ID   FGF5_HUMAN              Reviewed;         268 AA.
AC   P12034; B2R554; O75846; Q3Y8M3;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 4.
DT   25-JAN-2012, entry version 113.
DE   RecName: Full=Fibroblast growth factor 5;
DE            Short=FGF-5;
DE   AltName: Full=Heparin-binding growth factor 5;
DE            Short=HBGF-5;
DE   AltName: Full=Smag-82;
DE   Flags: Precursor;
GN   Name=FGF5;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC   TISSUE=Brain stem;
RX   MEDLINE=91045929; PubMed=1700424; DOI=10.1073/pnas.87.20.8022;
RA   Haub O., Drucker B., Goldfarb M.;
RT   "Expression of the murine fibroblast growth factor 5 gene in the adult
RT   central nervous system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8022-8026(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89096942; PubMed=3211147;
RA   Zhan X., Bates B., Hu X., Goldfarb M.;
RT   "The human FGF-5 oncogene encodes a novel protein related to
RT   fibroblast growth factors.";
RL   Mol. Cell. Biol. 8:3487-3495(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RA   Ozawa K., Suzuki S., Asada M., Tomooka Y., Li A., Yoneda A., Komi A.,
RA   Imamura T.;
RT   "An alternatively-spliced FGF-5 mRNA is abundant in brain and
RT   translates into a partial agonist/antagonist for FGF-5 neurotrophic
RT   activity.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC   TISSUE=Umbilical artery;
RX   MEDLINE=20379035; PubMed=10823842; DOI=10.1074/jbc.M910099199;
RA   de Vries C.J.M., van Achterberg T.A.E., Horrevoets A.J.G.,
RA   ten Cate J.W., Pannekoek H.;
RT   "Differential display identification of 40 genes with altered
RT   expression in activated human smooth muscle cells. Local expression in
RT   atherosclerotic lesions of smags, smooth muscle activation-specific
RT   genes.";
RL   J. Biol. Chem. 275:23939-23947(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-54.
RG   NIEHS SNPs program;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC   TISSUE=Cerebellum;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [8]
RP   INTERACTION WITH FGFR1 AND 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.,
RA   Coulier F., Gao G., Goldfarb M.;
RT   "Receptor specificity of the fibroblast growth factor family.";
RL   J. Biol. Chem. 271:15292-15297(1996).
RN   [9]
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 cell
CC       proliferation and cell differentiation. Required for normal
CC       regulation of the hair growth cycle. Functions as an inhibitor of
CC       hair elongation by promoting progression from anagen, the growth
CC       phase of the hair follicle, into catagen the apoptosis-induced
CC       regression phase (By similarity).
CC   -!- SUBUNIT: Interacts with FGFR1 and FGFR2. Affinity between
CC       fibroblast growth factors (FGFs) and their receptors is increased
CC       by heparan sulfate glycosaminoglycans that function as
CC       coreceptors.
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P12034-1; Sequence=Displayed;
CC       Name=Short; Synonyms=FGF-5S;
CC         IsoId=P12034-2; Sequence=VSP_001518, VSP_001519;
CC         Note=Seems to have an antagonistic effect compared to that of
CC         the isoform Long;
CC   -!- TISSUE SPECIFICITY: Expressed in neonatal brain.
CC   -!- DEVELOPMENTAL STAGE: Can transform NIH 3T3 cells.
CC   -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB60698.1; Type=Erroneous gene model prediction;
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/fgf5/";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M37825; AAB06463.1; -; mRNA.
DR   EMBL; M23536; AAB60699.1; -; Genomic_DNA.
DR   EMBL; M23534; AAB60699.1; JOINED; Genomic_DNA.
DR   EMBL; M23535; AAB60699.1; JOINED; Genomic_DNA.
DR   EMBL; M23534; AAB60698.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB016517; BAA33738.1; -; mRNA.
DR   EMBL; AF171928; AAF89742.1; -; mRNA.
DR   EMBL; DQ151636; AAZ67914.1; -; Genomic_DNA.
DR   EMBL; AK312065; BAG35001.1; -; mRNA.
DR   EMBL; CH471057; EAX05860.1; -; Genomic_DNA.
DR   IPI; IPI00295390; -.
DR   IPI; IPI01022135; -.
DR   PIR; A31194; TVHUF5.
DR   PIR; B31194; B31194.
DR   RefSeq; NP_004455.2; NM_004464.3.
DR   RefSeq; NP_149134.1; NM_033143.2.
DR   UniGene; Hs.37055; -.
DR   ProteinModelPortal; P12034; -.
DR   SMR; P12034; 84-219.
DR   DIP; DIP-4018N; -.
DR   STRING; P12034; -.
DR   DMDM; 85700417; -.
DR   PRIDE; P12034; -.
DR   Ensembl; ENST00000312465; ENSP00000311697; ENSG00000138675.
DR   GeneID; 2250; -.
DR   KEGG; hsa:2250; -.
DR   UCSC; uc003hmd.1; human.
DR   UCSC; uc003hme.1; human.
DR   CTD; 2250; -.
DR   GeneCards; GC04P081187; -.
DR   H-InvDB; HIX0004330; -.
DR   HGNC; HGNC:3683; FGF5.
DR   HPA; CAB010313; -.
DR   MIM; 165190; gene.
DR   neXtProt; NX_P12034; -.
DR   PharmGKB; PA28122; -.
DR   eggNOG; prNOG13725; -.
DR   HOGENOM; HBG715603; -.
DR   HOVERGEN; HBG007580; -.
DR   InParanoid; P12034; -.
DR   OMA; SHEANML; -.
DR   OrthoDB; EOG4HT8T7; -.
DR   PhylomeDB; P12034; -.
DR   Reactome; REACT_111102; Signal Transduction.
DR   NextBio; 9107; -.
DR   ArrayExpress; P12034; -.
DR   Bgee; P12034; -.
DR   CleanEx; HS_FGF5; -.
DR   Genevestigator; P12034; -.
DR   GermOnline; ENSG00000138675; Homo sapiens.
DR   GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR   GO; GO:0005104; F:fibroblast growth factor receptor binding; IDA:MGI.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
DR   GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
DR   InterPro; IPR008996; Cytokine_IL1-like.
DR   InterPro; IPR002209; GF_heparin-bd.
DR   InterPro; IPR002348; IL1_HBGF.
DR   KO; K04358; -.
DR   PANTHER; PTHR11486; IL1_HBGF; 1.
DR   Pfam; PF00167; FGF; 1.
DR   PRINTS; PR00263; HBGFFGF.
DR   PRINTS; PR00262; IL1HBGF.
DR   SMART; SM00442; FGF; 1.
DR   SUPFAM; SSF50353; Cytok_IL1_like; 1.
DR   PROSITE; PS00247; HBGF_FGF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Glycoprotein; Growth factor;
KW   Mitogen; Polymorphism; Proto-oncogene; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL        1     17       Potential.
FT   CHAIN        18    268       Fibroblast growth factor 5.
FT                                /FTId=PRO_0000008958.
FT   COMPBIAS     49     52       Poly-Ser.
FT   COMPBIAS     55     62       Poly-Ser.
FT   CARBOHYD    110    110       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     120    123       VLEI -> QVHR (in isoform Short).
FT                                /FTId=VSP_001518.
FT   VAR_SEQ     124    268       Missing (in isoform Short).
FT                                /FTId=VSP_001519.
FT   VARIANT      54     54       M -> V (in dbSNP:rs33950145).
FT                                /FTId=VAR_025174.
FT   CONFLICT     42     42       R -> I (in Ref. 1; AAB06463).
FT   CONFLICT     83     86       PSGR -> LGA (in Ref. 2; AAB60699).
FT   CONFLICT    224    224       Q -> QQ (in Ref. 5; AAZ67914).
FT   CONFLICT    238    238       K -> N (in Ref. 1; AAB06463 and 2;
FT                                AAB60699).
FT   CONFLICT    245    245       P -> S (in Ref. 1; AAB06463 and 2;
FT                                AAB60699).
SQ   SEQUENCE   268 AA;  29551 MW;  28B7268B26781BCF CRC64;
     MSLSFLLLLF FSHLILSAWA HGEKRLAPKG QPGPAATDRN PRGSSSRQSS SSAMSSSSAS
     SSPAASLGSQ GSGLEQSSFQ WSPSGRRTGS LYCRVGIGFH LQIYPDGKVN GSHEANMLSV
     LEIFAVSQGI VGIRGVFSNK FLAMSKKGKL HASAKFTDDC KFRERFQENS YNTYASAIHR
     TEKTGREWYV ALNKRGKAKR GCSPRVKPQH ISTHFLPRFK QSEQPELSFT VTVPEKKKPP
     SPIKPKIPLS APRKNTNSVK YRLKFRFG
//