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Protein

Gelsolin

Gene

Gsn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi469 – 4691Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi470 – 4701Calcium 1By similarity
Metal bindingi500 – 5001Calcium 1By similarity
Metal bindingi549 – 5491Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi589 – 5891Calcium 2By similarity
Metal bindingi589 – 5891Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi590 – 5901Calcium 2By similarity
Metal bindingi612 – 6121Calcium 2By similarity
Metal bindingi694 – 6941Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi695 – 6951Calcium 3By similarity
Metal bindingi717 – 7171Calcium 3By similarity

GO - Molecular functioni

  1. actin binding Source: RGD
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. actin filament polymerization Source: UniProtKB
  2. actin filament severing Source: UniProtKB
  3. actin nucleation Source: InterPro
  4. actin polymerization or depolymerization Source: RGD
  5. aging Source: RGD
  6. apoptotic process Source: RGD
  7. barbed-end actin filament capping Source: InterPro
  8. cellular response to cadmium ion Source: RGD
  9. cilium morphogenesis Source: UniProtKB
  10. oligodendrocyte development Source: RGD
  11. phosphatidylinositol-mediated signaling Source: RGD
  12. regulation of cell adhesion Source: RGD
  13. response to ethanol Source: RGD
  14. response to folic acid Source: RGD
  15. tissue regeneration Source: RGD
  16. vesicle-mediated transport Source: Ensembl
  17. wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_295384. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_345709. Amyloids.

Names & Taxonomyi

Protein namesi
Recommended name:
Gelsolin
Alternative name(s):
Actin-depolymerizing factor
Short name:
ADF
Brevin
Gene namesi
Name:Gsn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi1303089. Gsn.

Subcellular locationi

Isoform 1 :
  1. Secreted By similarity
Isoform 2 :
  1. Cytoplasmcytoskeleton By similarity

  2. Note: A cytoplasmic form may also exist.By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: RGD
  2. blood microparticle Source: Ensembl
  3. cytosol Source: UniProtKB
  4. extracellular region Source: UniProtKB
  5. extracellular space Source: RGD
  6. extracellular vesicular exosome Source: Ensembl
  7. focal adhesion Source: Ensembl
  8. lamellipodium Source: Ensembl
  9. perinuclear region of cytoplasm Source: RGD
  10. protein complex Source: RGD
  11. ruffle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 780755GelsolinPRO_0000288477Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841PhosphotyrosineBy similarity
Disulfide bondi213 ↔ 226By similarity
Modified residuei407 – 4071PhosphotyrosineBy similarity
Modified residuei463 – 4631PhosphotyrosineBy similarity
Modified residuei582 – 5821N6-acetyllysineBy similarity
Modified residuei601 – 6011PhosphotyrosineBy similarity
Modified residuei649 – 6491PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues in vitro.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ68FP1.
PRIDEiQ68FP1.

PTM databases

PhosphoSiteiQ68FP1.

Expressioni

Gene expression databases

GenevestigatoriQ68FP1.

Interactioni

Subunit structurei

Binds to actin and to fibronectin. Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X (By similarity). Interacts with the inactive form of EIF2AK2/PKR (By similarity).By similarity

Protein-protein interaction databases

BioGridi255439. 2 interactions.
IntActiQ68FP1. 1 interaction.
STRINGi10116.ENSRNOP00000025857.

Structurei

3D structure databases

ProteinModelPortaliQ68FP1.
SMRiQ68FP1. Positions 51-780.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati74 – 12451Gelsolin-like 1Add
BLAST
Repeati196 – 23641Gelsolin-like 2Add
BLAST
Repeati312 – 35443Gelsolin-like 3Add
BLAST
Repeati451 – 50252Gelsolin-like 4Add
BLAST
Repeati574 – 61441Gelsolin-like 5Add
BLAST
Repeati677 – 71943Gelsolin-like 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 174124Actin-severingSequence AnalysisAdd
BLAST
Regioni121 – 1244Actin-actin interfilament contact pointBy similarity
Regioni160 – 1678Polyphosphoinositide bindingBy similarity
Regioni186 – 1949Polyphosphoinositide bindingBy similarity
Regioni432 – 780349Actin-binding, Ca-sensitiveSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated
Contains 6 gelsolin-like repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG304849.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiQ68FP1.
KOiK05768.
OMAiANMEERK.
OrthoDBiEOG7288RJ.
PhylomeDBiQ68FP1.

Family and domain databases

Gene3Di3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR030004. Gelsolin.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF29. PTHR11977:SF29. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q68FP1-1) [UniParc]FASTAAdd to basket

Also known as: Secreted, Plasma

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPYCSSLRS ALLVLALCAL SPSHAATASR GRAQERAPQS RVSETRPSTM
60 70 80 90 100
VVEHPEFLKA GKEPGLQIWR VEKFDLVPVP PNLYGDFFTG DAYVILKTVQ
110 120 130 140 150
LRNGNLQYDL HYWLGNECSQ DESGAAAIFT VQLDDYLNGR AVQHREVQGF
160 170 180 190 200
ESSTFQGYFK SGLKYKKGGV ASGFKHVVPN EVVVQRLFQV KGRRVVRATE
210 220 230 240 250
VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ VSKGIRDNER
260 270 280 290 300
SGRAQVHVSE EGSEPEAMLQ VLGPKPDLPQ GTEDTAKEDA ANRRLAKLYK
310 320 330 340 350
VSNSGGSMSV SLVADENPFA QSALRSEDCF ILDHGRDGKI FVWKGKQANM
360 370 380 390 400
DERKAALKTA SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT
410 420 430 440 450
DGPGLSYLSS HIANVERVPF DAATLHTSTA MAAQHGMDDD GTGQKQIWRI
460 470 480 490 500
EGSNKVLVDP ATYGQFYGGD SYIILYNYRH GGRQGQIIYN WQGAQSTQDE
510 520 530 540 550
VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK PMIIYKGGTS
560 570 580 590 600
RDGGQTTPAS TRLFQVRASS SGATRAVEVM PKAGALNSND AFVLKTPSAA
610 620 630 640 650
YLWVGTGASD AEKTGALELL KVLRAQHVQV EEGSEPDGFW EALGGKTAYR
660 670 680 690 700
TSPRLKDKKM DAHPPRLFAC SNRIGRFVIE EVPGELMQED LATDDVMLLD
710 720 730 740 750
TWDQVFVWVG KDSQEEEKTE ALTSAKRYIE TDPANRDRRT PITVVRQGFE
760 770 780
PPSFVGWFLG WDDDYWSVDP LDRALAELAA
Length:780
Mass (Da):86,068
Last modified:October 11, 2004 - v1
Checksum:iE9B6A20C5A80D0E8
GO
Isoform 2 (identifier: Q68FP1-2) [UniParc]FASTAAdd to basket

Also known as: Cytoplasmic

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Show »
Length:731
Mass (Da):80,929
Checksum:i2AD1D7C83C98DFE0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949Missing in isoform 2. CuratedVSP_036722Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079472 mRNA. Translation: AAH79472.1.
RefSeqiNP_001004080.1. NM_001004080.1. [Q68FP1-1]
XP_006234102.1. XM_006234040.1. [Q68FP1-2]
UniGeneiRn.103770.

Genome annotation databases

EnsembliENSRNOT00000025857; ENSRNOP00000025857; ENSRNOG00000018991. [Q68FP1-1]
GeneIDi296654.
KEGGirno:296654.
UCSCiRGD:1303089. rat. [Q68FP1-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079472 mRNA. Translation: AAH79472.1.
RefSeqiNP_001004080.1. NM_001004080.1. [Q68FP1-1]
XP_006234102.1. XM_006234040.1. [Q68FP1-2]
UniGeneiRn.103770.

3D structure databases

ProteinModelPortaliQ68FP1.
SMRiQ68FP1. Positions 51-780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi255439. 2 interactions.
IntActiQ68FP1. 1 interaction.
STRINGi10116.ENSRNOP00000025857.

PTM databases

PhosphoSiteiQ68FP1.

Proteomic databases

PaxDbiQ68FP1.
PRIDEiQ68FP1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025857; ENSRNOP00000025857; ENSRNOG00000018991. [Q68FP1-1]
GeneIDi296654.
KEGGirno:296654.
UCSCiRGD:1303089. rat. [Q68FP1-1]

Organism-specific databases

CTDi2934.
RGDi1303089. Gsn.

Phylogenomic databases

eggNOGiNOG304849.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiQ68FP1.
KOiK05768.
OMAiANMEERK.
OrthoDBiEOG7288RJ.
PhylomeDBiQ68FP1.

Enzyme and pathway databases

ReactomeiREACT_295384. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_345709. Amyloids.

Miscellaneous databases

NextBioi641599.
PROiQ68FP1.

Gene expression databases

GenevestigatoriQ68FP1.

Family and domain databases

Gene3Di3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR030004. Gelsolin.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF29. PTHR11977:SF29. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  2. Lubec G., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 301-325; 396-417; 583-595 AND 614-621, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.

Entry informationi

Entry nameiGELS_RAT
AccessioniPrimary (citable) accession number: Q68FP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2004
Last modified: April 1, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.