[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 3). PubMed=3380788 [NCBI, ExPASy, EBI, Israel, Japan] Shimasaki S., Koga M., Esch F., Cooksey K., Mercado M., Koba A., Ueno N., Ying S.-Y., Ling N., Guillemin R.; "Primary structure of the human follistatin precursor and its genomic organization."; Proc. Natl. Acad. Sci. U.S.A. 85:4218-4222(1988).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Pancreas; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PROTEIN SEQUENCE OF 30-44. DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Z., Henzel W.J.; "Signal peptide prediction based on analysis of experimentally verified cleavage sites."; Protein Sci. 13:2819-2824(2004).
[4]	TISSUE SPECIFICITY. DOI=10.1210/jc.2004-0162; PubMed=15472207 [NCBI, ExPASy, EBI, Israel, Japan] Schneyer A.L., Wang Q., Sidis Y., Sluss P.M.; "Differential distribution of follistatin isoforms: application of a new FS315-specific immunoassay."; J. Clin. Endocrinol. Metab. 89:5067-5075(2004).
[5]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-317 IN COMPLEX WITH ACTIVIN A, AND DISULFIDE BONDS. DOI=10.1016/j.devcel.2005.09.008; PubMed=16198295 [NCBI, ExPASy, EBI, Israel, Japan] Thompson T.B., Lerch T.F., Cook R.W., Woodruff T.K., Jardetzky T.S.; "The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding."; Dev. Cell 9:535-543(2005).
[6]	X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 30-344 IN COMPLEX WITH ACTIVIN A, AND DISULFIDE BONDS. DOI=10.1074/jbc.M700737200; PubMed=17409095 [NCBI, ExPASy, EBI, Israel, Japan] Lerch T.F., Shimasaki S., Woodruff T.K., Jardetzky T.S.; "Structural and biophysical coupling of heparin and activin binding to follistatin isoform functions."; J. Biol. Chem. 282:15930-15939(2007).

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: Monomer (Potential).
INTERACTION:
P03950:ANG; NbExp=2; IntAct=EBI-1571188, EBI-525291;
P03950:ANG; NbExp=2; IntAct=EBI-1571208, EBI-525291;
SUBCELLULAR LOCATION: Secreted.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	FS315
Isoform ID	P19883-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	FS288
Isoform ID	P19883-2
Features which should be applied to build the isoform sequence: VSP_001565.

Name	3
Synonyms	FS303
Isoform ID	P19883-3
Features which should be applied to build the isoform sequence: VSP_001566.

TISSUE SPECIFICITY: Isoform 1 is the predominant isoform in serum but is undetectable in follicular fluid.
SIMILARITY: Contains 3 follistatin-like domains.
SIMILARITY: Contains 3 Kazal-like domains.
SIMILARITY: Contains 1 TB (TGF-beta binding) domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M19481; AAA35851.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19480; AAA35851.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004107; AAH04107.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A32141; A32141.

NP_037541.1; -.

3D structure databases

PDB

2B0U; X-ray; 2.80 A; C/D=30-317.	[ExPASy / RCSB / EBI]
2P6A; X-ray; 3.40 A; C/D=30-344.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2B0U; -.
2P6A; -.

ModBase

P19883.

Protein-protein interaction databases

IntAct

P19883; -.

Protein family/group databases

MEROPS

I01.966; -.

Organism-specific databases

HIX0004856; -.

HGNC:3971; FST.

FST.

HPA018155; -.

136470; gene. [NCBI / EBI]

Orphanet

3185; Stein-Leventhal syndrome.

PharmGKB

PA28388; -.

GeneCards

P19883.

Gene expression databases

ArrayExpress

P19883; -.

CleanEx

HS_FST; -.

GermOnline

ENSG00000134363; Homo sapiens.

Ontologies

GO:0005576;	Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0017106;	Molecular function: activin inhibitor activity (non-traceable author statement from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0046882;	Biological process: negative regulation of follicle-stimulating hormone secretion (non-traceable author statement from UniProtKB).
GO:0000122;	Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
GO:0051798;	Biological process: positive regulation of hair follicle development (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR003645; Fol_N.
IPR015204; Fol_N_sub.
IPR002350; Prot_inh_Kazal.
Graphical view of domain structure.

Pfam

PF09120; EGF-like_subdom; 1.
PF00050; Kazal_1; 3.
Pfam graphical view of domain structure.

SMART

SM00274; FOLN; 3.
SM00280; KAZAL; 3.
SMART graphical view of domain structure.

PROSITE

PS00282; KAZAL; FALSE_NEG.
PS51364; TB; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSG00000134363; Homo sapiens. [Contig view]

GeneID

10468; -.

Phylogenomic databases

HOGENOM

P19883; -.

HOVERGEN

P19883; -.

Other

NextBio

39699; -.

SOURCE

FST; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Direct protein sequencing; Glycoprotein; Repeat; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 29`	`29`
`CHAIN`	`30 344`	`315`	`Follistatin.`	`PRO_0000010103`
`DOMAIN`	`30 103`	`74`	`TB.`
`DOMAIN`	`94 117`	`24`	`Follistatin-like 1.`
`DOMAIN`	`118 164`	`47`	`Kazal-like 1.`
`DOMAIN`	`167 190`	`24`	`Follistatin-like 2.`
`DOMAIN`	`192 239`	`48`	`Kazal-like 2.`
`DOMAIN`	`244 268`	`25`	`Follistatin-like 3.`
`DOMAIN`	`270 316`	`47`	`Kazal-like 3.`
`COMPBIAS`	`321 333`	`13`	`Asp/Glu-rich (highly acidic).`
`CARBOHYD`	`124 124`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`288 288`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`32 55`
`DISULFID`	`42 88`
`DISULFID`	`56 91`
`DISULFID`	`95 106`
`DISULFID`	`100 116`
`DISULFID`	`118 150`
`DISULFID`	`122 143`
`DISULFID`	`132 164`
`DISULFID`	`192 225`
`DISULFID`	`196 218`
`DISULFID`	`207 239`
`DISULFID`	`270 302`
`DISULFID`	`274 295`
`DISULFID`	`284 316`
`VAR_SEQ`	`318 344`		`Missing (in isoform 2).`	`VSP_001565`
`VAR_SEQ`	`318 323`		`Missing (in isoform 3).`	`VSP_001566`
`STRAND`	`31 36`	`6`
`STRAND`	`42 44`	`3`
`STRAND`	`47 49`	`3`
`HELIX`	`52 56`	`5`
`STRAND`	`64 66`	`3`
`HELIX`	`72 77`	`6`
`TURN`	`78 80`	`3`
`STRAND`	`81 87`	`7`
`STRAND`	`89 91`	`3`
`STRAND`	`104 108`	`5`
`STRAND`	`114 118`	`5`
`HELIX`	`123 125`	`3`
`STRAND`	`131 133`	`3`
`STRAND`	`138 141`	`4`
`HELIX`	`142 152`	`11`
`STRAND`	`158 163`	`6`
`STRAND`	`166 168`	`3`
`STRAND`	`178 181`	`4`
`STRAND`	`187 190`	`4`
`STRAND`	`202 204`	`3`
`STRAND`	`206 208`	`3`
`STRAND`	`213 216`	`4`
`HELIX`	`217 227`	`11`
`STRAND`	`233 238`	`6`
`HELIX`	`245 247`	`3`
`STRAND`	`255 259`	`5`
`TURN`	`260 263`	`4`
`STRAND`	`264 268`	`5`
`STRAND`	`283 285`	`3`
`STRAND`	`290 293`	`4`
`HELIX`	`294 304`	`11`
`STRAND`	`310 314`	`5`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 38007 Da [This is the MW of the unprocessed precursor]

CRC64: D9BB45055D84AC90 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVRARHQPGG 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 QGRCKKTCRD VFCPGSSTCV 

       190        200        210        220        230        240 
VDQTNNAYCV TCNRICPEPA SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI 

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

       310        320        330        340 
ACSSGVLLEV KHSGSCNSIS EDTEEEEEDE DQDYSFPISS ILEW

P19883 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools