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UniProtKB/Swiss-Prot entry P06396


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GELS_HUMAN
Primary accession number P06396
Secondary accession number Q8WVV7
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 115)
Name and origin of the protein
Protein name Gelsolin [Precursor]
Synonyms Actin-depolymerizing factor
ADF
Brevin
AGEL
Gene name
Name: GSN
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE INITIATION.
DOI=10.1038/323455a0; PubMed=3020431 [NCBI, ExPASy, EBI, Israel, Japan]
Kwiatkowski D.J., Stossel T.P., Orkin S.H., Mole J.E., Colten H.R., Yin H.L.;
"Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain.";
Nature 323:455-458(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, and Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 53-72 (ISOFORM 2).
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[4]
INTERACTION WITH FIBRONECTIN.
PubMed=6092370 [NCBI, ExPASy, EBI, Israel, Japan]
Lind S.E., Janmey P.A.;
"Human plasma gelsolin binds to fibronectin.";
J. Biol. Chem. 259:13262-13266(1984).
[5]
IDENTITY OF FAF AMYLOID PROTEIN WITH GELSOLIN.
DOI=10.1016/0006-291X(90)90612-Q; PubMed=2157434 [NCBI, ExPASy, EBI, Israel, Japan]
Haltia M., Prelli F., Ghiso J., Kiuru S., Sommer H., Palo J., Frangione B.;
"Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein.";
Biochem. Biophys. Res. Commun. 167:927-932(1990).
[6]
IDENTITY OF FAF AMYLOID PROTEIN WITH GELSOLIN.
DOI=10.1016/0014-5793(90)80072-Q; PubMed=2153578 [NCBI, ExPASy, EBI, Israel, Japan]
Maury C.P.J., Alli K., Baumann M.;
"Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline.";
FEBS Lett. 260:85-87(1990).
[7]
DISULFIDE BOND.
DOI=10.1021/bi960920n; PubMed=8703941 [NCBI, ExPASy, EBI, Israel, Japan]
Wen D., Corina K., Chow E.P., Miller S., Janmey P.A., Pepinsky R.B.;
"The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure.";
Biochemistry 35:9700-9709(1996).
[8]
DISULFIDE BOND.
DOI=10.1016/S0014-5793(96)01439-1; PubMed=9003812 [NCBI, ExPASy, EBI, Israel, Japan]
Allen P.G.;
"Functional consequences of disulfide bond formation in gelsolin.";
FEBS Lett. 401:89-94(1997).
[9]
PHOSPHORYLATION AT TYR-86; TYR-409; TYR-465; TYR-603 AND TYR-651.
PubMed=10210201 [NCBI, ExPASy, EBI, Israel, Japan]
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. 8:234-241(1999).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-503.
DOI=10.1038/364685a0; PubMed=8395021 [NCBI, ExPASy, EBI, Israel, Japan]
McLaughlin P.J., Gooch J.T., Mannherz H.-G., Weeds A.G.;
"Structure of gelsolin segment 1-actin complex and the mechanism of filament severing.";
Nature 364:685-692(1993).
[11]
STRUCTURE BY NMR OF 177-196.
PubMed=8599675 [NCBI, ExPASy, EBI, Israel, Japan]
Xian W., Vegners R., Janmey P.A., Braunlin W.H.;
"Spectroscopic studies of a phosphoinositide-binding peptide from gelsolin: behavior in solutions of mixed solvent and anionic micelles.";
Biophys. J. 69:2695-2702(1995).
[12]
VARIANT FAF ASN-214.
PubMed=2176481 [NCBI, ExPASy, EBI, Israel, Japan]
Ghiso J., Haltia M., Prelli F., Novello J., Frangione B.;
"Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type.";
Biochem. J. 272:827-830(1990).
[13]
VARIANTS FAF ASN-214 AND TYR-214.
DOI=10.1038/ng1092-157; PubMed=1338910 [NCBI, ExPASy, EBI, Israel, Japan]
de la Chapelle A., Tolvanen R., Boysen G., Santavy J., Bleeker-Wagemakers L., Maury C.P.J., Kere J.;
"Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187.";
Nat. Genet. 2:157-160(1992).
[14]
VARIANTS [LARGE SCALE ANALYSIS] LEU-22; ILE-201 AND ASN-611.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X04412; CAA28000.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017491; AAH17491.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026033; AAH26033.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A03011; FAHUP.
RefSeq NP_000168.1; -.
UniGene Hs.522373
3D structure databases
PDB
1C0F; X-ray; 2.40 A; S=53-176.[ExPASy / RCSB / EBI]
1C0G; X-ray; 2.00 A; S=53-176.[ExPASy / RCSB / EBI]
1D4X; X-ray; 1.75 A; G=52-177.[ExPASy / RCSB / EBI]
1DEJ; X-ray; 2.40 A; S=53-176.[ExPASy / RCSB / EBI]
1EQY; X-ray; 2.30 A; S=52-176.[ExPASy / RCSB / EBI]
1ESV; X-ray; 2.00 A; S=52-176.[ExPASy / RCSB / EBI]
1H1V; X-ray; 2.99 A; G=439-769.[ExPASy / RCSB / EBI]
1KCQ; X-ray; 1.65 A; A=185-288.[ExPASy / RCSB / EBI]
1MDU; X-ray; 2.20 A; A/D=52-176.[ExPASy / RCSB / EBI]
1NLV; X-ray; 1.80 A; G=52-176.[ExPASy / RCSB / EBI]
1NM1; X-ray; 1.80 A; G=52-176.[ExPASy / RCSB / EBI]
1NMD; X-ray; 1.90 A; G=52-176.[ExPASy / RCSB / EBI]
1P8X; X-ray; 2.00 A; A/B/C=439-782.[ExPASy / RCSB / EBI]
1P8Z; X-ray; 2.60 A; G=52-187.[ExPASy / RCSB / EBI]
1SOL; NMR; -; A=177-196.[ExPASy / RCSB / EBI]
1T44; X-ray; 2.00 A; G=55-183.[ExPASy / RCSB / EBI]
1YAG; X-ray; 1.90 A; G=52-176.[ExPASy / RCSB / EBI]
1YVN; X-ray; 2.10 A; G=52-176.[ExPASy / RCSB / EBI]
2FF3; X-ray; 2.00 A; A=51-179.[ExPASy / RCSB / EBI]
2FF6; X-ray; 2.05 A; G=51-179.[ExPASy / RCSB / EBI]
2FH1; X-ray; 1.55 A; A/B/C=439-782.[ExPASy / RCSB / EBI]
2FH2; X-ray; 2.50 A; A/B/C=439-782.[ExPASy / RCSB / EBI]
2FH3; X-ray; 2.87 A; A/B/C=439-782.[ExPASy / RCSB / EBI]
2FH4; X-ray; 3.00 A; A/B/C=439-782.[ExPASy / RCSB / EBI]
3CI5; X-ray; 1.70 A; G=52-176.[ExPASy / RCSB / EBI]
3CIP; X-ray; 1.60 A; G=52-176.[ExPASy / RCSB / EBI]
3CJB; X-ray; 3.21 A; G=52-176.[ExPASy / RCSB / EBI]
3CJC; X-ray; 3.90 A; G=52-176.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1C0F; -.
1C0G; -.
1D4X; -.
1DEJ; -.
1EQY; -.
1ESV; -.
1H1V; -.
1KCQ; -.
1MDU; -.
1NLV; -.
1NM1; -.
1NMD; -.
1P8X; -.
1P8Z; -.
1SOL; -.
1T44; -.
1YAG; -.
1YVN; -.
2FF3; -.
2FF6; -.
2FH1; -.
2FH2; -.
2FH3; -.
2FH4; -.
3CI5; -.
3CIP; -.
3CJB; -.
3CJC; -.
SMR P06396; 54-782.
ModBase P06396.
Protein-protein interaction databases
DIP DIP:2196N; -.
IntAct P06396; -.
PTM databases
PhosphoSite P06396; -.
2D gel databases
OGP P06396; -.
Organism-specific databases
H-InvDB HIX0008346; -.
HGNC HGNC:4620; GSN.
GenAtlas GSN.
HPA CAB010823; -.
CAB016728; -.
MIM 105120; phenotype. [NCBI / EBI]
137350; gene. [NCBI / EBI]
Orphanet 69; Amyloidosis.
85448; Familial amyloidosis, Finnish type.
PharmGKB PA29011; -.
GeneCards P06396.
Gene expression databases
ArrayExpress P06396; -.
CleanEx HS_GSN; -.
GermOnline ENSG00000148180; Homo sapiens.
Ontologies
GO
GO:0015629; Cellular component: actin cytoskeleton (traceable author statement from ProtInc).
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0005576; Cellular component: extracellular region (inferred from direct assay from UniProtKB).
GO:0005509; Molecular function: calcium ion binding (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0030041; Biological process: actin filament polymerization (inferred from direct assay from UniProtKB).
GO:0051014; Biological process: actin filament severing (inferred from direct assay from UniProtKB).
GO:0051016; Biological process: barbed-end actin filament capping (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR007122; Gelsolin.
IPR007123; Gelsoln.
Graphical view of domain structure.
PANTHER PTHR11977; Gelsolin; 1.
Pfam PF00626; Gelsolin; 6.
Pfam graphical view of domain structure.
PRINTS PR00597; GELSOLIN.
SMART SM00262; GEL; 6.
SMART graphical view of domain structure.
BLOCKS P06396.
ProtoNet P06396.
Other
SWISS-3DIMAGE P06396.
Proteomic databases
PeptideAtlas P06396; -.
Genome annotation databases
Ensembl ENSG00000148180; Homo sapiens. [Contig view]
GeneID 2934; -.
KEGG hsa:2934; -.
Phylogenomic databases
HOGENOM P06396; -.
HOVERGEN P06396; -.
Other
LinkHub P06396; -.
NextBio 11625; -.
SOURCE GSN; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Actin capping; Actin-binding; Alternative initiation; Amyloid; Calcium; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Phosphoprotein; Polymorphism; Repeat; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    27  27      
CHAIN   28   782  755     Gelsolin. PRO_0000036385
REPEAT   76   126  51     Gelsolin-like 1. 
REPEAT   198   238  41     Gelsolin-like 2. 
REPEAT   314   356  43     Gelsolin-like 3. 
REPEAT   453   504  52     Gelsolin-like 4. 
REPEAT   576   616  41     Gelsolin-like 5. 
REPEAT   679   721  43     Gelsolin-like 6. 
REGION   53   176  124     Actin-severing (Potential). 
REGION   123   126  4     Actin-actin interfilament contact point. 
REGION   162   169  8     Polyphosphoinositide binding (By similarity). 
REGION   188   196  9     Polyphosphoinositide binding (By similarity). 
REGION   434   782  349     Actin-binding, Ca-sensitive (Potential). 
MOD_RES   86    86        Phosphotyrosine; by SRC; in vitro. 
MOD_RES   409   409        Phosphotyrosine; by SRC; in vitro. 
MOD_RES   465   465        Phosphotyrosine; by SRC. 
MOD_RES   603   603        Phosphotyrosine; by SRC; in vitro. 
MOD_RES   651   651        Phosphotyrosine; by SRC; in vitro. 
DISULFID   215   228        In isoform 1. 
VAR_SEQ   1    51        Missing (in isoform 2). VSP_018959
VARIANT   22    22  1     S -> L (in a breast cancer sample; somatic mutation). VAR_036337 
VARIANT   129   129  1     A -> T (in dbSNP:rs2230287 [NCBI]). VAR_024690 [3D]
VARIANT   201   201  1     T -> I (in a breast cancer sample; somatic mutation). VAR_036338 
VARIANT   214   214  1     D -> N (in FAF). VAR_007718 
VARIANT   214   214  1     D -> Y (in FAF). VAR_007719 
VARIANT   611   611  1     S -> N (in a breast cancer sample; somatic mutation). VAR_036339 
VARIANT   668   668  1     R -> L (in dbSNP:rs9696578 [NCBI]). VAR_033958 
HELIX   57    61  5      
STRAND   64    74  11      
STRAND   77    80  4      
HELIX   83    85  3      
STRAND   88    90  3      
STRAND   94   102  9      
STRAND   108   116  9      
HELIX   122   138  17      
TURN   139   141  3      
STRAND   143   149  7      
HELIX   155   158  4      
STRAND   166   169  4      
STRAND   188   203  16      
HELIX   207   209  3      
STRAND   214   219  6      
STRAND   221   228  8      
HELIX   234   250  17      
STRAND   256   262  7      
HELIX   268   274  7      
STRAND   447   453  7      
STRAND   456   459  4      
HELIX   462   464  3      
STRAND   467   469  3      
STRAND   472   482  11      
STRAND   485   494  10      
HELIX   500   516  17      
TURN   517   519  3      
STRAND   521   527  7      
HELIX   533   537  5      
TURN   538   541  4      
STRAND   544   548  5      
TURN   553   555  3      
STRAND   562   570  9      
STRAND   576   581  6      
HELIX   585   587  3      
STRAND   592   597  6      
STRAND   602   606  5      
HELIX   612   624  13      
STRAND   630   633  4      
HELIX   639   644  6      
HELIX   655   658  4      
STRAND   668   671  4      
HELIX   690   692  3      
STRAND   697   702  6      
STRAND   707   711  5      
HELIX   717   733  17      
STRAND   744   748  5      
HELIX   754   757  4      
STRAND   760   762  3      
Sequence information
Length: 782 AA [This is the length of the unprocessed precursor] Molecular weight: 85698 Da [This is the MW of the unprocessed precursor] CRC64: 8CEBC52257A160F7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPHRPAPAL LCALSLALCA LSLPVRAATA SRGASQAGAP QGRVPEARPN SMVVEHPEFL 

        70         80         90        100        110        120 
KAGKEPGLQI WRVEKFDLVP VPTNLYGDFF TGDAYVILKT VQLRNGNLQY DLHYWLGNEC 

       130        140        150        160        170        180 
SQDESGAAAI FTVQLDDYLN GRAVQHREVQ GFESATFLGY FKSGLKYKKG GVASGFKHVV 

       190        200        210        220        230        240 
PNEVVVQRLF QVKGRRVVRA TEVPVSWESF NNGDCFILDL GNNIHQWCGS NSNRYERLKA 

       250        260        270        280        290        300 
TQVSKGIRDN ERSGRARVHV SEEGTEPEAM LQVLGPKPAL PAGTEDTAKE DAANRKLAKL 

       310        320        330        340        350        360 
YKVSNGAGTM SVSLVADENP FAQGALKSED CFILDHGKDG KIFVWKGKQA NTEERKAALK 

       370        380        390        400        410        420 
TASDFITKMD YPKQTQVSVL PEGGETPLFK QFFKNWRDPD QTDGLGLSYL SSHIANVERV 

       430        440        450        460        470        480 
PFDAATLHTS TAMAAQHGMD DDGTGQKQIW RIEGSNKVPV DPATYGQFYG GDSYIILYNY 

       490        500        510        520        530        540 
RHGGRQGQII YNWQGAQSTQ DEVAASAILT AQLDEELGGT PVQSRVVQGK EPAHLMSLFG 

       550        560        570        580        590        600 
GKPMIIYKGG TSREGGQTAP ASTRLFQVRA NSAGATRAVE VLPKAGALNS NDAFVLKTPS 

       610        620        630        640        650        660 
AAYLWVGTGA SEAEKTGAQE LLRVLRAQPV QVAEGSEPDG FWEALGGKAA YRTSPRLKDK 

       670        680        690        700        710        720 
KMDAHPPRLF ACSNKIGRFV IEEVPGELMQ EDLATDDVML LDTWDQVFVW VGKDSQEEEK 

       730        740        750        760        770        780 
TEALTSAKRY IETDPANRDR RTPITVVKQG FEPPSFVGWF LGWDDDYWSV DPLDRAMAEL 


AA 

P06396 in FASTA format

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