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Protein

Gelsolin, cytoplasmic

Gene
N/A
Organism
Halocynthia roretzi (Sea squirt) (Cynthia roretzi)
Status
Reviewed-Annotation score: Annotation score: 3 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi421Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi422Calcium 1By similarity1
Metal bindingi449Calcium 1By similarity1
Metal bindingi499Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi539Calcium 2By similarity1
Metal bindingi539Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi540Calcium 2By similarity1
Metal bindingi562Calcium 2By similarity1
Metal bindingi642Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi665Calcium 3By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Gelsolin, cytoplasmic
Alternative name(s):
Actin-depolymerizing factor
Short name:
ADF
Ascidian gelsolin
OrganismiHalocynthia roretzi (Sea squirt) (Cynthia roretzi)
Taxonomic identifieri7729 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataTunicataAscidiaceaStolidobranchiaPyuridaeHalocynthia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002187251 – 715Gelsolin, cytoplasmicAdd BLAST715

Expressioni

Tissue specificityi

Predominantly in the body wall muscle, but expression is not restricted to muscle cells.

Inductioni

Interaction with actin is suppressed by PIP2.

Structurei

3D structure databases

ProteinModelPortaliO61270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati24 – 75Gelsolin-like 1Add BLAST52
Repeati147 – 187Gelsolin-like 2Add BLAST41
Repeati260 – 306Gelsolin-like 3Add BLAST47
Repeati405 – 451Gelsolin-like 4Add BLAST47
Repeati524 – 564Gelsolin-like 5Add BLAST41
Repeati625 – 667Gelsolin-like 6Add BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 124Actin-severingSequence analysisAdd BLAST124
Regioni72 – 75Actin-actin interfilament contact point4
Regioni136 – 145Polyphosphoinositide binding10
Regioni384 – 715Actin-binding, Ca-sensitiveSequence analysisAdd BLAST332

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG004183.

Family and domain databases

Gene3Di3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
[Graphical view]
SUPFAMiSSF82754. SSF82754. 1 hit.

Sequencei

Sequence statusi: Complete.

O61270-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTELEIQKA GKETGIQIWR IEDFELVPVP KTNHGKFYTG DSYIILKTTA
60 70 80 90 100
LESGRGFEWN LHYWQGKESS QDERGAVAIL AVKMDDHLNG GPVEHREVQG
110 120 130 140 150
NESAAFKGLF PTITYLIGGV ASGFTHVEIN EVEDRKVLTR VKGKRPVRAT
160 170 180 190 200
QVPIKWTSLT DSDSYVFDIG KEIYVWSGPK ASHFEKNKAI QYADGLKNER
210 220 230 240 250
QGRAELHHID SLDDKESRTM LKDFFGEAFP GSIPSGESDT VQQVGTTIKL
260 270 280 290 300
FRISDDSGTL KITLVSENSP FNQGDLSSGD TFVLANARTN HIFVWKGKDS
310 320 330 340 350
SRTERASAAN PDNSFFNKIE MPLTSKLTVL PEGGETANFK SLFTNWKSSR
360 370 380 390 400
DQRGLGQVHS INKTAKVAKE TFDASVLHSN PKKAAESKMI DDGSGKTQIW
410 420 430 440 450
RVASLRKEPV PKELYGQFYG GDCYIIMYTP QRGANVLYYW QGNKASINER
460 470 480 490 500
TALPIQTKNT HETECDGNAS QIRVVQGTEP PHMMMLFGGK PLIVHLGDTI
510 520 530 540 550
SPTGKSKAAS TRLYQVQSFF AGRCRAVEVP AKSSHLNSND AFLLITPSGS
560 570 580 590 600
YIWVGKGAVE SEIQGAKDTA GILKISKYEI INENQEPNEF WTALGGQSDY
610 620 630 640 650
WRDEREEGVP VEPRLFEMSN ATGNFIAEEI NSNYVQSDLN PDSIMMLDAW
660 670 680 690 700
NYIYVWIGKE ANQEEKMSFK SLVDNYVKTD GSGRSKDIPR EVFDQGKEPL
710
SFTGHFLGWD KTLWD
Length:715
Mass (Da):79,866
Last modified:August 1, 1998 - v1
Checksum:i63AFCC6541255136
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009981 mRNA. Translation: BAA28674.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009981 mRNA. Translation: BAA28674.1.

3D structure databases

ProteinModelPortaliO61270.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004183.

Family and domain databases

Gene3Di3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PfamiPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
[Graphical view]
SUPFAMiSSF82754. SSF82754. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGELS_HALRO
AccessioniPrimary (citable) accession number: O61270
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: August 1, 1998
Last modified: January 20, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.