FST_PIG
ID FST_PIG Reviewed; 344 AA.
AC P10669; P10670;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Follistatin {ECO:0000303|PubMed:3365249};
DE Short=FS;
DE AltName: Full=Activin-binding protein {ECO:0000303|PubMed:8340384};
DE Contains:
DE RecName: Full=FS-303;
DE AltName: Full=FS-B;
DE Flags: Precursor;
GN Name=FST {ECO:0000250|UniProtKB:P19883};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3365249; DOI=10.1016/s0006-291x(88)80097-4;
RA Shimasaki S., Koga M., Esch F., Mercado M., Cooksey K., Koba A., Ling N.;
RT "Porcine follistatin gene structure supports two forms of mature
RT follistatin produced by alternative splicing.";
RL Biochem. Biophys. Res. Commun. 152:717-723(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-334.
RX PubMed=3153465; DOI=10.1210/mend-1-11-849;
RA Esch F.S., Shimasaki S., Mercado M., Cooksey K., Ling N., Ying S., Ueno N.,
RA Guillemin R.;
RT "Structural characterization of follistatin: a novel follicle-stimulating
RT hormone release-inhibiting polypeptide from the gonad.";
RL Mol. Endocrinol. 1:849-855(1987).
RN [3]
RP PROTEIN SEQUENCE OF 30-37.
RX PubMed=3120188; DOI=10.1073/pnas.84.23.8282;
RA Ueno N., Ling N., Ying S.Y., Esch F., Shimasaki S., Guillemin R.;
RT "Isolation and partial characterization of follistatin: a single-chain Mr
RT 35,000 monomeric protein that inhibits the release of follicle-stimulating
RT hormone.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8282-8286(1987).
RN [4]
RP PROTEIN SEQUENCE OF 30-35; 120-128; 284-292 AND 312-344, SIGNAL SEQUENCE
RP CLEAVAGE SITE, GLYCOSYLATION AT ASN-288, AND IDENTIFICATION OF FS-303.
RX PubMed=8340384; DOI=10.1016/s0021-9258(18)82296-7;
RA Sugino K., Kurosawa N., Nakamura T., Takio K., Shimasaki S., Ling N.,
RA Titani K., Sugino H.;
RT "Molecular heterogeneity of follistatin, an activin-binding protein. Higher
RT affinity of the carboxyl-terminal truncated forms for heparan sulfate
RT proteoglycans on the ovarian granulosa cell.";
RL J. Biol. Chem. 268:15579-15587(1993).
CC -!- FUNCTION: Binds directly to activin and functions as an activin
CC antagonist. Specific inhibitor of the biosynthesis and secretion of
CC pituitary follicle stimulating hormone (FSH).
CC -!- SUBUNIT: Monomer. Isoform 2/FS-288 interacts with GDF11.
CC {ECO:0000250|UniProtKB:P19883, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=FS-315, FS-A;
CC IsoId=P10669-1; Sequence=Displayed;
CC Name=2; Synonyms=FS-288, FS-C;
CC IsoId=P10669-2; Sequence=VSP_001567;
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8340384}.
CC -!- PTM: FS-303 may be derived from mature isoform 1 by post-translational
CC proteolytic cleavage. It is the most abundant form in ovaries
CC (PubMed:8340384). {ECO:0000269|PubMed:8340384}.
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DR EMBL; M19529; AAA31036.1; -; Genomic_DNA.
DR EMBL; M19529; AAA31037.1; -; Genomic_DNA.
DR EMBL; M36512; AAA31038.1; -; Genomic_DNA.
DR PIR; A27701; A27701.
DR AlphaFoldDB; P10669; -.
DR SMR; P10669; -.
DR STRING; 9823.ENSSSCP00000017901; -.
DR MEROPS; I01.966; -.
DR iPTMnet; P10669; -.
DR PaxDb; P10669; -.
DR PRIDE; P10669; -.
DR Ensembl; ENSSSCT00005072078; ENSSSCP00005045016; ENSSSCG00005044724. [P10669-2]
DR Ensembl; ENSSSCT00015046401; ENSSSCP00015018366; ENSSSCG00015034381. [P10669-1]
DR Ensembl; ENSSSCT00015046584; ENSSSCP00015018425; ENSSSCG00015034381. [P10669-2]
DR Ensembl; ENSSSCT00025030617; ENSSSCP00025012951; ENSSSCG00025022494. [P10669-2]
DR Ensembl; ENSSSCT00030032510; ENSSSCP00030014615; ENSSSCG00030023421. [P10669-2]
DR Ensembl; ENSSSCT00030032534; ENSSSCP00030014628; ENSSSCG00030023421. [P10669-1]
DR Ensembl; ENSSSCT00035108421; ENSSSCP00035046965; ENSSSCG00035079239. [P10669-2]
DR Ensembl; ENSSSCT00040041296; ENSSSCP00040017298; ENSSSCG00040030658. [P10669-1]
DR Ensembl; ENSSSCT00040041443; ENSSSCP00040017360; ENSSSCG00040030658. [P10669-2]
DR Ensembl; ENSSSCT00045047171; ENSSSCP00045032752; ENSSSCG00045027630. [P10669-2]
DR Ensembl; ENSSSCT00050044398; ENSSSCP00050018278; ENSSSCG00050033092. [P10669-2]
DR Ensembl; ENSSSCT00055013575; ENSSSCP00055010685; ENSSSCG00055006989. [P10669-2]
DR Ensembl; ENSSSCT00060042408; ENSSSCP00060018058; ENSSSCG00060031325. [P10669-2]
DR Ensembl; ENSSSCT00065055893; ENSSSCP00065024288; ENSSSCG00065040871. [P10669-2]
DR Ensembl; ENSSSCT00070005017; ENSSSCP00070004078; ENSSSCG00070002683. [P10669-1]
DR Ensembl; ENSSSCT00070005029; ENSSSCP00070004090; ENSSSCG00070002683. [P10669-2]
DR eggNOG; KOG3649; Eukaryota.
DR HOGENOM; CLU_050745_0_0_1; -.
DR InParanoid; P10669; -.
DR PRO; PR:P10669; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 16.
DR Genevisible; P10669; SS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
DR Gene3D; 3.90.290.10; -; 1.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR015369; Follistatin/Osteonectin_EGF.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR Pfam; PF09289; FOLN; 1.
DR Pfam; PF07648; Kazal_2; 3.
DR SMART; SM00274; FOLN; 3.
DR SMART; SM00280; KAZAL; 3.
DR SUPFAM; SSF100895; SSF100895; 3.
DR SUPFAM; SSF57581; SSF57581; 1.
DR PROSITE; PS51465; KAZAL_2; 3.
DR PROSITE; PS51364; TB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:3120188,
FT ECO:0000269|PubMed:8340384"
FT CHAIN 30..344
FT /note="Follistatin"
FT /id="PRO_0000010105"
FT CHAIN 30..332
FT /note="FS-303"
FT /id="PRO_0000419163"
FT DOMAIN 30..103
FT /note="TB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 94..117
FT /note="Follistatin-like 1"
FT DOMAIN 112..166
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 167..190
FT /note="Follistatin-like 2"
FT DOMAIN 186..241
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 244..268
FT /note="Follistatin-like 3"
FT DOMAIN 264..318
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 314..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8340384"
FT DISULFID 32..55
FT /evidence="ECO:0000250|UniProtKB:P19883,
FT ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 42..88
FT /evidence="ECO:0000250|UniProtKB:P19883,
FT ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 56..91
FT /evidence="ECO:0000250|UniProtKB:P19883,
FT ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 95..106
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 100..116
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 118..150
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 122..143
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 132..164
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 168..179
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 173..189
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 192..225
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 196..218
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 207..239
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 245..256
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 250..267
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 270..302
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 274..295
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT DISULFID 284..316
FT /evidence="ECO:0000250|UniProtKB:P19883"
FT VAR_SEQ 318..344
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001567"
SQ SEQUENCE 344 AA; 38035 MW; 6906E7A23CF9BD21 CRC64;
MVRPKHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR
LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP
DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGKCKKTCRD VFCPGSSTCV
VDQTNNAYCV TCNRICPEPT SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI
KAKSCEDIQC TGGKKCLWDF KVGRGRCSLC DELCPESKSE EPVCASDNAT YASECAMKEA
ACSSGVLLEV KHSGSCNSIS EDTEEEEEDE DQDYSFPISS ILEW
