Follistatin
Details
- Name
- Follistatin
- Synonyms
- Activin-binding protein
- FS
- Gene Name
- FST
- Organism
- Humans
- 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
- Functionsactivin binding / signal transducer activityProcesseshematopoietic progenitor cell differentiation / negative regulation of activin receptor signaling pathway / negative regulation of transcription from RNA polymerase II promoter / positive regulation of hair follicle development / signal transductionComponentsextracellular region
- General Function
- Signal transducer activity
- Specific Function
- Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).
- Pfam Domain Function
- 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
- Not Available
- External Identifiers
Resource Link UniProtKB ID P19883 UniProtKB Entry Name FST_HUMAN HGNC ID HGNC:3971 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]