Fibroblast growth factor 10 precursor

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Reviewed, UniProtKB/Swiss-Prot O15520 (FGF10_HUMAN)

Last modified February 9, 2010. Version 96. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Fibroblast growth factor 10
      Short name=FGF-10
Alternative name(s):
    Keratinocyte growth factor 2

Gene names

Name:

FGF10

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	208 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (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 structure	Interacts with FGFBP1. Ref.7
Subcellular location	Secreted Potential.
Involvement in 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. Ref.9 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. Ref.10 Ref.11
Sequence similarities	Belongs to the heparin-binding growth factors family.

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Ontologies

Keywords
Cellular component	Secreted
Disease	Disease mutation Ectodermal dysplasia Lacrimo-auriculo-dento-digital syndrome
Domain	Signal
Molecular function	Growth factor
PTM	Glycoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	ERK1 and ERK2 cascade Inferred from direct assay. Source: UniProtKB actin cytoskeleton reorganization Inferred from direct assay. Source: UniProtKB activation of MAPK activity Inferred from direct assay. Source: UniProtKB branching morphogenesis of a tube Inferred from direct assay. Source: UniProtKB fibroblast growth factor receptor signaling pathway Inferred from Experiment. Source: Reactome lacrimal gland development Inferred from mutant phenotype. Source: UniProtKB lung saccule development Inferred from mutant phenotype. Source: UniProtKB mesonephros development Inferred from expression pattern. Source: UniProtKB metanephros development Inferred from expression pattern. Source: UniProtKB negative regulation of cell cycle arrest Inferred from direct assay. Source: UniProtKB positive chemotaxis Inferred from direct assay. Source: UniProtKB positive regulation of ATPase activity Inferred from direct assay. Source: UniProtKB positive regulation of DNA repair Inferred from direct assay. Source: UniProtKB positive regulation of DNA replication Inferred from mutant phenotype. Source: UniProtKB positive regulation of ERK1 and ERK2 cascade Inferred from direct assay. Source: UniProtKB positive regulation of Ras protein signal transduction Inferred from direct assay. Source: UniProtKB positive regulation of cyclin-dependent protein kinase activity during G1/S Inferred from direct assay. Source: UniProtKB positive regulation of epithelial cell proliferation involved in wound healing Non-traceable author statement. Source: UniProtKB positive regulation of hair follicle cell proliferation Inferred from direct assay. Source: UniProtKB positive regulation of keratinocyte migration Inferred from direct assay. Source: UniProtKB positive regulation of keratinocyte proliferation Inferred from direct assay. Source: UniProtKB positive regulation of lymphocyte proliferation Inferred from direct assay. Source: UniProtKB positive regulation of peptidyl-tyrosine phosphorylation Inferred from direct assay. Source: UniProtKB positive regulation of urothelial cell proliferation Inferred from direct assay. Source: UniProtKB protein localization at cell surface Inferred from direct assay. Source: UniProtKB radial glial cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB regulation of saliva secretion Inferred from mutant phenotype. Source: UniProtKB salivary gland development Inferred from mutant phenotype. Source: UniProtKB tear secretion Inferred from mutant phenotype. Source: UniProtKB thymus development Inferred from direct assay. Source: UniProtKB urothelial cell proliferation Inferred from direct assay. Source: UniProtKB
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB extracellular space Inferred from direct assay. Source: UniProtKB nucleus Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from direct assay. Source: UniProtKB
Molecular function	chemoattractant activity Inferred from direct assay. Source: UniProtKB growth factor activity Inferred from direct assay. Source: UniProtKB heparin binding Inferred from direct assay. Source: UniProtKB type 2 fibroblast growth factor receptor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
FGFR2	P21802	1	EBI-1035684,EBI-1028658

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 37

Potential

Chain

38 – 208

171

Fibroblast growth factor 10

PRO_0000008981

Regions

Compositional bias

52 – 62

Poly-Ser

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

196

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

106

C → F in LADDS. Ref.11

VAR_029888

Natural variant

156

I → R in LADDS. Ref.10

VAR_029889

Experimental info

Sequence conflict

120

V → A in AAL05875. Ref.3

Sequence conflict

134

M → R in AAL05875. Ref.3

Secondary structure

208

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

O15520-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C0A0705C108680B3
Show »

FASTA

208

23,436

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of human fibroblast growth factor-10." Emoto H., Tagashira S., Mattei M.-G., Yamasaki M., Hashimoto G., Katsumata T., Negoro T., Nakatsuka M., Birnbaum D., Coulier F., Itoh N. J. Biol. Chem. 272:23191-23194(1997) [PubMed: 9287324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[2]	"Cutaneous wound healing by keratinocyte growth factor 2." 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. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[3]	Zhang Y., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." 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. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	NIEHS SNPs program Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"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." Beer H.-D., Bittner M., Niklaus G., Munding C., Max N., Goppelt A., Werner S. Oncogene 24:5269-5277(2005) [PubMed: 15806171] [Abstract] Cited for: INTERACTION WITH FGFBP1.
[8]	"Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors." Yeh B.K., Igarashi M., Eliseenkova A.V., Plotnikov A.N., Sher I., Ron D., Aaronson S.A., Mohammadi M. Proc. Natl. Acad. Sci. U.S.A. 100:2266-2271(2003) [PubMed: 12591959] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 69-208 IN COMPLEX WITH FGFR2.
[9]	"Mutations in the gene encoding fibroblast growth factor 10 are associated with aplasia of lacrimal and salivary glands." 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. Nat. Genet. 37:125-127(2005) [PubMed: 15654336] [Abstract] Cited for: INVOLVEMENT IN ALSG.
[10]	"LADD syndrome is caused by FGF10 mutations." Milunsky J.M., Zhao G., Maher T.A., Colby R., Everman D.B. Clin. Genet. 69:349-354(2006) [PubMed: 16630169] [Abstract] Cited for: VARIANT LADDS ARG-156.
[11]	"Mutations in different components of FGF signaling in LADD syndrome." 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. Nat. Genet. 38:414-417(2006) [PubMed: 16501574] [Abstract] Cited for: VARIANT LADDS PHE-106.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB002097 mRNA. Translation: BAA22331.1.
U67918 mRNA. Translation: AAB61991.1.
AF411527 mRNA. Translation: AAL05875.1.
CR541665 mRNA. Translation: CAG46466.1.
AY604046 Genomic DNA. Translation: AAS99733.1.
BC069561 mRNA. Translation: AAH69561.1.
BC105021 mRNA. Translation: AAI05022.1.
BC105023 mRNA. Translation: AAI05024.1.

IPI

IPI00007307.

RefSeq

NP_004456.1.

UniGene

Hs.664499

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NUN	X-ray	2.90	A	64-208	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6037N.

IntAct

O15520. 1 interaction.

STRING

O15520.

PTM databases

PhosphoSite

O15520.

Proteomic databases

PRIDE

O15520.

Genome annotation databases

Ensembl

ENST00000264664; ENSP00000264664; ENSG00000070193; Homo sapiens. [Genome view]

GeneID

2255.

KEGG

hsa:2255.

UCSC

uc003jog.1. human.

Organism-specific databases

CTD

2255.

GeneCards

GC05M044340.

H-InvDB

HIX0031935.

HGNC

HGNC:3666. FGF10.

HPA

CAB010315.

MIM

149730. phenotype.
180920. phenotype.
602115. gene.

Orphanet

86815. Aplasia of lacrimal and salivary glands.

PharmGKB

PA28106.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07737.

HOGENOM

HBG715603.

HOVERGEN

O15520.

InParanoid

O15520.

OMA

XKEFNND.

OrthoDB

EOG9QRKPR.

PhylomeDB

O15520.

Enzyme and pathway databases

Reactome

REACT_9470. Signaling by FGFR.

Gene expression databases

ArrayExpress

O15520.

Bgee

O15520.

CleanEx

HS_FGF10.

Genevestigator

O15520.

GermOnline

ENSG00000070193. Homo sapiens.

Family and domain databases

InterPro

IPR008996. Cytokine_IL1-like.
IPR002209. GF_heparin_bd.
IPR002348. IL1_HBGF.
[Graphical view]

PANTHER

PTHR11486. IL1_HBGF. 1 hit.

Pfam

PF00167. FGF. 1 hit.
[Graphical view]

PRINTS

PR00263. HBGFFGF.
PR00262. IL1HBGF.

SMART

SM00442. FGF. 1 hit.
[Graphical view]

PROSITE

PS00247. HBGF_FGF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

9135.

SOURCE

Search...

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Entry information

Entry name

FGF10_HUMAN

Accession

Primary (citable) accession number: O15520
Secondary accession number(s): Q6FHT6, Q96P59

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Human chromosome 5: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents