Gelsolin

Details

Name
Gelsolin
Kind
protein
Synonyms
  • Actin-depolymerizing factor
  • ADF
  • AGEL
  • Brevin
Gene Name
GSN
UniProtKB Entry
P06396Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0007918|Gelsolin
MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFL
KAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNEC
SQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVV
PNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNRYERLKA
TQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKL
YKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALK
TASDFITKMDYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGLGLSYLSSHIANVERV
PFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNY
RHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFG
GKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPS
AAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDK
KMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEK
TEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAEL
AA
Number of residues
782
Molecular Weight
85696.935
Theoretical pI
6.19
GO Classification
Functions
actin filament binding / phosphatidylinositol 3-kinase catalytic subunit binding / phosphatidylinositol-4,5-bisphosphate binding
Processes
actin filament depolymerization / actin filament organization / actin polymerization or depolymerization / cardiac muscle cell contraction / cell projection assembly / cellular response to type II interferon / central nervous system development / cilium assembly / relaxation of cardiac muscle / response to muscle stretch
Components
ficolin-1-rich granule lumen / phagocytic vesicle / secretory granule lumen
General Function
Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (PubMed:19666512). Plays a role in ciliogenesis (PubMed:20393563)
Specific Function
Actin binding
Pfam Domain Function
Signal Regions
1-27
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm, cytoskeleton
Gene sequence
>lcl|BSEQ0012897|Gelsolin (GSN)
ATGGCTCCGCACCGCCCCGCGCCCGCGCTGCTTTGCGCGCTGTCCCTGGCGCTGTGCGCG
CTGTCGCTGCCCGTCCGCGCGGCCACTGCGTCGCGGGGGGCGTCCCAGGCGGGGGCGCCC
CAGGGGCGGGTGCCCGAGGCGCGGCCCAACAGCATGGTGGTGGAACACCCCGAGTTCCTC
AAGGCAGGGAAGGAGCCTGGCCTGCAGATCTGGCGTGTGGAGAAGTTCGATCTGGTGCCC
GTGCCCACCAACCTTTATGGAGACTTCTTCACGGGCGACGCCTACGTCATCCTGAAGACA
GTGCAGCTGAGGAACGGAAATCTGCAGTATGACCTCCACTACTGGCTGGGCAATGAGTGC
AGCCAGGATGAGAGCGGGGCGGCCGCCATCTTTACCGTGCAGCTGGATGACTACCTGAAC
GGCCGGGCCGTGCAGCACCGTGAGGTCCAGGGCTTCGAGTCGGCCACCTTCCTAGGCTAC
TTCAAGTCTGGCCTGAAGTACAAGAAAGGAGGTGTGGCATCAGGATTCAAGCACGTGGTA
CCCAACGAGGTGGTGGTGCAGAGACTCTTCCAGGTCAAAGGGCGGCGTGTGGTCCGTGCC
ACCGAGGTACCTGTGTCCTGGGAGAGCTTCAACAATGGCGACTGCTTCATCCTGGACCTG
GGCAACAACATCCACCAGTGGTGTGGTTCCAACAGCAATCGGTATGAAAGACTGAAGGCC
ACACAGGTGTCCAAGGGCATCCGGGACAACGAGCGGAGTGGCCGGGCCCGAGTGCACGTG
TCTGAGGAGGGCACTGAGCCCGAGGCGATGCTCCAGGTGCTGGGCCCCAAGCCGGCTCTG
CCTGCAGGTACCGAGGACACCGCCAAGGAGGATGCGGCCAACCGCAAGCTGGCCAAGCTC
TACAAGGTCTCCAATGGTGCAGGGACCATGTCCGTCTCCCTCGTGGCTGATGAGAACCCC
TTCGCCCAGGGGGCCCTGAAGTCAGAGGACTGCTTCATCCTGGACCACGGCAAAGATGGG
AAAATCTTTGTCTGGAAAGGCAAGCAGGCAAACACGGAGGAGAGGAAGGCTGCCCTCAAA
ACAGCCTCTGACTTCATCACCAAGATGGACTACCCCAAGCAGACTCAGGTCTCGGTCCTT
CCTGAGGGCGGTGAGACCCCACTGTTCAAGCAGTTCTTCAAGAACTGGCGGGACCCAGAC
CAGACAGATGGCCTGGGCTTGTCCTACCTTTCCAGCCATATCGCCAACGTGGAGCGGGTG
CCCTTCGACGCCGCCACCCTGCACACCTCCACTGCCATGGCCGCCCAGCACGGCATGGAT
GACGATGGCACAGGCCAGAAACAGATCTGGAGAATCGAAGGTTCCAACAAGGTGCCCGTG
GACCCTGCCACATATGGACAGTTCTATGGAGGCGACAGCTACATCATTCTGTACAACTAC
CGCCATGGTGGCCGCCAGGGGCAGATAATCTATAACTGGCAGGGTGCCCAGTCTACCCAG
GATGAGGTCGCTGCATCTGCCATCCTGACTGCTCAGCTGGATGAGGAGCTGGGAGGTACC
CCTGTCCAGAGCCGTGTGGTCCAAGGCAAGGAGCCCGCCCACCTCATGAGCCTGTTTGGT
GGGAAGCCCATGATCATCTACAAGGGCGGCACCTCCCGCGAGGGCGGGCAGACAGCCCCT
GCCAGCACCCGCCTCTTCCAGGTCCGCGCCAACAGCGCTGGAGCCACCCGGGCTGTTGAG
GTATTGCCTAAGGCTGGTGCACTGAACTCCAACGATGCCTTTGTTCTGAAAACCCCCTCA
GCCGCCTACCTGTGGGTGGGTACAGGAGCCAGCGAGGCAGAGAAGACGGGGGCCCAGGAG
CTGCTCAGGGTGCTGCGGGCCCAACCTGTGCAGGTGGCAGAAGGCAGCGAGCCAGATGGC
TTCTGGGAGGCCCTGGGCGGGAAGGCTGCCTACCGCACATCCCCACGGCTGAAGGACAAG
AAGATGGATGCCCATCCTCCTCGCCTCTTTGCCTGCTCCAACAAGATTGGACGTTTTGTG
ATCGAAGAGGTTCCTGGTGAGCTCATGCAGGAAGACCTGGCAACGGATGACGTCATGCTT
CTGGACACCTGGGACCAGGTCTTTGTCTGGGTTGGAAAGGATTCTCAAGAAGAAGAAAAG
ACAGAAGCCTTGACTTCTGCTAAGCGGTACATCGAGACGGACCCAGCCAATCGGGATCGG
CGGACGCCCATCACCGTGGTGAAGCAAGGCTTTGAGCCTCCCTCCTTTGTGGGCTGGTTC
CTTGGCTGGGATGATGATTACTGGTCTGTGGACCCCTTGGACAGGGCCATGGCTGAGCTG
GCTGCCTGA
Chromosome Location
9
Locus
9q33.2
External Identifiers
ResourceLink
UniProtKB IDP06396
UniProtKB Entry NameGELS_HUMAN
GenBank Protein ID736249
GenBank Gene IDX04412
GeneCard IDGSN
HGNC IDHGNC:4620
PDB ID(s)1C0F, 1C0G, 1D4X, 1DEJ, 1EQY, 1ESV, 1H1V, 1KCQ, 1MDU, 1NLV, 1NM1, 1NMD, 1P8X, 1P8Z, 1SOL, 1T44, 1YAG, 1YVN, 2FF3, 2FF6, 2FH1, 2FH2, 2FH3, 2FH4, 3A5L, 3A5M, 3A5N, 3A5O, 3CI5, 3CIP, 3CJB, 3CJC, 3FFK, 3FFN, 3TU5, 4PKG, 4PKH, 4PKI, 4S10, 4Z94, 5FAE, 5FAF, 5H3M, 5H3N, 5O2Z, 5UBO, 5ZZ0, 6H1F, 6JCO, 6JEG, 6JEH, 6LJE, 6LJF, 6Q9R, 6Q9Z, 6QBF, 6QW3, 7P2B
KEGG IDhsa:2934
NCBI Gene ID2934
General References
  1. Kwiatkowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, Yin HL: Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature. 1986 Oct 2-8;323(6087):455-8. [Article]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [Article]
  4. 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]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [Article]
  6. Lind SE, Janmey PA: Human plasma gelsolin binds to fibronectin. J Biol Chem. 1984 Nov 10;259(21):13262-6. [Article]
  7. Haltia M, Prelli F, Ghiso J, Kiuru S, Somer H, Palo J, Frangione B: Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein. Biochem Biophys Res Commun. 1990 Mar 30;167(3):927-32. [Article]
  8. Maury CP, Alli K, Baumann M: Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline. FEBS Lett. 1990 Jan 15;260(1):85-7. [Article]
  9. Wen D, Corina K, Chow EP, Miller S, Janmey PA, Pepinsky RB: The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure. Biochemistry. 1996 Jul 30;35(30):9700-9. [Article]
  10. Allen PG: Functional consequences of disulfide bond formation in gelsolin. FEBS Lett. 1997 Jan 13;401(1):89-94. [Article]
  11. De Corte V, Demol H, Goethals M, Van Damme J, Gettemans J, Vandekerckhove J: Identification of Tyr438 as the major in vitro c-Src phosphorylation site in human gelsolin: a mass spectrometric approach. Protein Sci. 1999 Jan;8(1):234-41. [Article]
  12. Kim J, Lee JE, Heynen-Genel S, Suyama E, Ono K, Lee K, Ideker T, Aza-Blanc P, Gleeson JG: Functional genomic screen for modulators of ciliogenesis and cilium length. Nature. 2010 Apr 15;464(7291):1048-51. doi: 10.1038/nature08895. [Article]
  13. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  14. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  15. McLaughlin PJ, Gooch JT, Mannherz HG, Weeds AG: Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature. 1993 Aug 19;364(6439):685-92. [Article]
  16. Xian W, Vegners R, Janmey PA, Braunlin WH: Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: behavior in solutions of mixed solvent and anionic micelles. Biophys J. 1995 Dec;69(6):2695-702. [Article]
  17. Chumnarnsilpa S, Loonchanta A, Xue B, Choe H, Urosev D, Wang H, Lindberg U, Burtnick LD, Robinson RC: Calcium ion exchange in crystalline gelsolin. J Mol Biol. 2006 Mar 31;357(3):773-82. Epub 2006 Jan 26. [Article]
  18. Durer ZA, Kudryashov DS, Sawaya MR, Altenbach C, Hubbell W, Reisler E: Structural states and dynamics of the D-loop in actin. Biophys J. 2012 Sep 5;103(5):930-9. [Article]
  19. Ghiso J, Haltia M, Prelli F, Novello J, Frangione B: Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type. Biochem J. 1990 Dec 15;272(3):827-30. [Article]
  20. de la Chapelle A, Tolvanen R, Boysen G, Santavy J, Bleeker-Wagemakers L, Maury CP, Kere J: Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187. Nat Genet. 1992 Oct;2(2):157-60. [Article]
  21. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Latrunculin AexperimentalunknowntargetDetails
Copperapproved, investigationalunknowntargetDetails
Zincapproved, investigationalunknowntargetDetails
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