Follistatin

Details

Name
Follistatin
Kind
protein
Synonyms
  • Activin-binding protein
  • FS
Gene Name
FST
UniProtKB Entry
P19883Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0009447|Follistatin
MVRARHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGR
LSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAP
DCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCV
VDQTNNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCI
KAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEA
ACSSGVLLEVKHSGSCNSISEDTEEEEEDEDQDYSFPISSILEW
Number of residues
344
Molecular Weight
38006.785
Theoretical pI
Not Available
GO Classification
Functions
activin receptor antagonist activity / heparan sulfate proteoglycan binding
Processes
ameloblast differentiation / BMP signaling pathway / cell differentiation / female gonad development / gamete generation / hair follicle morphogenesis / keratinocyte proliferation / negative regulation of epithelial cell differentiation / negative regulation of transcription by RNA polymerase II / odontogenesis of dentin-containing tooth / pattern specification process / regulation of BMP signaling pathway / response to organic cyclic compound / skeletal system development
Components
cytoplasm / extracellular space / nucleus
General Function
Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH)
Specific Function
activin binding
Pfam Domain Function
Signal Regions
1-29
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0013165|Follistatin (FST)
ATGGTCCGCGCGAGGCACCAGCCGGGTGGGCTTTGCCTCCTGCTGCTGCTGCTCTGCCAG
TTCATGGAGGACCGCAGTGCCCAGGCTGGGAACTGCTGGCTCCGTCAAGCGAAGAACGGC
CGCTGCCAGGTCCTGTACAAGACCGAACTGAGCAAGGAGGAGTGCTGCAGCACCGGCCGG
CTGAGCACCTCGTGGACCGAGGAGGACGTGAATGACAACACACTCTTCAAGTGGATGATT
TTCAACGGGGGCGCCCCCAACTGCATCCCCTGTAAAGAAACGTGTGAGAACGTGGACTGT
GGACCTGGGAAAAAATGCCGAATGAACAAGAAGAACAAACCCCGCTGCGTCTGCGCCCCG
GATTGTTCCAACATCACCTGGAAGGGTCCAGTCTGCGGGCTGGATGGGAAAACCTACCGC
AATGAATGTGCACTCCTAAAGGCAAGATGTAAAGAGCAGCCAGAACTGGAAGTCCAGTAC
CAAGGCAGATGTAAAAAGACTTGTCGGGATGTTTTCTGTCCAGGCAGCTCCACATGTGTG
GTGGACCAGACCAATAATGCCTACTGTGTGACCTGTAATCGGATTTGCCCAGAGCCTGCT
TCCTCTGAGCAATATCTCTGTGGGAATGATGGAGTCACCTACTCCAGTGCCTGCCACCTG
AGAAAGGCTACCTGCCTGCTGGGCAGATCTATTGGATTAGCCTATGAGGGAAAGTGTATC
AAAGCAAAGTCCTGTGAAGATATCCAGTGCACTGGTGGGAAAAAATGTTTATGGGATTTC
AAGGTTGGGAGAGGCCGGTGTTCCCTCTGTGATGAGCTGTGCCCTGACAGTAAGTCGGAT
GAGCCTGTCTGTGCCAGTGACAATGCCACTTATGCCAGCGAGTGTGCCATGAAGGAAGCT
GCCTGCTCCTCAGGTGTGCTACTGGAAGTAAAGCACTCCGGATCTTGCAACTGA
Chromosome Location
5
Locus
5q11.2
External Identifiers
ResourceLink
UniProtKB IDP19883
UniProtKB Entry NameFST_HUMAN
GeneCard IDFST
HGNC IDHGNC:3971
PDB ID(s)2B0U, 2P6A, 3HH2, 5JHW
KEGG IDhsa:10468
NCBI Gene ID10468
General References
  1. Shimasaki S, Koga M, Esch F, Cooksey K, Mercado M, Koba A, Ueno N, Ying SY, Ling N, Guillemin R: Primary structure of the human follistatin precursor and its genomic organization. Proc Natl Acad Sci U S A. 1988 Jun;85(12):4218-22. [Article]
  2. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [Article]
  5. Schneyer AL, Wang Q, Sidis Y, Sluss PM: Differential distribution of follistatin isoforms: application of a new FS315-specific immunoassay. J Clin Endocrinol Metab. 2004 Oct;89(10):5067-75. [Article]
  6. Thompson TB, Lerch TF, Cook RW, Woodruff TK, Jardetzky TS: The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding. Dev Cell. 2005 Oct;9(4):535-43. [Article]
  7. Lerch TF, Shimasaki S, Woodruff TK, Jardetzky TS: Structural and biophysical coupling of heparin and activin binding to follistatin isoform functions. J Biol Chem. 2007 May 25;282(21):15930-9. Epub 2007 Apr 3. [Article]
  8. Cash JN, Rejon CA, McPherron AC, Bernard DJ, Thompson TB: The structure of myostatin:follistatin 288: insights into receptor utilization and heparin binding. EMBO J. 2009 Sep 2;28(17):2662-76. doi: 10.1038/emboj.2009.205. Epub 2009 Jul 30. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
D-Myo-Inositol-HexasulphateexperimentalunknowntargetDetails