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P21674 (FST_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Follistatin

Short name=FS
Alternative name(s):
Activin-binding protein
Gene names
Name:Fst
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).

Subunit structure

Monomer Potential.

Subcellular location

Secreted.

Sequence similarities

Contains 3 follistatin-like domains.

Contains 3 Kazal-like domains.

Contains 1 TB (TGF-beta binding) domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

female gonad development

Inferred from electronic annotation. Source: Ensembl

gamete generation

Inferred from electronic annotation. Source: Ensembl

hair follicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

hematopoietic progenitor cell differentiation

Inferred from electronic annotation. Source: Ensembl

keratinocyte proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of activin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of follicle-stimulating hormone secretion

Traceable author statement Ref.1. Source: RGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

pattern specification process

Inferred from electronic annotation. Source: Ensembl

positive regulation of hair follicle development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactivin binding

Traceable author statement PubMed 12203361. Source: RGD

heparan sulfate proteoglycan binding

Inferred from direct assay Ref.3. Source: RGD

protein binding

Inferred from physical interaction Ref.4. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

INHBAP084762EBI-5746973,EBI-8077140From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 344315Follistatin
PRO_0000010106

Regions

Domain30 – 10374TB
Domain94 – 11724Follistatin-like 1
Domain112 – 16655Kazal-like 1
Domain167 – 19024Follistatin-like 2
Domain186 – 24156Kazal-like 2
Domain244 – 26825Follistatin-like 3
Domain264 – 31855Kazal-like 3
Compositional bias321 – 33313Asp/Glu-rich (highly acidic)

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Disulfide bond32 ↔ 55 By similarity
Disulfide bond42 ↔ 88 By similarity
Disulfide bond56 ↔ 91 By similarity
Disulfide bond95 ↔ 106 Ref.3 Ref.4
Disulfide bond100 ↔ 116 Ref.3 Ref.4
Disulfide bond118 ↔ 150 Ref.3 Ref.4
Disulfide bond122 ↔ 143 Ref.3 Ref.4
Disulfide bond132 ↔ 164 Ref.3 Ref.4
Disulfide bond168 ↔ 179 Ref.3 Ref.4
Disulfide bond173 ↔ 189 Ref.3 Ref.4
Disulfide bond192 ↔ 225 Ref.3 Ref.4
Disulfide bond196 ↔ 218 Ref.3 Ref.4
Disulfide bond207 ↔ 239 Ref.3 Ref.4
Disulfide bond270 ↔ 302 By similarity
Disulfide bond274 ↔ 295 By similarity
Disulfide bond284 ↔ 316 By similarity

Secondary structure

............................. 344
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21674 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 864244CF05436552

FASTA34437,838
        10         20         30         40         50         60 
MVCARHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR 

        70         80         90        100        110        120 
LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP 

       130        140        150        160        170        180 
DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGKCKKTCRD VFCPGSSTCV 

       190        200        210        220        230        240 
VDQTNNAYCV TCNRICPEPS SSEQSLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI 

       250        260        270        280        290        300 
KAKSCEDIQC GGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA 

       310        320        330        340 
ACSSGVLLEV KHSGSCNSIS EETEEEEEEE DQDYSFPISS TLEW 

« Hide

References

[1]"Follistatin gene expression in the ovary and extragonadal tissues."
Shimasaki S., Koga M., Buscaglia M.L., Simmons D.M., Bicsak T.A., Ling N.
Mol. Endocrinol. 3:651-659(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Ovary.
[2]"Structural and functional characterization of the rat follistatin (activin-binding protein) gene promoter."
Miyanaga K., Shimasaki S.
Mol. Cell. Endocrinol. 92:99-109(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[3]"Crystal structures of the heparan sulfate-binding domain of follistatin. Insights into ligand binding."
Innis C.A., Hyvonen M.
J. Biol. Chem. 278:39969-39977(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 93-165 ALONE AND IN COMPLEX WITH HEPARIN ANALOGS, DISULFIDE BONDS.
[4]"Structural basis for the inhibition of activin signalling by follistatin."
Harrington A.E., Morris-Triggs S.A., Ruotolo B.T., Robinson C.V., Ohnuma S., Hyvonen M.
EMBO J. 25:1035-1045(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 93-241 IN COMPLEX WITH ACTIVIN A, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31591 expand/collapse EMBL AC list , M31586, M31587, M31588, M31589, M31590 Genomic DNA. Translation: AAB60704.1.
S58913 Genomic DNA. Translation: AAP13905.1.
PIRI57698.
RefSeqNP_036693.1. NM_012561.1.
UniGeneRn.162557.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LR7X-ray1.50A93-165[»]
1LR8X-ray2.10A93-165[»]
1LR9X-ray2.50A93-165[»]
2ARPX-ray2.00F93-241[»]
ProteinModelPortalP21674.
SMRP21674. Positions 30-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP21674. 2 interactions.
MINTMINT-1787002.

Protein family/group databases

MEROPSI01.966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015680; ENSRNOP00000015680; ENSRNOG00000011631.
GeneID24373.
KEGGrno:24373.

Organism-specific databases

CTD10468.
RGD2633. Fst.

Phylogenomic databases

eggNOGNOG267610.
GeneTreeENSGT00440000033501.
HOGENOMHOG000261649.
HOVERGENHBG051666.
InParanoidP21674.
KOK04661.
OMAEAVCASD.
OrthoDBEOG7GBFXR.
PhylomeDBP21674.
TreeFamTF106409.

Gene expression databases

GenevestigatorP21674.

Family and domain databases

InterProIPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR017878. TB_dom.
[Graphical view]
PfamPF09289. FOLN. 1 hit.
PF07648. Kazal_2. 3 hits.
[Graphical view]
SMARTSM00274. FOLN. 3 hits.
SM00280. KAZAL. 3 hits.
[Graphical view]
SUPFAMSSF57581. SSF57581. 1 hit.
PROSITEPS51465. KAZAL_2. 3 hits.
PS51364. TB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21674.
NextBio603119.
PROP21674.

Entry information

Entry nameFST_RAT
AccessionPrimary (citable) accession number: P21674
Secondary accession number(s): Q80XW7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references