Gelsolin

Details

Name
Gelsolin
Synonyms
  • Actin-depolymerizing factor
  • ADF
  • AGEL
  • Brevin
Gene Name
GSN
Organism
Humans
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 binding / calcium ion binding / myosin II binding / protein domain specific binding
Processes
actin filament capping / actin filament polymerization / actin filament reorganization / actin filament severing / actin nucleation / aging / amyloid fibril formation / apoptotic process / barbed-end actin filament capping / cellular component disassembly involved in execution phase of apoptosis / cellular protein metabolic process / cellular response to cadmium ion / cilium morphogenesis / hepatocyte apoptotic process / negative regulation of viral entry into host cell / oligodendrocyte development / phagocytosis, engulfment / phosphatidylinositol-mediated signaling / positive regulation of actin nucleation / positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / positive regulation of gene expression / positive regulation of keratinocyte apoptotic process / positive regulation of protein processing in phagocytic vesicle / programmed cell death / protein destabilization / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of podosome assembly / regulation of receptor clustering / regulation of wound healing, spreading of epidermal cells / renal protein absorption / response to ethanol / response to folic acid / sequestering of actin monomers / striated muscle atrophy / tissue regeneration
Components
actin cap / actin cytoskeleton / blood microparticle / cortical actin cytoskeleton / cytoplasm / cytosol / extracellular exosome / extracellular region / extracellular space / focal adhesion / lamellipodium / myelin sheath / perinuclear region of cytoplasm / plasma membrane / podosome / ruffle / sarcoplasm
General Function
Protein domain specific binding
Specific 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. Plays a role in ciliogenesis.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
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
External Identifiers
ResourceLink
UniProtKB IDP06396
UniProtKB Entry NameGELS_HUMAN
GenBank Protein ID736249
GenBank Gene IDX04412
HGNC IDHGNC:4620
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. [PubMed:3020431]
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  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. [PubMed:12665801]
  6. Lind SE, Janmey PA: Human plasma gelsolin binds to fibronectin. J Biol Chem. 1984 Nov 10;259(21):13262-6. [PubMed:6092370]
  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. [PubMed:2157434]
  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. [PubMed:2153578]
  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. [PubMed:8703941]
  10. Allen PG: Functional consequences of disulfide bond formation in gelsolin. FEBS Lett. 1997 Jan 13;401(1):89-94. [PubMed:9003812]
  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. [PubMed:10210201]
  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. [PubMed:20393563]
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  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. [PubMed:8599675]
  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. [PubMed:16466744]
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  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. [PubMed:2176481]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02621Latrunculin AexperimentalunknownDetails
DB09130Copperapproved, investigationalunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownDetails