Reviewed, UniProtKB/Swiss-Prot P31371 (FGF9_HUMAN)

Names and origin

Protein names

Recommended name:
    Glia-activating factor
      Short name=GAF
Alternative name(s):
    Fibroblast growth factor 9
      Short name=FGF-9
    HBGF-9

Gene names

Name:

FGF9

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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.

General annotation (Comments)

Function	May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.
Subunit structure	Monomer.
Subcellular location	Secreted.
Tissue specificity	Glial cells.
Post-translational modification	Three molecular species were found (30 kDa, 29 kDa and 25 kDa), cleaved at Leu-4, Val-13 and Ser-34 respectively. The smaller ones might be products of proteolytic digestion. Furthermore, there may be a functional signal sequence in the 30 kDa species which is uncleavable in the secretion step. N-glycosylated.
Involvement in disease	The continuous overexpression of GAFS may lead to malignant cell growth caused by an autocrine loop.
Sequence similarities	Belongs to the heparin-binding growth factors family.

Ontologies

Keywords
Biological process	Differentiation
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Ligand	Heparin-binding
Molecular function	Developmental protein Growth factor Mitogen
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell proliferation Inferred from electronic annotation. Source: UniProtKB-KW cell-cell signaling Traceable author statement. Source: ProtInc fibroblast growth factor receptor signaling pathway Inferred from Experiment. Source: Reactome
Cellular component	extracellular space Ref.1 Inferred from direct assay. Source: MGI
Molecular function	growth factor activity Ref.1 Traceable author statement. Source: ProtInc heparin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 3

3

Ref.5

PRO_0000008973

Chain

4 – 208

205

Glia-activating factor

PRO_0000008974

Amino acid modifications

Glycosylation

79

1

N-linked (GlcNAc...)

Natural variations

Natural variant

94

1

I → V: dbSNP rs12427696. Ref.2

VAR_020944

Experimental info

Sequence conflict

24 – 26

3

VLP → SLL AA sequence Ref.5

Sequence conflict

34

1

S → A AA sequence Ref.5

Secondary structure

1

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208

Helix Strand Turn

Details...

Helix

53 – 60

8

Beta strand

63 – 68

6

Beta strand

73 – 76

4

Beta strand

82 – 87

6

Helix

91 – 93

3

Beta strand

95 – 101

7

Beta strand

104 – 109

6

Turn

110 – 112

3

Beta strand

115 – 118

4

Beta strand

124 – 129

6

Helix

132 – 134

3

Beta strand

136 – 142

7

Beta strand

145 – 154

10

Turn

156 – 158

3

Beta strand

161 – 163

3

Helix

175 – 177

3

Helix

183 – 185

3

Beta strand

187 – 190

4

Helix

194 – 196

3

Helix

200 – 203

4

Sequences

	Sequence		Length	Mass (Da)
	P31371-1 [UniParc]. Last modified October 1, 1994. Version 3. Checksum: F32A0E7106EF59C9	FASTA	208	23,441
	10 20 30 40 50 60 MAPLGEVGNY FGVQDAVPFG NVPVLPVDSP VLLSDHLGQS EAGGLPRGPA VTDLDHLKGI 70 80 90 100 110 120 LRRRQLYCRT GFHLEIFPNG TIQGTRKDHS RFGILEFISI AVGLVSIRGV DSGLYLGMNE 130 140 150 160 170 180 KGELYGSEKL TQECVFREQF EENWYNTYSS NLYKHVDTGR RYYVALNKDG TPREGTRTKR 190 200 HQKFTHFLPR PVDPDKVPEL YKDILSQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a novel cytokine cDNA encoding the ninth member of the fibroblast growth factor family, which has a unique secretion property." Miyamoto M., Naruo K., Seko C., Matsumoto S., Kondo T., Kurokawa T. Mol. Cell. Biol. 13:4251-4259(1993) [PubMed: 8321227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Foreskin.
[2]	NIEHS SNPs program Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-94.
[3]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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].
[5]	"Novel secretory heparin-binding factors from human glioma cells (glia-activating factors) involved in glial cell growth. Purification and biological properties." Naruo K., Seko C., Kuroshima K., Matsutani E., Sasada R., Kondo T., Kurokawa T. J. Biol. Chem. 268:2857-2864(1993) [PubMed: 8428960] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-26 AND 34-54. Tissue: Glial tumor.
[6]	"Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces." Hecht H.J., Adar R., Hofmann B., Bogin O., Weich H., Yayon A. Acta Crystallogr. D 57:378-384(2001) [PubMed: 11223514] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

R&D Systems' cytokine source book: FGF-9

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

D14838 mRNA. Translation: BAA03572.1.
AY682094 Genomic DNA. Translation: AAT74624.1.
AL139378 Genomic DNA. Translation: CAC17692.1.
BC069692 mRNA. Translation: AAH69692.1.
BC103978 mRNA. Translation: AAI03979.1.
BC103979 mRNA. Translation: AAI03980.1.

IPI

IPI00011172.

PIR

A48137.

RefSeq

NP_002001.1.

UniGene

Hs.111
Hs.603710

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G82	X-ray	2.60	A/B/C/D	49-208	[»]
1IHK	X-ray	2.20	A	35-208	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6036N.

Proteomic databases

PRIDE

P31371.

Genome annotation databases

Ensembl

ENSG00000102678. Homo sapiens. [Contig view]

GeneID

2254.

KEGG

hsa:2254.

Organism-specific databases

GeneCards

GC13P021144.

H-InvDB

HIX0037350.

HGNC

HGNC:3687. FGF9.

HPA

CAB004392.

MIM

600921. gene.

PharmGKB

PA28126.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P31371.

HOVERGEN

P31371.

OMA

P31371. RFTHFLP.

Enzyme and pathway databases

Pathway_Interaction_DB

fgf_pathway. FGF signaling pathway.

Reactome

REACT_9470. Signaling by FGFR.

Gene expression databases

ArrayExpress

P31371.

Bgee

P31371.

CleanEx

HS_FGF9.

GermOnline

ENSG00000102678. Homo sapiens.

Family and domain databases

InterPro

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.

ProDom

PD000831. IL1_HBGF. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00442. FGF. 1 hit.
[Graphical view]

PROSITE

PS00247. HBGF_FGF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

9131.

SOURCE

Search...

Entry information

Entry name

FGF9_HUMAN

Accession

Primary (citable) accession number: P31371
Secondary accession number(s): Q3SY32

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)