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P21674

- FST_RAT

UniProt

P21674 - FST_RAT

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Protein

Follistatin

Gene

Fst

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. activin binding Source: RGD
  2. heparan sulfate proteoglycan binding Source: RGD

GO - Biological processi

  1. BMP signaling pathway Source: Ensembl
  2. female gonad development Source: Ensembl
  3. gamete generation Source: Ensembl
  4. hair follicle morphogenesis Source: Ensembl
  5. hematopoietic progenitor cell differentiation Source: Ensembl
  6. keratinocyte proliferation Source: Ensembl
  7. negative regulation of activin receptor signaling pathway Source: Ensembl
  8. negative regulation of cell differentiation Source: Ensembl
  9. negative regulation of follicle-stimulating hormone secretion Source: RGD
  10. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  11. odontogenesis of dentin-containing tooth Source: Ensembl
  12. pattern specification process Source: Ensembl
  13. positive regulation of hair follicle development Source: Ensembl
  14. skeletal system development Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_198273. Antagonism of Activin by Follistatin.

Protein family/group databases

MEROPSiI01.966.

Names & Taxonomyi

Protein namesi
Recommended name:
Follistatin
Short name:
FS
Alternative name(s):
Activin-binding protein
Gene namesi
Name:Fst
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi2633. Fst.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular region Source: UniProtKB-KW
  3. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 344315FollistatinPRO_0000010106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 55PROSITE-ProRule annotation
Disulfide bondi42 ↔ 88PROSITE-ProRule annotation
Disulfide bondi56 ↔ 91PROSITE-ProRule annotation
Disulfide bondi95 ↔ 106
Disulfide bondi100 ↔ 116
Disulfide bondi118 ↔ 150
Disulfide bondi122 ↔ 143
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi132 ↔ 164
Disulfide bondi168 ↔ 179
Disulfide bondi173 ↔ 189
Disulfide bondi192 ↔ 225
Disulfide bondi196 ↔ 218
Disulfide bondi207 ↔ 239
Disulfide bondi270 ↔ 302PROSITE-ProRule annotation
Disulfide bondi274 ↔ 295PROSITE-ProRule annotation
Disulfide bondi284 ↔ 316PROSITE-ProRule annotation
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Gene expression databases

ExpressionAtlasiP21674. baseline and differential.
GenevestigatoriP21674.

Interactioni

Subunit structurei

Monomer.Curated

Binary interactionsi

WithEntry#Exp.IntActNotes
INHBAP084762EBI-5746973,EBI-8077140From a different organism.

Protein-protein interaction databases

IntActiP21674. 2 interactions.
MINTiMINT-1787002.

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi104 – 1085Combined sources
Beta strandi114 – 1185Combined sources
Helixi122 – 1243Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi138 – 1414Combined sources
Helixi142 – 15110Combined sources
Beta strandi158 – 1625Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi185 – 1906Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi213 – 2164Combined sources
Helixi217 – 22711Combined sources
Beta strandi233 – 2386Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LR7X-ray1.50A93-165[»]
1LR8X-ray2.10A93-165[»]
1LR9X-ray2.50A93-165[»]
2ARPX-ray2.00F93-241[»]
ProteinModelPortaliP21674.
SMRiP21674. Positions 30-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21674.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 10374TBAdd
BLAST
Domaini94 – 11724Follistatin-like 1Add
BLAST
Domaini112 – 16655Kazal-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini167 – 19024Follistatin-like 2Add
BLAST
Domaini186 – 24156Kazal-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini244 – 26825Follistatin-like 3Add
BLAST
Domaini264 – 31855Kazal-like 3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi321 – 33313Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Contains 3 follistatin-like domains.Curated
Contains 3 Kazal-like domains.PROSITE-ProRule annotation
Contains 1 TB (TGF-beta binding) domain.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG267610.
GeneTreeiENSGT00440000033501.
HOGENOMiHOG000261649.
HOVERGENiHBG051666.
InParanoidiP21674.
KOiK04661.
OMAiEAVCASD.
OrthoDBiEOG7GBFXR.
PhylomeDBiP21674.
TreeFamiTF106409.

Family and domain databases

InterProiIPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR017878. TB_dom.
[Graphical view]
PfamiPF09289. FOLN. 1 hit.
PF07648. Kazal_2. 3 hits.
[Graphical view]
SMARTiSM00274. FOLN. 3 hits.
SM00280. KAZAL. 3 hits.
[Graphical view]
SUPFAMiSSF57581. SSF57581. 1 hit.
PROSITEiPS51465. KAZAL_2. 3 hits.
PS51364. TB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21674-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVCARHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL
60 70 80 90 100
SKEECCSTGR LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC
110 120 130 140 150
GPGKKCRMNK KNKPRCVCAP DCSNITWKGP VCGLDGKTYR NECALLKARC
160 170 180 190 200
KEQPELEVQY QGKCKKTCRD VFCPGSSTCV VDQTNNAYCV TCNRICPEPS
210 220 230 240 250
SSEQSLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI KAKSCEDIQC
260 270 280 290 300
GGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA
310 320 330 340
ACSSGVLLEV KHSGSCNSIS EETEEEEEEE DQDYSFPISS TLEW
Length:344
Mass (Da):37,838
Last modified:May 1, 1991 - v1
Checksum:i864244CF05436552
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31591
, M31586, M31587, M31588, M31589, M31590 Genomic DNA. Translation: AAB60704.1.
S58913 Genomic DNA. Translation: AAP13905.1.
PIRiI57698.
RefSeqiNP_036693.1. NM_012561.1.
UniGeneiRn.162557.

Genome annotation databases

EnsembliENSRNOT00000015680; ENSRNOP00000015680; ENSRNOG00000011631.
GeneIDi24373.
KEGGirno:24373.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31591
, M31586 , M31587 , M31588 , M31589 , M31590 Genomic DNA. Translation: AAB60704.1 .
S58913 Genomic DNA. Translation: AAP13905.1 .
PIRi I57698.
RefSeqi NP_036693.1. NM_012561.1.
UniGenei Rn.162557.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LR7 X-ray 1.50 A 93-165 [» ]
1LR8 X-ray 2.10 A 93-165 [» ]
1LR9 X-ray 2.50 A 93-165 [» ]
2ARP X-ray 2.00 F 93-241 [» ]
ProteinModelPortali P21674.
SMRi P21674. Positions 30-317.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P21674. 2 interactions.
MINTi MINT-1787002.

Protein family/group databases

MEROPSi I01.966.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000015680 ; ENSRNOP00000015680 ; ENSRNOG00000011631 .
GeneIDi 24373.
KEGGi rno:24373.

Organism-specific databases

CTDi 10468.
RGDi 2633. Fst.

Phylogenomic databases

eggNOGi NOG267610.
GeneTreei ENSGT00440000033501.
HOGENOMi HOG000261649.
HOVERGENi HBG051666.
InParanoidi P21674.
KOi K04661.
OMAi EAVCASD.
OrthoDBi EOG7GBFXR.
PhylomeDBi P21674.
TreeFami TF106409.

Enzyme and pathway databases

Reactomei REACT_198273. Antagonism of Activin by Follistatin.

Miscellaneous databases

EvolutionaryTracei P21674.
NextBioi 603119.
PROi P21674.

Gene expression databases

ExpressionAtlasi P21674. baseline and differential.
Genevestigatori P21674.

Family and domain databases

InterProi IPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR017878. TB_dom.
[Graphical view ]
Pfami PF09289. FOLN. 1 hit.
PF07648. Kazal_2. 3 hits.
[Graphical view ]
SMARTi SM00274. FOLN. 3 hits.
SM00280. KAZAL. 3 hits.
[Graphical view ]
SUPFAMi SSF57581. SSF57581. 1 hit.
PROSITEi PS51465. KAZAL_2. 3 hits.
PS51364. TB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiFST_RAT
AccessioniPrimary (citable) accession number: P21674
Secondary accession number(s): Q80XW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 26, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3