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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)DescriptionActionsGraphical viewLength
Metal bindingi467Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi468Calcium 1By similarity1
Metal bindingi498Calcium 1By similarity1
Metal bindingi547Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi587Calcium 2By similarity1
Metal bindingi587Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi588Calcium 2By similarity1
Metal bindingi610Calcium 2By similarity1
Metal bindingi692Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi693Calcium 3By similarity1
Metal bindingi715Calcium 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

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
Proteomesi
  • UP000000539 Componenti: Unplaced

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 – 23Sequence analysisAdd BLAST23
ChainiPRO_000003639224 – 778GelsolinAdd BLAST755

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactor.
IntActiO93510. 1 interactor.
STRINGi9031.ENSGALP00000002197.

Structurei

3D structure databases

ProteinModelPortaliO93510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati72 – 122Gelsolin-like 1Add BLAST51
Repeati194 – 234Gelsolin-like 2Add BLAST41
Repeati310 – 352Gelsolin-like 3Add BLAST43
Repeati449 – 500Gelsolin-like 4Add BLAST52
Repeati572 – 612Gelsolin-like 5Add BLAST41
Repeati675 – 717Gelsolin-like 6Add BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 172Actin-severingSequence analysisAdd BLAST124
Regioni119 – 122Actin-actin interfilament contact point4
Regioni158 – 165Polyphosphoinositide bindingBy similarity8
Regioni184 – 192Polyphosphoinositide bindingBy similarity9
Regioni430 – 778Actin-binding, Ca-sensitiveSequence analysisAdd BLAST349

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

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676048. 1 interactor.
IntActiO93510. 1 interactor.
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

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiO93510.
KOiK05768.
PhylomeDBiO93510.

Miscellaneous databases

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...

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: October 5, 2016
This is version 98 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

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.