinocyte growth factor. A fibroblast growth factor family member with
RT unusual target cell specificity.";
RL Ann. N. Y. Acad. Sci. 638:62-77(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLU-62.
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 [8]
RP PROTEIN SEQUENCE OF 32-44.
RX PubMed=2915979; DOI=10.1073/pnas.86.3.802;
RA Rubin J.S., Osada H., Finch P.W., Taylor W.G., Rudikoff S., Aaronson S.A.;
RT "Purification and characterization of a newly identified growth factor
RT specific for epithelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:802-806(1989).
RN [9]
RP INTERACTION WITH FGFR2, AND FUNCTION IN CELL PROLIFERATION.
RX PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
RA Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F.,
RA Gao G., Goldfarb M.;
RT "Receptor specificity of the fibroblast growth factor family.";
RL J. Biol. Chem. 271:15292-15297(1996).
RN [10]
RP INTERACTION WITH FGFBP1.
RX PubMed=15806171; DOI=10.1038/sj.onc.1208560;
RA Beer H.-D., Bittner M., Niklaus G., Munding C., Max N., Goppelt A.,
RA Werner S.;
RT "The fibroblast growth factor binding protein is a novel interaction
RT partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity:
RT implications for epithelial repair.";
RL Oncogene 24:5269-5277(2005).
RN [11]
RP INTERACTION WITH FGFR2, AND FUNCTION IN STIMULATION OF CELL PROLIFERATION.
RX PubMed=16597617; DOI=10.1074/jbc.m601252200;
RA Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M., Ornitz D.M.;
RT "Receptor specificity of the fibroblast growth factor family. The complete
RT mammalian FGF family.";
RL J. Biol. Chem. 281:15694-15700(2006).
RN [12]
RP REVIEW.
RX PubMed=20094046; DOI=10.1038/nrc2780;
RA Turner N., Grose R.;
RT "Fibroblast growth factor signalling: from development to cancer.";
RL Nat. Rev. Cancer 10:116-129(2010).
CC -!- FUNCTION: Plays an important role in the regulation of embryonic
CC development, cell proliferation and cell differentiation. Required for
CC normal branching morphogenesis. Growth factor active on keratinocytes.
CC Possible major paracrine effector of normal epithelial cell
CC proliferation. {ECO:0000269|PubMed:16597617,
CC ECO:0000269|PubMed:8663044}.
CC -!- SUBUNIT: Interacts with FGFBP1. Interacts with FGFR2. Affinity between
CC fibroblast growth factors (FGFs) and their receptors is increased by
CC heparan sulfate glycosaminoglycans that function as coreceptors.
CC {ECO:0000269|PubMed:15806171, ECO:0000269|PubMed:16597617,
CC ECO:0000269|PubMed:8663044}.
CC -!- INTERACTION:
CC P21781; P21802-3: FGFR2; NbExp=2; IntAct=EBI-3937699, EBI-6354683;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P21781-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P21781-2; Sequence=VSP_055090;
CC -!- TISSUE SPECIFICITY: Epithelial cell.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
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DR EMBL; M60828; AAA63210.1; -; mRNA.
DR EMBL; S81661; AAB21431.1; -; mRNA.
DR EMBL; AK313160; BAG35978.1; -; mRNA.
DR EMBL; CR542002; CAG46799.1; -; mRNA.
DR EMBL; AC022306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77375.1; -; Genomic_DNA.
DR EMBL; CH471082; EAW77376.1; -; Genomic_DNA.
DR EMBL; BC010956; AAH10956.1; -; mRNA.
DR CCDS; CCDS10131.1; -. [P21781-1]
DR PIR; A36301; A36301.
DR PIR; B46289; B46289.
DR RefSeq; NP_002000.1; NM_002009.3. [P21781-1]
DR AlphaFoldDB; P21781; -.
DR SMR; P21781; -.
DR BioGRID; 108543; 5.
DR DIP; DIP-4010N; -.
DR IntAct; P21781; 5.
DR STRING; 9606.ENSP00000267843; -.
DR BindingDB; P21781; -.
DR ChEMBL; CHEMBL3286071; -.
DR GlyGen; P21781; 1 site.
DR iPTMnet; P21781; -.
DR PhosphoSitePlus; P21781; -.
DR BioMuta; FGF7; -.
DR DMDM; 122756; -.
DR MassIVE; P21781; -.
DR PaxDb; P21781; -.
DR PeptideAtlas; P21781; -.
DR PRIDE; P21781; -.
DR ProteomicsDB; 40695; -.
DR ProteomicsDB; 53903; -. [P21781-1]
DR Antibodypedia; 12143; 402 antibodies from 35 providers.
DR DNASU; 2252; -.
DR Ensembl; ENST00000267843.9; ENSP00000267843.4; ENSG00000140285.12. [P21781-1]
DR Ensembl; ENST00000560270.1; ENSP00000454205.1; ENSG00000140285.12. [P21781-2]
DR GeneID; 2252; -.
DR KEGG; hsa:2252; -.
DR MANE-Select; ENST00000267843.9; ENSP00000267843.4; NM_002009.4; NP_002000.1.
DR UCSC; uc001zxn.3; human. [P21781-1]
DR CTD; 2252; -.
DR DisGeNET; 2252; -.
DR GeneCards; FGF7; -.
DR HGNC; HGNC:3685; FGF7.
DR HPA; ENSG00000140285; Tissue enhanced (urinary).
DR MIM; 148180; gene.
DR neXtProt; NX_P21781; -.
DR OpenTargets; ENSG00000140285; -.
DR PharmGKB; PA28124; -.
DR VEuPathDB; HostDB:ENSG00000140285; -.
DR eggNOG; KOG3885; Eukaryota.
DR GeneTree; ENSGT00940000159843; -.
DR HOGENOM; CLU_081609_3_1_1; -.
DR InParanoid; P21781; -.
DR OMA; QYYICMN; -.
DR OrthoDB; 1153514at2759; -.
DR PhylomeDB; P21781; -.
DR TreeFam; TF317805; -.
DR PathwayCommons; P21781; -.
DR Reactome; R-HSA-109704; PI3K Cascade.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-190377; FGFR2b ligand binding and activation.
DR Reactome; R-HSA-2033519; Activated point mutants of FGFR2.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-5654221; Phospholipase C-mediated cascade, FGFR2.
DR Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SignaLink; P21781; -.
DR SIGNOR; P21781; -.
DR BioGRID-ORCS; 2252; 13 hits in 1066 CRISPR screens.
DR GeneWiki; FGF7; -.
DR GenomeRNAi; 2252; -.
DR Pharos; P21781; Tbio.
DR PRO; PR:P21781; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P21781; protein.
DR Bgee; ENSG00000140285; Expressed in calcaneal tendon and 128 other tissues.
DR ExpressionAtlas; P21781; baseline and differential.
DR Genevisible; P21781; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005111; F:type 2 fibroblast growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IBA:GO_Central.
DR GO; GO:0010463; P:mesenchymal cell proliferation; IDA:UniProtKB.
DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl.
DR GO; GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IDA:UniProtKB.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IDA:UniProtKB.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; TAS:ProtInc.
DR GO; GO:0061033; P:secretion by lung epithelial cell involved in lung growth; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR CDD; cd00058; FGF; 1.
DR InterPro; IPR028247; FGF7.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; PTHR11486; 1.
DR PANTHER; PTHR11486:SF20; PTHR11486:SF20; 1.
DR Pfam; PF00167; FGF; 1.
DR PRINTS; PR00263; HBGFFGF.
DR SMART; SM00442; FGF; 1.
DR SUPFAM; SSF50353; SSF50353; 1.
DR PROSITE; PS00247; HBGF_FGF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Glycoprotein;
KW Growth factor; Heparin-binding; Mitogen; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:2475908,
FT ECO:0000269|PubMed:2915979"
FT CHAIN 32..194
FT /note="Fibroblast growth factor 7"
FT /id="PRO_0000008965"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 96..194
FT /note="NIMEIRTVAVGIVAIKGVESEFYLAMNKEGKLYAKKECNEDCNFKELILENH
FT YNTYASAKWTHNGGEMFVALNQKGIPVRGKKTKKEQKTAHFLPMAIT -> SK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055090"
FT VARIANT 59
FT /note="M -> T (in dbSNP:rs34531231)"
FT /id="VAR_049063"
FT VARIANT 62
FT /note="G -> E (in dbSNP:rs17850705)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_071038"
SQ SEQUENCE 194 AA; 22509 MW; B19192474E6049E2 CRC64;
MHKWILTWIL PTLLYRSCFH IICLVGTISL ACNDMTPEQM ATNVNCSSPE RHTRSYDYME
GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MKNNYNIMEI RTVAVGIVAI KGVESEFYLA
MNKEGKLYAK KECNEDCNFK ELILENHYNT YASAKWTHNG GEMFVALNQK GIPVRGKKTK
KEQKTAHFLP MAIT
