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Protein

Gelsolin

Gene

GSN

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 bindingi467 – 4671Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi468 – 4681Calcium 1By similarity
Metal bindingi498 – 4981Calcium 1By similarity
Metal bindingi547 – 5471Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi587 – 5871Calcium 2By similarity
Metal bindingi587 – 5871Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi588 – 5881Calcium 2By similarity
Metal bindingi610 – 6101Calcium 2By similarity
Metal bindingi692 – 6921Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi693 – 6931Calcium 3By similarity
Metal bindingi715 – 7151Calcium 3By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. actin filament severing Source: InterPro
  2. actin nucleation Source: InterPro
  3. barbed-end actin filament capping Source: InterPro
  4. cilium morphogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Gelsolin
Alternative name(s):
Actin-depolymerizing factor
Short name:
ADF
Brevin
Homogenin
Gene namesi
Name:GSN
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Secreted By similarity. Cytoplasmcytoskeleton By similarity
Note: A cytoplasmic form may also exist.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-SubCell
  3. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 778755GelsolinPRO_0000036392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi211 ↔ 224By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO93510.
PRIDEiO93510.

Expressioni

Tissue specificityi

Highly expressed in homogene cells of the basilar papilla. Also detected in subcutaneous layer of the skin.1 Publication

Interactioni

Subunit structurei

Binds to actin and to fibronectin.Curated

Protein-protein interaction databases

BioGridi676048. 1 interaction.
IntActiO93510. 1 interaction.
STRINGi9031.ENSGALP00000002197.

Structurei

3D structure databases

ProteinModelPortaliO93510.
SMRiO93510. Positions 50-776.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati72 – 12251Gelsolin-like 1Add
BLAST
Repeati194 – 23441Gelsolin-like 2Add
BLAST
Repeati310 – 35243Gelsolin-like 3Add
BLAST
Repeati449 – 50052Gelsolin-like 4Add
BLAST
Repeati572 – 61241Gelsolin-like 5Add
BLAST
Repeati675 – 71743Gelsolin-like 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 172124Actin-severingSequence AnalysisAdd
BLAST
Regioni119 – 1224Actin-actin interfilament contact point
Regioni158 – 1658Polyphosphoinositide bindingBy similarity
Regioni184 – 1929Polyphosphoinositide bindingBy similarity
Regioni430 – 778349Actin-binding, Ca-sensitiveSequence AnalysisAdd
BLAST

Domaini

Comprises six structurally related domains, in a calcium-free environment, pack together to form a compact globular structure in which the putative actin-binding sequences are not sufficiently exposed to enable binding to occur. Binding calcium may release the connections that join the N- and C-terminal halves of gelsolin, enabling each half to bind actin relatively independently. The severing and capping properties of gelsolin are inhibited by binding polyphosphoinositides.

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG304849.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiO93510.
KOiK05768.
PhylomeDBiO93510.

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]

Sequencei

Sequence statusi: Complete.

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

O93510-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKQGFGYIF LTIFCTMALK LNCVSSVSVA GLGYVVTAAV VLSAVPVSMV
60 70 80 90 100
EHAEFSKAGK EPGLQIWRIE KFDLVPVPKN LYGDFFTGDS YLVLNTIRQR
110 120 130 140 150
SGNLQYDLHF WLGDESSQDE RGAAAIFTVQ MDDYLQGKAV QHREVQGHES
160 170 180 190 200
STFLGYFKSG IKYKAGGVAS GFRHVVPNEV TVQRLLQVKG RRTVRATEVP
210 220 230 240 250
VSWESFNTGD CFILDLGSNI YQWCGSNSNR QERLKATVLA KGIRDNEKNG
260 270 280 290 300
RAKVFVSEEG AEREEMLQVL GPKPSLPQGA SDDTKTDTAN RKLAKLYKVS
310 320 330 340 350
NGAGNMAVSL VADENPFSQA ALNTEDCFIL DHGTDGKIFV WKGRSANSDE
360 370 380 390 400
RKAALKTATD FIDKMGYPKH TQVQVLPESG ETPLFKQFFK NWRDKDQTEG
410 420 430 440 450
LGEAYISGHV AKIEKVPFDA ATLHTSRAMA AQHGMEDDGS GKKQIWRIEG
460 470 480 490 500
SEKVPVDPAT YGQFYGGDSY IILYDYRHAG KQGQIIYTWQ GAHSTQDEIA
510 520 530 540 550
TSAFLTVQLD EELGGSPVQK RVVQGKEPPH LMSMFGGKPL IVYKGGTSRE
560 570 580 590 600
GGQTTPAQTR LFQVRSSTSG ATRAVELDPA ASQLNSNDAF VLKTPSAAYL
610 620 630 640 650
WVGRGSNSAE LSGAQELLKV LGARPVQVSE GREPDNFWVA LGGKAPYRTS
660 670 680 690 700
PRLKDKKMDA YPPRLFACSN KSGRFTIEEV PGDLTQDDLA TDDVMILDTW
710 720 730 740 750
DQVFVWIGKD AQEEEKTEAL KSAKRYIETD PASRDKRTPV TLVKQGLEPP
760 770
TFSGWFLGWD DDYWSVDPLQ RAMADVDV
Length:778
Mass (Da):85,832
Last modified:November 1, 1998 - v1
Checksum:i7C8DFB0336B068FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042795 mRNA. Translation: AAC62928.1.
RefSeqiNP_990265.1. NM_204934.1.
UniGeneiGga.4451.

Genome annotation databases

GeneIDi395774.
KEGGigga:395774.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042795 mRNA. Translation: AAC62928.1.
RefSeqiNP_990265.1. NM_204934.1.
UniGeneiGga.4451.

3D structure databases

ProteinModelPortaliO93510.
SMRiO93510. Positions 50-776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676048. 1 interaction.
IntActiO93510. 1 interaction.
STRINGi9031.ENSGALP00000002197.

Proteomic databases

PaxDbiO93510.
PRIDEiO93510.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi395774.
KEGGigga:395774.

Organism-specific databases

CTDi2934.

Phylogenomic databases

eggNOGiNOG304849.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiO93510.
KOiK05768.
PhylomeDBiO93510.

Miscellaneous databases

NextBioi20815842.
PROiO93510.

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

  1. "Molecular markers for cell types of the inner ear and candidate genes for hearing disorders."
    Heller S., Sheane C.A., Javed Z., Hudspeth A.J.
    Proc. Natl. Acad. Sci. U.S.A. 95:11400-11405(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: White leghorn.
    Tissue: Basilar papilla.

Entry informationi

Entry nameiGELS_CHICK
AccessioniPrimary (citable) accession number: O93510
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: November 1, 1998
Last modified: March 4, 2015
This is version 91 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, 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.