P21674 (FST_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Follistatin
Short name=FS

Alternative name(s):
Activin-binding protein

Gene names

Name:

Fst

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	344 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	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 component	Secreted
Domain	Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Inferred from electronic annotation. Source: Compara female gonad development Inferred from electronic annotation. Source: Compara gamete generation Inferred from electronic annotation. Source: Compara hair follicle morphogenesis Inferred from electronic annotation. Source: Compara hematopoietic progenitor cell differentiation Inferred from electronic annotation. Source: Compara keratinocyte proliferation Inferred from electronic annotation. Source: Compara negative regulation of activin receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of cell differentiation Inferred from electronic annotation. Source: Compara 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: Compara odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara pattern specification process Inferred from electronic annotation. Source: Compara positive regulation of hair follicle development Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	activin binding Traceable author statement PubMed 12203361. Source: RGD heparan sulfate proteoglycan binding Inferred from direct assay Ref.3. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Chain

30 – 344

315

Follistatin

PRO_0000010106

Regions

Domain

30 – 103

74

TB

Domain

94 – 117

24

Follistatin-like 1

Domain

112 – 166

55

Kazal-like 1

Domain

167 – 190

24

Follistatin-like 2

Domain

186 – 241

56

Kazal-like 2

Domain

244 – 268

25

Follistatin-like 3

Domain

264 – 318

55

Kazal-like 3

Compositional bias

321 – 333

13

Asp/Glu-rich (highly acidic)

Amino acid modifications

Glycosylation

124

1

N-linked (GlcNAc...) Potential

Glycosylation

288

1

N-linked (GlcNAc...) Potential

Disulfide bond

32 ↔ 55

By similarity

Disulfide bond

42 ↔ 88

By similarity

Disulfide bond

56 ↔ 91

By similarity

Disulfide bond

95 ↔ 106

Ref.3 Ref.4

Disulfide bond

100 ↔ 116

Ref.3 Ref.4

Disulfide bond

118 ↔ 150

Ref.3 Ref.4

Disulfide bond

122 ↔ 143

Ref.3 Ref.4

Disulfide bond

132 ↔ 164

Ref.3 Ref.4

Disulfide bond

168 ↔ 179

Ref.3 Ref.4

Disulfide bond

173 ↔ 189

Ref.3 Ref.4

Disulfide bond

192 ↔ 225

Ref.3 Ref.4

Disulfide bond

196 ↔ 218

Ref.3 Ref.4

Disulfide bond

207 ↔ 239

Ref.3 Ref.4

Disulfide bond

270 ↔ 302

By similarity

Disulfide bond

274 ↔ 295

By similarity

Disulfide bond

284 ↔ 316

By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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344

Helix Strand Turn

Details...

Beta strand

104 – 108

5

Beta strand

114 – 118

5

Helix

122 – 124

3

Beta strand

131 – 133

3

Beta strand

138 – 141

4

Helix

142 – 151

10

Beta strand

158 – 162

5

Beta strand

166 – 168

3

Beta strand

178 – 181

4

Beta strand

185 – 190

6

Beta strand

200 – 202

3

Beta strand

206 – 208

3

Beta strand

213 – 216

4

Helix

217 – 227

11

Beta strand

233 – 238

6

Sequences

	Sequence		Length	Mass (Da)
	P21674 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 864244CF05436552	FASTA	344	37,838
	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

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 , M31586, M31587, M31588, M31589, M31590 Genomic DNA. Translation: AAB60704.1.
S58913 Genomic DNA. Translation: AAP13905.1.

IPI

IPI00205317.

PIR

I57698.

RefSeq

NP_036693.1. NM_012561.1.

UniGene

Rn.162557.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P21674.

SMR

P21674. Positions 30-317.

ModBase

Search...

Protein-protein interaction databases

IntAct

P21674. 1 interaction.

MINT

MINT-1787002.

Protein family/group databases

MEROPS

I01.966.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000015680; ENSRNOP00000015680; ENSRNOG00000011631.

GeneID

24373.

KEGG

rno:24373.

Organism-specific databases

CTD

10468.

RGD

2633. Fst.

Phylogenomic databases

eggNOG

NOG267610.

GeneTree

ENSGT00440000033501.

HOGENOM

HOG000261649.

HOVERGEN

HBG051666.

InParanoid

P21674.

KO

K04661.

OMA

EAVCASD.

OrthoDB

EOG4QRH47.

Gene expression databases

ArrayExpress

P21674.

Genevestigator

P21674.

GermOnline

ENSRNOG00000011631. Rattus norvegicus.

Family and domain databases

InterPro

IPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR017878. TB_dom.
[Graphical view]

Pfam

PF09289. FOLN. 1 hit.
PF07648. Kazal_2. 3 hits.
[Graphical view]

SMART

SM00274. FOLN. 3 hits.
SM00280. KAZAL. 3 hits.
[Graphical view]

PROSITE

PS00282. KAZAL_1. False negative.
PS51465. KAZAL_2. 3 hits.
PS51364. TB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P21674.

NextBio

603119.

Entry information

Entry name

FST_RAT

Accession

Primary (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:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program