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Q96PD4 (IL17F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-17F

Short name=IL-17F
Alternative name(s):
Cytokine ML-1
Gene names
Name:IL17F
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulates the production of other cytokines such as IL-6, IL-8 and granulocyte colony-stimulating factor, and can regulate cartilage matrix turnover. Stimulates PBMC and T-cell proliferation. Inhibits angiogenesis.

Subunit structure

Homodimer; disulfide-linked. Ref.7

Subcellular location

Secreted.

Tissue specificity

Expressed in activated, but not resting, CD4+ T-cells and activated monocytes.

Involvement in disease

Candidiasis, familial, 6 (CANDF6) [MIM:613956]: A primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the IL-17 family.

Sequence caution

The sequence AAL14427.1 differs from that shown. Reason: Intron retention.

The sequence CAD92646.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSignal
   Molecular functionCytokine
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcartilage development

Inferred from direct assay Ref.6. Source: UniProtKB

cytokine biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: InterPro

lymphotoxin A biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of angiogenesis

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of cytokine production involved in inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

proteoglycan metabolic process

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of granulocyte macrophage colony-stimulating factor biosynthetic process

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of interleukin-2 biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of interleukin-6 biosynthetic process

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of interleukin-8 biosynthetic process

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Non-traceable author statement Ref.6. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncytokine activity

Inferred from direct assay Ref.1. Source: UniProtKB

cytokine binding

Inferred from direct assay Ref.6. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.5
Chain31 – 163133Interleukin-17F
PRO_0000015432

Amino acid modifications

Glycosylation831N-linked (GlcNAc...) Ref.7
Disulfide bond47Interchain (with C-137) Ref.7
Disulfide bond102 ↔ 152 Ref.7
Disulfide bond107 ↔ 154 Ref.7
Disulfide bond137Interchain (with C-47) Ref.7

Natural variations

Natural variant951S → L in CANDF6. Ref.8
VAR_065813
Natural variant1261E → G.
Corresponds to variant rs2397084 [ dbSNP | Ensembl ].
VAR_058287
Natural variant1551V → I.
Corresponds to variant rs11465553 [ dbSNP | Ensembl ].
VAR_058288
Natural variant1611H → R. Ref.3
Corresponds to variant rs763780 [ dbSNP | Ensembl ].
VAR_058289

Secondary structure

........................ 163
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96PD4 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: E5287737C9E7BD46

FASTA16318,045
        10         20         30         40         50         60 
MTVKTLHGPA MVKYLLLSIL GLAFLSEAAA RKIPKVGHTF FQKPESCPPV PGGSMKLDIG 

        70         80         90        100        110        120 
IINENQRVSM SRNIESRSTS PWNYTVTWDP NRYPSEVVQA QCRNLGCINA QGKEDISMNS 

       130        140        150        160 
VPIQQETLVV RRKHQGCSVS FQLEKVLVTV GCTCVTPVIH HVQ 

« Hide

References

« Hide 'large scale' references
[1]"IL-17F, a novel cytokine selectively expressed in activated T cells and monocytes, regulates angiogenesis and endothelial cell cytokine production."
Starnes T., Robertson M.J., Sledge G., Kelich S., Nakshatri H., Broxmeyer H.E., Hromas R.
J. Immunol. 167:4137-4140(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-161.
Tissue: Blood.
[4]"Identification of a novel cytokine, ML-1, and its expression in subjects with asthma."
Kawaguchi M., Onuchic L.F., Li X.-D., Essayan D.M., Schroeder J., Xiao H.-Q., Liu M.C., Krishnaswamy G., Germino G., Huang S.-K.
J. Immunol. 167:4430-4435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-163.
[5]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-45.
[6]"IL-17s adopt a cystine knot fold: structure and activity of a novel cytokine, IL-17F, and implications for receptor binding."
Hymowitz S.G., Filvaroff E.H., Yin J.P., Lee J., Cai L., Risser P., Maruoka M., Mao W., Foster J., Kelley R.F., Pan G., Gurney A.L., de Vos A.M., Starovasnik M.A.
EMBO J. 20:5332-5341(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), CHARACTERIZATION.
[7]"Structural basis of receptor sharing by interleukin 17 cytokines."
Ely L.K., Fischer S., Garcia K.C.
Nat. Immunol. 10:1245-1251(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 31-163 IN COMPLEX WITH IL17R, GLYCOSYLATION AT ASN-83, SUBUNIT, DISULFIDE BONDS.
[8]"Chronic mucocutaneous candidiasis in humans with inborn errors of interleukin-17 immunity."
Puel A., Cypowyj S., Bustamante J., Wright J.F., Liu L., Lim H.K., Migaud M., Israel L., Chrabieh M., Audry M., Gumbleton M., Toulon A., Bodemer C., El-Baghdadi J., Whitters M., Paradis T., Brooks J., Collins M. expand/collapse author list , Wolfman N.M., Al-Muhsen S., Galicchio M., Abel L., Picard C., Casanova J.L.
Science 332:65-68(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CANDF6 LEU-95.
+Additional computationally mapped references.

Web resources

Wikipedia

Interleukin-17 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF384857 mRNA. Translation: AAK83350.1.
AL034343 Genomic DNA. Translation: CAD92646.1. Sequence problems.
BC070124 mRNA. Translation: AAH70124.1.
AF332389 mRNA. Translation: AAL14427.1. Sequence problems.
RefSeqNP_443104.1. NM_052872.3.
UniGeneHs.272295.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JPYX-ray2.85A/B/X/Y31-163[»]
3JVFX-ray3.30A/B31-163[»]
ProteinModelPortalQ96PD4.
SMRQ96PD4. Positions 38-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000337432.

Polymorphism databases

DMDM239938888.

Proteomic databases

PaxDbQ96PD4.
PRIDEQ96PD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336123; ENSP00000337432; ENSG00000112116.
GeneID112744.
KEGGhsa:112744.
UCSCuc003pal.1. human.

Organism-specific databases

CTD112744.
GeneCardsGC06M052101.
HGNCHGNC:16404. IL17F.
MIM606496. gene.
613956. phenotype.
neXtProtNX_Q96PD4.
Orphanet1334. Chronic mucocutaneous candidiasis.
PharmGKBPA29800.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248962.
HOGENOMHOG000064520.
HOVERGENHBG006143.
InParanoidQ96PD4.
KOK05494.
OMACPPLEDN.
OrthoDBEOG70089V.
PhylomeDBQ96PD4.
TreeFamTF314701.

Gene expression databases

BgeeQ96PD4.
CleanExHS_IL17F.
HS_IL24.
GenevestigatorQ96PD4.

Family and domain databases

InterProIPR020440. IL-17_chr.
IPR010345. IL-17_fam.
[Graphical view]
PANTHERPTHR21295. PTHR21295. 1 hit.
PfamPF06083. IL17. 1 hit.
[Graphical view]
PRINTSPR01932. INTRLEUKIN17.
ProtoNetSearch...

Other

EvolutionaryTraceQ96PD4.
GenomeRNAi112744.
NextBio78647.
PROQ96PD4.
SOURCESearch...

Entry information

Entry nameIL17F_HUMAN
AccessionPrimary (citable) accession number: Q96PD4
Secondary accession number(s): Q6NSI0 expand/collapse secondary AC list , Q7Z6P4, Q96PI8, Q9NUE6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM