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P13020 (GELS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gelsolin
Alternative name(s):
Actin-depolymerizing factor
Short name=ADF
Brevin
Gene names
Name:Gsn
Synonyms:Gsb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

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. Ref.6

Subcellular location

Isoform 2: Cytoplasmcytoskeleton.

Isoform 1: Secreted.

Post-translational modification

Phosphorylated on tyrosine residues in vitro By similarity.

Sequence similarities

Belongs to the villin/gelsolin family.

Contains 6 gelsolin-like repeats.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCytoplasm
Cytoskeleton
Secreted
   Coding sequence diversityAlternative initiation
   DomainRepeat
Signal
   LigandActin-binding
Calcium
Metal-binding
   Molecular functionActin capping
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

actin filament polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament severing

Inferred from sequence or structural similarity. Source: UniProtKB

aging

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: Ensembl

cellular response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

cilium morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

oligodendrocyte development

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to folic acid

Inferred from electronic annotation. Source: Ensembl

tissue regeneration

Inferred from electronic annotation. Source: Ensembl

vesicle-mediated transport

Inferred from mutant phenotype PubMed 11514591. Source: MGI

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from direct assay PubMed 15294161. Source: MGI

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 23055941. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P13020-1)

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.
Isoform 2 (identifier: P13020-2)

Also known as: Cytoplasmic;

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.
Note: Initiator Met-1 is removed or contains a N-acetylalanine at position 1.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 780755Gelsolin
PRO_0000036387

Regions

Repeat74 – 12451Gelsolin-like 1
Repeat196 – 23641Gelsolin-like 2
Repeat312 – 35443Gelsolin-like 3
Repeat451 – 50252Gelsolin-like 4
Repeat574 – 61441Gelsolin-like 5
Repeat677 – 71943Gelsolin-like 6
Region51 – 174124Actin-severing Potential
Region121 – 1244Actin-actin interfilament contact point
Region160 – 1678Polyphosphoinositide binding By similarity
Region186 – 1949Polyphosphoinositide binding By similarity
Region432 – 780349Actin-binding, Ca-sensitive Potential

Sites

Metal binding4691Calcium 1; via carbonyl oxygen By similarity
Metal binding4701Calcium 1 By similarity
Metal binding5001Calcium 1 By similarity
Metal binding5491Calcium 1; via carbonyl oxygen By similarity
Metal binding5891Calcium 2 By similarity
Metal binding5891Calcium 2; via carbonyl oxygen By similarity
Metal binding5901Calcium 2 By similarity
Metal binding6121Calcium 2 By similarity
Metal binding6941Calcium 3; via carbonyl oxygen By similarity
Metal binding6951Calcium 3 By similarity
Metal binding7171Calcium 3 By similarity

Amino acid modifications

Modified residue841Phosphotyrosine By similarity
Modified residue4071Phosphotyrosine By similarity
Modified residue4631Phosphotyrosine By similarity
Modified residue5821N6-acetyllysine Ref.7
Modified residue6011Phosphotyrosine By similarity
Modified residue6491Phosphotyrosine By similarity
Disulfide bond213 ↔ 226In isoform 1 By similarity

Natural variations

Alternative sequence1 – 4949Missing in isoform 2.
VSP_018960

Experimental info

Sequence conflict262 – 2632GG → ET in AAA37677. Ref.1
Sequence conflict2741P → H in BAC41004. Ref.2
Sequence conflict2941R → K in AAA37677. Ref.1
Sequence conflict3161E → K in BAC41004. Ref.2
Sequence conflict3231A → P in AAA37677. Ref.1
Sequence conflict4231A → G in AAA37677. Ref.1
Sequence conflict6151G → A in AAA37677. Ref.1
Sequence conflict6381A → G in AAA37677. Ref.1
Sequence conflict6481A → S in AAA37677. Ref.1
Sequence conflict7631D → N in AAA37677. Ref.1

Secondary structure

................................................................... 780
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Secreted) (Plasma) [UniParc].

Last modified February 12, 2003. Version 3.
Checksum: AE94297BE457FF2D

FASTA78085,942
        10         20         30         40         50         60 
MAPYRSSLLC ALLLLALCAL SPSHAATTSR GRAQERAPQS RVSEARPSTM VVEHPEFLKA 

        70         80         90        100        110        120 
GKEPGLQIWR VEKFDLVPVP PNLYGDFFTG DAYVILKTVQ LRNGNLQYDL HYWLGNECSQ 

       130        140        150        160        170        180 
DESGAAAIFT VQLDDYLNGR AVQHREVQGF ESSTFSGYFK SGLKYKKGGV ASGFKHVVPN 

       190        200        210        220        230        240 
EVVVQRLFQV KGRRVVRATE VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ 

       250        260        270        280        290        300 
VSKGIRDNER SGRAQVHVSE EGGEPEAMLQ VLGPKPALPE GTEDTAKEDA ANRRLAKLYK 

       310        320        330        340        350        360 
VSNGAGSMSV SLVADENPFA QGALRSEDCF ILDHGRDGKI FVWKGKQANM EERKAALKTA 

       370        380        390        400        410        420 
SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT DGPGLGYLSS HIANVERVPF 

       430        440        450        460        470        480 
DAATLHTSTA MAAQHGMDDD GTGQKQIWRI EGSNKVPVDP ATYGQFYGGD SYIILYNYRH 

       490        500        510        520        530        540 
GGRQGQIIYN WQGAQSTQDE VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK 

       550        560        570        580        590        600 
PMIIYKGGTS RDGGQTAPAS IRLFQVRASS SGATRAVEVM PKSGALNSND AFVLKTPSAA 

       610        620        630        640        650        660 
YLWVGAGASE AEKTGAQELL KVLRSQHVQV EEGSEPDAFW EALGGKTAYR TSPRLKDKKM 

       670        680        690        700        710        720 
DAHPPRLFAC SNRIGRFVIE EVPGELMQED LATDDVMLLD TWDQVFVWVG KDSQEEEKTE 

       730        740        750        760        770        780 
ALTSAKRYIE TDPANRDRRT PITVVRQGFE PPSFVGWFLG WDDNYWSVDP LDRALAELAA 

« Hide

Isoform 2 (Cytoplasmic) [UniParc].

Checksum: 56F6A4964DF1CB04
Show »

FASTA73180,763

References

« Hide 'large scale' references
[1]"Cloning of murine gelsolin and its regulation during differentiation of embryonal carcinoma cells."
Dieffenbach C.W., Sengupta D.N., Krause D., Sawzak D., Silverman R.H.
J. Biol. Chem. 264:13281-13288(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Head and Spleen.
[3]"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: Mammary gland.
[4]Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 50-70 (ISOFORM 2), PROTEIN SEQUENCE OF 74-97; 146-160; 167-186; 254-293; 301-336; 359-366; 372-388; 396-445; 456-479; 529-546; 552-562; 583-621; 625-646; 667-673; 712-736 AND 739-746 (ISOFORMS 1/2), CLEAVAGE OF INITIATOR METHIONINE (ISOFORM 2), ACETYLATION AT MET-1 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
[5]"Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 51-73.
Tissue: Fibroblast.
[6]"Regulation of actin dynamics by protein kinase R control of gelsolin enforces basal innate immune defense."
Irving A.T., Wang D., Vasilevski O., Latchoumanin O., Kozer N., Clayton A.H., Szczepny A., Morimoto H., Xu D., Williams B.R., Sadler A.J.
Immunity 36:795-806(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF2AK2.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04953 mRNA. Translation: AAA37677.1.
AK076156 mRNA. Translation: BAC36223.1.
AK089934 mRNA. Translation: BAC41004.1.
AK143664 mRNA. Translation: BAE25485.1.
BC023143 mRNA. Translation: AAH23143.2.
CCDSCCDS15960.1. [P13020-1]
RefSeqNP_666232.2. NM_146120.4. [P13020-1]
UniGeneMm.21109.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NPHX-ray3.00A439-767[»]
4CBUX-ray1.30G50-174[»]
4CBWX-ray2.50G50-174[»]
4CBXX-ray2.20G50-174[»]
ProteinModelPortalP13020.
SMRP13020. Positions 48-780.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230683. 6 interactions.
IntActP13020. 7 interactions.
MINTMINT-1608422.

PTM databases

PhosphoSiteP13020.

2D gel databases

REPRODUCTION-2DPAGEP13020.

Proteomic databases

MaxQBP13020.
PaxDbP13020.
PRIDEP13020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028239; ENSMUSP00000028239; ENSMUSG00000026879. [P13020-1]
GeneID227753.
KEGGmmu:227753.
UCSCuc008jkc.2. mouse. [P13020-1]

Organism-specific databases

CTD2934.
MGIMGI:95851. Gsn.

Phylogenomic databases

eggNOGNOG304849.
GeneTreeENSGT00620000087675.
HOGENOMHOG000233630.
HOVERGENHBG004183.
InParanoidP13020.
KOK05768.
OMARIEKFDL.
OrthoDBEOG7288RJ.
PhylomeDBP13020.
TreeFamTF313468.

Gene expression databases

ArrayExpressP13020.
BgeeP13020.
CleanExMM_GSN.
GenevestigatorP13020.

Family and domain databases

Gene3D3.40.20.10. 6 hits.
InterProIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERPTHR11977. PTHR11977. 1 hit.
PfamPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSPR00597. GELSOLIN.
SMARTSM00262. GEL. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGSN. mouse.
EvolutionaryTraceP13020.
NextBio378824.
PROP13020.
SOURCESearch...

Entry information

Entry nameGELS_MOUSE
AccessionPrimary (citable) accession number: P13020
Secondary accession number(s): Q3UPB1, Q8R590
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 12, 2003
Last modified: July 9, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot