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follistatin; FS; activin-binding protein (FST)
Function:
- activin-binding protein & activin antagonist in vitro
- can bind to heparin sulfate proteoglycans & may function in vivo to present activins to their receptors [1]
- specific inhibitor of the biosynthesis & secretion of pituitary follicle stimulating hormone (FSH)
- follistatin appears to inhibit myostatin [2]
Structure:
- monomer (putative)
- contains 3 follistatin-like domains
- contains 3 Kazal-like domains
- contains 1 TB (TGF-beta binding) domain
Compartment: secreted
Alternative splicing: named isoforms=3
Expression:
- isoform 1 is the predominant isoform in serum but is undetectable in follicular fluid
Pathology:
- follistatin deficient mice die within a few hours of birth; defects are more widespread than with activin-deficient mice suggesting that follistatin may modulate the actions of several members of the TGF-beta family
General
glycoprotein
secreted protein
Properties
SIZE: entity length = 344 aa
MW = 38 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-29}
TB {30-103}
MOTIF: cysteine residue {C32}
MODIFICATION: cysteine residue {C55}
cysteine residue {C42}
MODIFICATION: cysteine residue {C88}
cysteine residue {C55}
MODIFICATION: cysteine residue {C32}
cysteine residue {C56}
MODIFICATION: cysteine residue {C91}
cysteine residue {C88}
MODIFICATION: cysteine residue {C42}
cysteine residue {C91}
MODIFICATION: cysteine residue {C56}
Follistatin-like 1 {94-117}
MOTIF: cysteine residue {C95}
MODIFICATION: cysteine residue {C106}
cysteine residue {C100}
MODIFICATION: cysteine residue {C116}
cysteine residue {C106}
MODIFICATION: cysteine residue {C95}
cysteine residue {C116}
MODIFICATION: cysteine residue {C100}
Kazal-type serine protease inhibitor domain {118-164}
MOTIF: cysteine residue {X+0}
MODIFICATION: cysteine residue {X+X4}
cysteine residue {X+X1}
MODIFICATION: cysteine residue {X+X3}
cysteine residue {X+X2}
MODIFICATION: cysteine residue {X+X5}
cysteine residue {X+X3}
MODIFICATION: cysteine residue {X+X1}
cysteine residue {X+X4}
MODIFICATION: cysteine residue {X+0}
cysteine residue {X+X5}
MODIFICATION: cysteine residue {X+X2}
cysteine residue {C118}
MODIFICATION: cysteine residue {C150}
cysteine residue {C122}
MODIFICATION: cysteine residue {C143}
N-glycosylation site {N124}
cysteine residue {C132}
MODIFICATION: cysteine residue {C164}
cysteine residue {C143}
MODIFICATION: cysteine residue {C122}
cysteine residue {C150}
MODIFICATION: cysteine residue {C118}
cysteine residue {C164}
MODIFICATION: cysteine residue {C132}
FOR-BINDING-OF: serine protease
Follistatin-like 2 {167-190}
Kazal-type serine protease inhibitor domain {192-239}
MOTIF: cysteine residue {X+0}
MODIFICATION: cysteine residue {X+X4}
cysteine residue {X+X1}
MODIFICATION: cysteine residue {X+X3}
cysteine residue {X+X2}
MODIFICATION: cysteine residue {X+X5}
cysteine residue {X+X3}
MODIFICATION: cysteine residue {X+X1}
cysteine residue {X+X4}
MODIFICATION: cysteine residue {X+0}
cysteine residue {X+X5}
MODIFICATION: cysteine residue {X+X2}
cysteine residue {C192}
MODIFICATION: cysteine residue {C225}
cysteine residue {C196}
MODIFICATION: cysteine residue {C218}
cysteine residue {C207}
MODIFICATION: cysteine residue {C239}
cysteine residue {C218}
MODIFICATION: cysteine residue {C196}
cysteine residue {C225}
MODIFICATION: cysteine residue {C192}
cysteine residue {C239}
MODIFICATION: cysteine residue {C207}
FOR-BINDING-OF: serine protease
Follistatin-like 3 {244-268}
Kazal-type serine protease inhibitor domain {270-316}
MOTIF: cysteine residue {X+0}
MODIFICATION: cysteine residue {X+X4}
cysteine residue {X+X1}
MODIFICATION: cysteine residue {X+X3}
cysteine residue {X+X2}
MODIFICATION: cysteine residue {X+X5}
cysteine residue {X+X3}
MODIFICATION: cysteine residue {X+X1}
cysteine residue {X+X4}
MODIFICATION: cysteine residue {X+0}
cysteine residue {X+X5}
MODIFICATION: cysteine residue {X+X2}
cysteine residue {C270}
MODIFICATION: cysteine residue {C302}
cysteine residue {C274}
MODIFICATION: cysteine residue {C295}
cysteine residue {C284}
MODIFICATION: cysteine residue {C316}
N-glycosylation site {N288}
cysteine residue {C295}
MODIFICATION: cysteine residue {C274}
cysteine residue {C302}
MODIFICATION: cysteine residue {C270}
cysteine residue {C316}
MODIFICATION: cysteine residue {C284}
FOR-BINDING-OF: serine protease
acidic region {321-333}
MOTIF: acidic residue (SEVERAL)
Database Correlations
OMIM 136470
UniProt P19883
PFAM correlations
Entrez Gene 10468
References
- Matzuk MM, Lu N, Vogel H, Sellheyer K, Roop DR, Bradley A.
Multiple defects and perinatal death in mice deficient in
follistatin.
Nature. 1995 Mar 23;374(6520):360-3.
PMID: 7885475
- Benabdallah BF et al
Inhibiting myostatin with follistatin improves the success
of myoblast transplantation in dystrophic mice.
Cell Transplant. 2008;17(3):337-50.
PMID: 18522236
UniProt :accession P19883