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Protein

Gelsolin

Gene

Gsn

Organism
Mus musculus (Mouse)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi469Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi470Calcium 1By similarity1
Metal bindingi500Calcium 1By similarity1
Metal bindingi549Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi589Calcium 2By similarity1
Metal bindingi589Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi590Calcium 2By similarity1
Metal bindingi612Calcium 2By similarity1
Metal bindingi694Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi695Calcium 3By similarity1
Metal bindingi717Calcium 3By similarity1

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-MMU-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-MMU-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Gelsolin
Alternative name(s):
Actin-depolymerizing factor
Short name:
ADF
Brevin
Gene namesi
Name:Gsn
Synonyms:Gsb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:95851. Gsn.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000003638726 – 780GelsolinAdd BLAST755

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei84PhosphotyrosineBy similarity1
Disulfide bondi213 ↔ 226In isoform 1By similarity
Modified residuei407PhosphotyrosineBy similarity1
Modified residuei463PhosphotyrosineBy similarity1
Modified residuei582N6-acetyllysineCombined sources1
Modified residuei601PhosphotyrosineBy similarity1
Modified residuei649PhosphotyrosineBy similarity1
Modified residuei740PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylated on tyrosine residues in vitro.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP13020.
PaxDbiP13020.
PeptideAtlasiP13020.
PRIDEiP13020.

2D gel databases

REPRODUCTION-2DPAGEP13020.

PTM databases

iPTMnetiP13020.
PhosphoSitePlusiP13020.
SwissPalmiP13020.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026879.
CleanExiMM_GSN.
ExpressionAtlasiP13020. baseline and differential.
GenevisibleiP13020. MM.

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 similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi230683. 6 interactors.
DIPiDIP-31941N.
IntActiP13020. 8 interactors.
MINTiMINT-1608422.
STRINGi10090.ENSMUSP00000028239.

Structurei

Secondary structure

1780
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi57 – 59Combined sources3
Beta strandi62 – 72Combined sources11
Beta strandi75 – 78Combined sources4
Helixi81 – 83Combined sources3
Beta strandi86 – 88Combined sources3
Beta strandi92 – 100Combined sources9
Beta strandi106 – 114Combined sources9
Helixi120 – 136Combined sources17
Turni137 – 139Combined sources3
Beta strandi141 – 147Combined sources7
Helixi153 – 156Combined sources4
Beta strandi164 – 167Combined sources4
Beta strandi445 – 451Combined sources7
Beta strandi454 – 457Combined sources4
Helixi460 – 462Combined sources3
Beta strandi465 – 467Combined sources3
Beta strandi470 – 477Combined sources8
Beta strandi486 – 492Combined sources7
Helixi498 – 514Combined sources17
Turni515 – 517Combined sources3
Beta strandi519 – 525Combined sources7
Helixi531 – 535Combined sources5
Turni536 – 539Combined sources4
Beta strandi542 – 546Combined sources5
Beta strandi551 – 553Combined sources3
Beta strandi560 – 568Combined sources9
Beta strandi570 – 572Combined sources3
Beta strandi574 – 579Combined sources6
Helixi583 – 585Combined sources3
Beta strandi590 – 595Combined sources6
Beta strandi600 – 604Combined sources5
Helixi610 – 623Combined sources14
Beta strandi627 – 631Combined sources5
Helixi637 – 643Combined sources7
Helixi653 – 656Combined sources4
Helixi660 – 662Combined sources3
Beta strandi666 – 671Combined sources6
Beta strandi674 – 676Combined sources3
Beta strandi678 – 681Combined sources4
Helixi688 – 690Combined sources3
Beta strandi695 – 700Combined sources6
Beta strandi705 – 709Combined sources5
Helixi715 – 729Combined sources15
Turni733 – 735Combined sources3
Beta strandi742 – 746Combined sources5
Helixi752 – 755Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NPHX-ray3.00A439-767[»]
4CBUX-ray1.30G50-174[»]
4CBWX-ray2.50G50-174[»]
4CBXX-ray2.20G50-174[»]
ProteinModelPortaliP13020.
SMRiP13020.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13020.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati74 – 124Gelsolin-like 1Add BLAST51
Repeati196 – 236Gelsolin-like 2Add BLAST41
Repeati312 – 354Gelsolin-like 3Add BLAST43
Repeati451 – 502Gelsolin-like 4Add BLAST52
Repeati574 – 614Gelsolin-like 5Add BLAST41
Repeati677 – 719Gelsolin-like 6Add BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni51 – 174Actin-severingSequence analysisAdd BLAST124
Regioni121 – 124Actin-actin interfilament contact point4
Regioni160 – 167Polyphosphoinositide bindingBy similarity8
Regioni186 – 194Polyphosphoinositide bindingBy similarity9
Regioni432 – 780Actin-binding, Ca-sensitiveSequence analysisAdd BLAST349

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiP13020.
KOiK05768.
OMAiANMEERK.
OrthoDBiEOG091G05SC.
PhylomeDBiP13020.
TreeFamiTF313468.

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: P13020-1) [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
MAPYRSSLLC ALLLLALCAL SPSHAATTSR GRAQERAPQS RVSEARPSTM
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
ESSTFSGYFK SGLKYKKGGV ASGFKHVVPN EVVVQRLFQV KGRRVVRATE
210 220 230 240 250
VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ VSKGIRDNER
260 270 280 290 300
SGRAQVHVSE EGGEPEAMLQ VLGPKPALPE GTEDTAKEDA ANRRLAKLYK
310 320 330 340 350
VSNGAGSMSV SLVADENPFA QGALRSEDCF ILDHGRDGKI FVWKGKQANM
360 370 380 390 400
EERKAALKTA SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT
410 420 430 440 450
DGPGLGYLSS HIANVERVPF DAATLHTSTA MAAQHGMDDD GTGQKQIWRI
460 470 480 490 500
EGSNKVPVDP ATYGQFYGGD SYIILYNYRH GGRQGQIIYN WQGAQSTQDE
510 520 530 540 550
VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK PMIIYKGGTS
560 570 580 590 600
RDGGQTAPAS IRLFQVRASS SGATRAVEVM PKSGALNSND AFVLKTPSAA
610 620 630 640 650
YLWVGAGASE AEKTGAQELL KVLRSQHVQV EEGSEPDAFW 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 WDDNYWSVDP LDRALAELAA
Length:780
Mass (Da):85,942
Last modified:February 12, 2003 - v3
Checksum:iAE94297BE457FF2D
GO
Isoform 2 (identifier: P13020-2) [UniParc]FASTAAdd to basket
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-acetylmethionine at position 1.1 Publication
Show »
Length:731
Mass (Da):80,763
Checksum:i56F6A4964DF1CB04
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti262 – 263GG → ET in AAA37677 (PubMed:2546951).Curated2
Sequence conflicti274P → H in BAC41004 (PubMed:16141072).Curated1
Sequence conflicti294R → K in AAA37677 (PubMed:2546951).Curated1
Sequence conflicti316E → K in BAC41004 (PubMed:16141072).Curated1
Sequence conflicti323A → P in AAA37677 (PubMed:2546951).Curated1
Sequence conflicti423A → G in AAA37677 (PubMed:2546951).Curated1
Sequence conflicti615G → A in AAA37677 (PubMed:2546951).Curated1
Sequence conflicti638A → G in AAA37677 (PubMed:2546951).Curated1
Sequence conflicti648A → S in AAA37677 (PubMed:2546951).Curated1
Sequence conflicti763D → N in AAA37677 (PubMed:2546951).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0189601 – 49Missing in isoform 2. 2 PublicationsAdd BLAST49

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15960.1. [P13020-1]
CCDS79785.1. [P13020-2]
RefSeqiNP_666232.2. NM_146120.4. [P13020-1]
UniGeneiMm.21109.
Mm.443.

Genome annotation databases

EnsembliENSMUST00000028239; ENSMUSP00000028239; ENSMUSG00000026879. [P13020-1]
ENSMUST00000201185; ENSMUSP00000144561; ENSMUSG00000026879. [P13020-2]
GeneIDi227753.
KEGGimmu:227753.
UCSCiuc008jkc.2. mouse. [P13020-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15960.1. [P13020-1]
CCDS79785.1. [P13020-2]
RefSeqiNP_666232.2. NM_146120.4. [P13020-1]
UniGeneiMm.21109.
Mm.443.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NPHX-ray3.00A439-767[»]
4CBUX-ray1.30G50-174[»]
4CBWX-ray2.50G50-174[»]
4CBXX-ray2.20G50-174[»]
ProteinModelPortaliP13020.
SMRiP13020.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230683. 6 interactors.
DIPiDIP-31941N.
IntActiP13020. 8 interactors.
MINTiMINT-1608422.
STRINGi10090.ENSMUSP00000028239.

PTM databases

iPTMnetiP13020.
PhosphoSitePlusiP13020.
SwissPalmiP13020.

2D gel databases

REPRODUCTION-2DPAGEP13020.

Proteomic databases

MaxQBiP13020.
PaxDbiP13020.
PeptideAtlasiP13020.
PRIDEiP13020.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028239; ENSMUSP00000028239; ENSMUSG00000026879. [P13020-1]
ENSMUST00000201185; ENSMUSP00000144561; ENSMUSG00000026879. [P13020-2]
GeneIDi227753.
KEGGimmu:227753.
UCSCiuc008jkc.2. mouse. [P13020-1]

Organism-specific databases

CTDi2934.
MGIiMGI:95851. Gsn.

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiP13020.
KOiK05768.
OMAiANMEERK.
OrthoDBiEOG091G05SC.
PhylomeDBiP13020.
TreeFamiTF313468.

Enzyme and pathway databases

ReactomeiR-MMU-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiGsn. mouse.
EvolutionaryTraceiP13020.
PROiP13020.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026879.
CleanExiMM_GSN.
ExpressionAtlasiP13020. baseline and differential.
GenevisibleiP13020. MM.

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...

Entry informationi

Entry nameiGELS_MOUSE
AccessioniPrimary (citable) accession number: P13020
Secondary accession number(s): Q3UPB1, Q8R590
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 12, 2003
Last modified: November 30, 2016
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.