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UniProtKB/Swiss-Prot entry O15520


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FGF10_HUMAN
Primary accession number O15520
Secondary accession numbers Q6FHT6 Q96P59
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    June 10, 2008 (Entry version 80)
Name and origin of the protein
Protein name Fibroblast growth factor 10 [Precursor]
Synonyms FGF-10
Keratinocyte growth factor 2
Gene name
Name: FGF10
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
DOI=10.1074/jbc.272.37.23191; PubMed=9287324 [NCBI, ExPASy, EBI, Israel, Japan]
Emoto H., Tagashira S., Mattei M.-G., Yamasaki M., Hashimoto G., Katsumata T., Negoro T., Nakatsuka M., Birnbaum D., Coulier F., Itoh N.;
"Structure and expression of human fibroblast growth factor-10.";
J. Biol. Chem. 272:23191-23194(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
Jimenez P.A., Gruber J.R., Liu B., Feng P., Florence C., Blunt A., Huddleston K.A., Teliska M., Alfonso P., Coleman T.A., Ornitz D.M., Dillon P.A., Duan R.D.;
"Cutaneous wound healing by keratinocyte growth factor 2.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Zhang Y., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.;
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH FGFBP1.
DOI=10.1038/sj.onc.1208560; PubMed=15806171 [NCBI, ExPASy, EBI, Israel, Japan]
Beer H.-D., Bittner M., Niklaus G., Munding C., Max N., Goppelt A., Werner S.;
"The fibroblast growth factor binding protein is a novel interaction partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity: implications for epithelial repair.";
Oncogene 24:5269-5277(2005).
[8]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 69-208 IN COMPLEX WITH FGFR2.
DOI=10.1073/pnas.0436500100; PubMed=12591959 [NCBI, ExPASy, EBI, Israel, Japan]
Yeh B.K., Igarashi M., Eliseenkova A.V., Plotnikov A.N., Sher I., Ron D., Aaronson S.A., Mohammadi M.;
"Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors.";
Proc. Natl. Acad. Sci. U.S.A. 100:2266-2271(2003).
[9]
INVOLVEMENT IN ALSG.
DOI=10.1038/ng1507; PubMed=15654336 [NCBI, ExPASy, EBI, Israel, Japan]
Entesarian M., Matsson H., Klar J., Bergendal B., Olson L., Arakaki R., Hayashi Y., Ohuchi H., Falahat B., Bolstad A.I., Jonsson R., Wahren-Herlenius M., Dahl N.;
"Mutations in the gene encoding fibroblast growth factor 10 are associated with aplasia of lacrimal and salivary glands.";
Nat. Genet. 37:125-127(2005).
[10]
VARIANT LADDS ARG-156.
DOI=10.1111/j.1399-0004.2006.00597.x; PubMed=16630169 [NCBI, ExPASy, EBI, Israel, Japan]
Milunsky J.M., Zhao G., Maher T.A., Colby R., Everman D.B.;
"LADD syndrome is caused by FGF10 mutations.";
Clin. Genet. 69:349-354(2006).
[11]
VARIANT LADDS PHE-106.
DOI=10.1038/ng1757; PubMed=16501574 [NCBI, ExPASy, EBI, Israel, Japan]
Rohmann E., Brunner H.G., Kayserili H., Uyguner O., Nuernberg G., Lew E.D., Dobbie A., Eswarakumar V.P., Uzumcu A., Ulubil-Emeroglu M., Leroy J.G., Li Y., Becker C., Lehnerdt K., Cremers C.W.R.J., Yueksel-Apak M., Nuernberg P., Kubisch C., Schlessinger J., van Bokhoven H., Wollnik B.;
"Mutations in different components of FGF signaling in LADD syndrome.";
Nat. Genet. 38:414-417(2006).
Comments
  • FUNCTION: Could be a growth factor active in the process of wound healing. Acts as a mitogen in the lung. May act in a manner similar to FGF-7.
  • SUBUNIT: Interacts with FGFBP1.
  • INTERACTION:
    P21802:FGFR2; NbExp=1; IntAct=EBI-1035684, EBI-1028658;
  • SUBCELLULAR LOCATION: Secreted (Potential).
  • DISEASE: Defects in FGF10 are the cause of autosomal dominant aplasia of lacrimal and salivary glands (ALSG) [MIM:180920]. ALSG has variable expressivity, and affected individuals may have aplasia or hypoplasia of the lacrimal, parotid, submandibular and sublingual glands and absence of the lacrimal puncta. The disorder is characterized by irritable eyes, recurrent eye infections, epiphora (constant tearing) and xerostomia (dryness of the mouth), which increases the risk of dental erosion, dental caries, periodontal disease and oral infections.
  • DISEASE: Defects in FGF10 are a cause of lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:149730]; also known as Levy-Hollister syndrome. LADDS is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. LADDS is an autosomal dominant syndrome characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.
  • SIMILARITY: Belongs to the heparin-binding growth factors family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB002097; BAA22331.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U67918; AAB61991.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF411527; AAL05875.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541665; CAG46466.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY604046; AAS99733.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069561; AAH69561.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105021; AAI05022.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105023; AAI05024.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_004456.1; -.
UniGene Hs.664499
3D structure databases
PDB
1NUN; X-ray; 2.90 A; A=64-208.[ExPASy / RCSB / EBI]
PDBsum 1NUN; -.
ModBase O15520.
Protein-protein interaction databases
DIP DIP:6037N; -.
IntAct O15520; -.
PTM databases
PhosphoSite O15520; -.
Enzyme and pathway databases
Reactome REACT_9470; Signaling by FGFR.
Polymorphism databases
NIEHS-SNPs FGF10.
Organism-specific databases
H-InvDB HIX0031935; -.
HGNC HGNC:3666; FGF10.
GeneLynx FGF10; Homo sapiens.
GenAtlas FGF10.
HPA CAB010315; -.
MIM 149730; phenotype. [NCBI / EBI]
180920; phenotype. [NCBI / EBI]
602115; gene. [NCBI / EBI]
Orphanet 86815; Aplasia of lacrimal and salivary glands.
2363; Lacrimo-auriculo-dento-digital syndrome.
PharmGKB PA28106; -.
GeneCards O15520.
Gene expression databases
ArrayExpress O15520; -.
CleanEx HS_FGF10; -.
GermOnline ENSG00000070193; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (non-traceable author statement from UniProtKB).
GO:0005615; Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0005104; Molecular function: fibroblast growth factor receptor binding (inferred from direct assay from UniProtKB).
GO:0008083; Molecular function: growth factor activity (inferred from direct assay from UniProtKB).
GO:0008201; Molecular function: heparin binding (inferred from direct assay from UniProtKB).
GO:0008543; Biological process: fibroblast growth factor receptor signaling pathway (non-traceable author statement from UniProtKB).
GO:0009887; Biological process: organ morphogenesis (traceable author statement from ProtInc).
GO:0048260; Biological process: positive regulation of receptor-mediated endocytosis (non-traceable author statement from UniProtKB).
GO:0050677; Biological process: positive regulation of urothelial cell proliferation (inferred from direct assay from UniProtKB).
GO:0000060; Biological process: protein import into nucleus, translocation (non-traceable author statement from UniProtKB).
GO:0045449; Biological process: regulation of transcription (non-traceable author statement from UniProtKB).
GO:0006950; Biological process: response to stress (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002209; GF_heparin_bd.
IPR002348; IL1_HBGF.
Graphical view of domain structure.
PANTHER PTHR11486; IL1_HBGF; 1.
Pfam PF00167; FGF; 1.
Pfam graphical view of domain structure.
PRINTS PR00263; HBGFFGF.
PR00262; IL1HBGF.
ProDom PD000831; IL1_HBGF; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00442; FGF; 1.
SMART graphical view of domain structure.
PROSITE PS00247; HBGF_FGF; 1.
BLOCKS O15520.
Genome annotation databases
Ensembl ENSG00000070193; Homo sapiens. [Contig view]
GeneID 2255; -.
KEGG hsa:2255; -.
Phylogenomic databases
HOGENOM O15520; -.
HOVERGEN O15520; -.
Other
SOURCE FGF10; Homo sapiens.
ProtoNet O15520.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Disease mutation; Ectodermal dysplasia; Glycoprotein; Growth factor; Lacrimo-auriculo-dento-digital syndrome; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    37  37     Potential. 
CHAIN   38   208  171     Fibroblast growth factor 10. PRO_0000008981
COMPBIAS   52    62  11     Poly-Ser. 
CARBOHYD   51    51        N-linked (GlcNAc...) (Potential). 
CARBOHYD   196   196        N-linked (GlcNAc...) (Potential). 
VARIANT   106   106  1     C -> F (in LADDS). VAR_029888 
VARIANT   156   156  1     I -> R (in LADDS). VAR_029889 
CONFLICT   120   120        V -> A (in Ref. 3; AAL05875). 
CONFLICT   134   134        M -> R (in Ref. 3; AAL05875). 
HELIX   70    73  4      
STRAND   76    84  9      
STRAND   89    92  4      
STRAND   98   101  4      
STRAND   111   117  7      
STRAND   120   125  6      
TURN   126   129  4      
STRAND   130   134  5      
STRAND   138   145  8      
STRAND   150   156  7      
STRAND   162   171  10      
STRAND   174   177  4      
HELIX   189   191  3      
HELIX   197   199  3      
STRAND   201   205  5      
Sequence information
Length: 208 AA [This is the length of the unprocessed precursor] Molecular weight: 23436 Da [This is the MW of the unprocessed precursor] CRC64: C0A0705C108680B3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWKWILTHCA SAFPHLPGCC CCCFLLLFLV SSVPVTCQAL GQDMVSPEAT NSSSSSFSSP 

        70         80         90        100        110        120 
SSAGRHVRSY NHLQGDVRWR KLFSFTKYFL KIEKNGKVSG TKKENCPYSI LEITSVEIGV 

       130        140        150        160        170        180 
VAVKAINSNY YLAMNKKGKL YGSKEFNNDC KLKERIEENG YNTYASFNWQ HNGRQMYVAL 

       190        200 
NGKGAPRRGQ KTRRKNTSAH FLPMVVHS 

O15520 in FASTA format

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