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O93510 (GELS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Homogenin
Gene names
Name:GSN
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subunit structure

Binds to actin and to fibronectin.

Subcellular location

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

Tissue specificity

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

Domain

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 similarities

Belongs to the villin/gelsolin family.

Contains 6 gelsolin-like repeats.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCytoplasm
Cytoskeleton
Secreted
   DomainRepeat
Signal
   LigandActin-binding
Calcium
Metal-binding
   Molecular functionActin capping
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

cilium morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 778755Gelsolin
PRO_0000036392

Regions

Repeat72 – 12251Gelsolin-like 1
Repeat194 – 23441Gelsolin-like 2
Repeat310 – 35243Gelsolin-like 3
Repeat449 – 50052Gelsolin-like 4
Repeat572 – 61241Gelsolin-like 5
Repeat675 – 71743Gelsolin-like 6
Region49 – 172124Actin-severing Potential
Region119 – 1224Actin-actin interfilament contact point
Region158 – 1658Polyphosphoinositide binding By similarity
Region184 – 1929Polyphosphoinositide binding By similarity
Region430 – 778349Actin-binding, Ca-sensitive Potential

Sites

Metal binding4671Calcium 1; via carbonyl oxygen By similarity
Metal binding4681Calcium 1 By similarity
Metal binding4981Calcium 1 By similarity
Metal binding5471Calcium 1; via carbonyl oxygen By similarity
Metal binding5871Calcium 2 By similarity
Metal binding5871Calcium 2; via carbonyl oxygen By similarity
Metal binding5881Calcium 2 By similarity
Metal binding6101Calcium 2 By similarity
Metal binding6921Calcium 3; via carbonyl oxygen By similarity
Metal binding6931Calcium 3 By similarity
Metal binding7151Calcium 3 By similarity

Amino acid modifications

Disulfide bond211 ↔ 224 By similarity

Sequences

Sequence LengthMass (Da)Tools
O93510 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 7C8DFB0336B068FD

FASTA77885,832
        10         20         30         40         50         60 
MGKQGFGYIF LTIFCTMALK LNCVSSVSVA GLGYVVTAAV VLSAVPVSMV EHAEFSKAGK 

        70         80         90        100        110        120 
EPGLQIWRIE KFDLVPVPKN LYGDFFTGDS YLVLNTIRQR SGNLQYDLHF WLGDESSQDE 

       130        140        150        160        170        180 
RGAAAIFTVQ MDDYLQGKAV QHREVQGHES STFLGYFKSG IKYKAGGVAS GFRHVVPNEV 

       190        200        210        220        230        240 
TVQRLLQVKG RRTVRATEVP VSWESFNTGD CFILDLGSNI YQWCGSNSNR QERLKATVLA 

       250        260        270        280        290        300 
KGIRDNEKNG RAKVFVSEEG AEREEMLQVL GPKPSLPQGA SDDTKTDTAN RKLAKLYKVS 

       310        320        330        340        350        360 
NGAGNMAVSL VADENPFSQA ALNTEDCFIL DHGTDGKIFV WKGRSANSDE RKAALKTATD 

       370        380        390        400        410        420 
FIDKMGYPKH TQVQVLPESG ETPLFKQFFK NWRDKDQTEG LGEAYISGHV AKIEKVPFDA 

       430        440        450        460        470        480 
ATLHTSRAMA AQHGMEDDGS GKKQIWRIEG SEKVPVDPAT YGQFYGGDSY IILYDYRHAG 

       490        500        510        520        530        540 
KQGQIIYTWQ GAHSTQDEIA TSAFLTVQLD EELGGSPVQK RVVQGKEPPH LMSMFGGKPL 

       550        560        570        580        590        600 
IVYKGGTSRE GGQTTPAQTR LFQVRSSTSG ATRAVELDPA ASQLNSNDAF VLKTPSAAYL 

       610        620        630        640        650        660 
WVGRGSNSAE LSGAQELLKV LGARPVQVSE GREPDNFWVA LGGKAPYRTS PRLKDKKMDA 

       670        680        690        700        710        720 
YPPRLFACSN KSGRFTIEEV PGDLTQDDLA TDDVMILDTW DQVFVWIGKD AQEEEKTEAL 

       730        740        750        760        770 
KSAKRYIETD PASRDKRTPV TLVKQGLEPP TFSGWFLGWD DDYWSVDPLQ RAMADVDV 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF042795 mRNA. Translation: AAC62928.1.
RefSeqNP_990265.1. NM_204934.1.
UniGeneGga.4451.

3D structure databases

ProteinModelPortalO93510.
SMRO93510. Positions 50-776.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676048. 1 interaction.
IntActO93510. 1 interaction.
STRING9031.ENSGALP00000002197.

Proteomic databases

PaxDbO93510.
PRIDEO93510.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID395774.
KEGGgga:395774.

Organism-specific databases

CTD2934.

Phylogenomic databases

eggNOGNOG304849.
HOGENOMHOG000233630.
HOVERGENHBG004183.
InParanoidO93510.
KOK05768.
PhylomeDBO93510.

Family and domain databases

InterProIPR007123. 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

NextBio20815842.
PROO93510.

Entry information

Entry nameGELS_CHICK
AccessionPrimary (citable) accession number: O93510
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 84 of the entry and version 1 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