You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP07709
Secondary Accession Numbers
  • 13418
Name Gelsolin
Synonyms
  1. ADF
  2. AGEL
  3. Actin-depolymerizing factor
  4. Brevin
Gene Name GSN
Protein Type Unknown
Biological Properties
General Function Involved in actin 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
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
protein binding
cytoskeletal protein binding
actin binding
Cellular Location
  1. Isoform 1:Secreted
Gene Properties
Chromosome Location Chromosome:9
Locus 9q33
SNPs GSN
Gene Sequence
>2349 bp
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
Protein Properties
Number of Residues 782
Molecular Weight 85696.9
Theoretical pI 6.19
Pfam Domain Function
Signals
  • 1-27
Transmembrane Regions
  • None
Protein Sequence
>Gelsolin
MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFL
KAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNEC
SQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVV
PNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNRYERLKA
TQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKL
YKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALK
TASDFITKMDYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGLGLSYLSSHIANVERV
PFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNY
RHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFG
GKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPS
AAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDK
KMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEK
TEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAEL
AA
GenBank ID Protein 736249
UniProtKB/Swiss-Prot ID P06396
UniProtKB/Swiss-Prot Entry Name GELS_HUMAN
PDB IDs
GenBank Gene ID X04412
GeneCard ID GSN
GenAtlas ID GSN
HGNC ID HGNC:4620
References
General References
  1. 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. [PubMed:15489334 ]
  2. 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. [PubMed:16959974 ]
  3. 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 ]
  4. 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 ]
  5. Lind SE, Janmey PA: Human plasma gelsolin binds to fibronectin. J Biol Chem. 1984 Nov 10;259(21):13262-6. [PubMed:6092370 ]
  6. 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 ]
  7. 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 ]
  8. 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 ]
  9. Allen PG: Functional consequences of disulfide bond formation in gelsolin. FEBS Lett. 1997 Jan 13;401(1):89-94. [PubMed:9003812 ]
  10. 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 ]
  11. 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. [PubMed:8395021 ]
  12. 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 ]
  13. 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 ]
  14. 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. [PubMed:1338910 ]