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Protein

Gelsolin

Gene

GSN

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi420Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi421Calcium 1By similarity1
Metal bindingi451Calcium 1By similarity1
Metal bindingi500Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi540Calcium 2By similarity1
Metal bindingi540Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi541Calcium 2By similarity1
Metal bindingi563Calcium 2By similarity1
Metal bindingi645Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi646Calcium 3By similarity1
Metal bindingi668Calcium 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
Gene namesi
Name:GSN
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003675001 – 731GelsolinAdd BLAST731

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35PhosphotyrosineBy similarity1
Disulfide bondi164 ↔ 177
Modified residuei358PhosphotyrosineBy similarity1
Modified residuei414PhosphotyrosineBy similarity1
Modified residuei533N6-acetyllysineBy similarity1
Modified residuei552PhosphotyrosineBy similarity1
Modified residuei600PhosphotyrosineBy similarity1
Modified residuei691PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PeptideAtlasiQ28372.
PRIDEiQ28372.

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 similarity).By similarity

Structurei

Secondary structure

1731
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 10Combined sources3
Beta strandi13 – 22Combined sources10
Beta strandi24 – 29Combined sources6
Helixi32 – 34Combined sources3
Beta strandi37 – 39Combined sources3
Beta strandi43 – 51Combined sources9
Beta strandi57 – 65Combined sources9
Helixi71 – 87Combined sources17
Turni88 – 90Combined sources3
Beta strandi93 – 98Combined sources6
Helixi104 – 108Combined sources5
Beta strandi114 – 118Combined sources5
Turni121 – 124Combined sources4
Beta strandi137 – 142Combined sources6
Beta strandi144 – 146Combined sources3
Beta strandi148 – 152Combined sources5
Helixi156 – 158Combined sources3
Beta strandi161 – 168Combined sources8
Beta strandi170 – 177Combined sources8
Helixi183 – 199Combined sources17
Helixi201 – 203Combined sources3
Beta strandi205 – 211Combined sources7
Helixi217 – 223Combined sources7
Helixi234 – 236Combined sources3
Helixi237 – 243Combined sources7
Beta strandi248 – 253Combined sources6
Beta strandi255 – 258Combined sources4
Beta strandi260 – 270Combined sources11
Helixi272 – 274Combined sources3
Beta strandi279 – 285Combined sources7
Helixi286 – 288Combined sources3
Beta strandi290 – 295Combined sources6
Beta strandi297 – 299Combined sources3
Helixi301 – 304Combined sources4
Helixi307 – 317Combined sources11
Beta strandi325 – 330Combined sources6
Helixi336 – 339Combined sources4
Beta strandi342 – 344Combined sources3
Beta strandi351 – 355Combined sources5
Helixi361 – 363Combined sources3
Turni373 – 375Combined sources3
Helixi376 – 378Combined sources3
Helixi380 – 386Combined sources7
Beta strandi396 – 402Combined sources7
Beta strandi405 – 408Combined sources4
Helixi411 – 413Combined sources3
Beta strandi416 – 418Combined sources3
Beta strandi421 – 431Combined sources11
Beta strandi434 – 443Combined sources10
Helixi449 – 464Combined sources16
Turni465 – 467Combined sources3
Beta strandi470 – 476Combined sources7
Helixi482 – 485Combined sources4
Beta strandi493 – 498Combined sources6
Turni503 – 505Combined sources3
Beta strandi511 – 519Combined sources9
Beta strandi525 – 530Combined sources6
Helixi534 – 536Combined sources3
Beta strandi539 – 546Combined sources8
Beta strandi551 – 555Combined sources5
Helixi561 – 574Combined sources14
Beta strandi580 – 582Combined sources3
Helixi588 – 592Combined sources5
Turni593 – 595Combined sources3
Helixi610 – 613Combined sources4
Beta strandi617 – 622Combined sources6
Turni624 – 626Combined sources3
Beta strandi629 – 632Combined sources4
Helixi639 – 641Combined sources3
Beta strandi646 – 651Combined sources6
Beta strandi656 – 660Combined sources5
Helixi666 – 669Combined sources4
Helixi672 – 682Combined sources11
Beta strandi693 – 697Combined sources5
Helixi703 – 706Combined sources4
Helixi714 – 717Combined sources4
Helixi721 – 729Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D0NX-ray2.50A/B3-731[»]
1RGIX-ray3.00G2-347[»]
2FGHX-ray2.80A/B2-731[»]
ProteinModelPortaliQ28372.
SMRiQ28372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ28372.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati25 – 75Gelsolin-like 1Add BLAST51
Repeati147 – 187Gelsolin-like 2Add BLAST41
Repeati263 – 305Gelsolin-like 3Add BLAST43
Repeati402 – 453Gelsolin-like 4Add BLAST52
Repeati525 – 565Gelsolin-like 5Add BLAST41
Repeati628 – 670Gelsolin-like 6Add BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 125Actin-severingSequence analysisAdd BLAST124
Regioni72 – 75Actin-actin interfilament contact point4
Regioni111 – 118Polyphosphoinositide bindingBy similarity8
Regioni137 – 145Polyphosphoinositide bindingBy similarity9
Regioni383 – 731Actin-binding, Ca-sensitiveSequence analysisAdd BLAST349

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG004183.
InParanoidiQ28372.
KOiK05768.

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.

Q28372-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVEHPEFLK AGKEPGLQIW RVEKFDLVPV PPNLYGDFFT GDAYVILKTV
60 70 80 90 100
QLRNGILQYD LHYWLGNECS QDESGAAAIF TVQLDDYLNG RAVQHREVQG
110 120 130 140 150
FESATFLGYF KSGLKYKKGG VASGFKHVVP NEVVVQRLLQ VKGRRVVRAT
160 170 180 190 200
EVPVSWESFN NGDCFILDLG NNIYQWCGSK SNRFERLKAT QVSKGIRDNE
210 220 230 240 250
RSGRAQVSVF EEGAEPEAML QVLGPKPTLP EATEDTVKED AANRKLAKLY
260 270 280 290 300
KVSNGAGPMV VSLVADENPF AQGALRSEDC FILDHGKDGK IFVWKGKQAN
310 320 330 340 350
MEERKAALKT ASDFISKMDY PKQTQVSVLP EGGETPLFRQ FFKNWRDPDQ
360 370 380 390 400
TEGLGLAYLS SHIAHVERVP FDAATLHTST AMAAQHGMDD DGTGQKQIWR
410 420 430 440 450
VEGSNKVPVD PATYGQFYGG DSYIILYNYR HGSRQGQIIY NWQGAQSTQD
460 470 480 490 500
EVAASAILTA QLDEELGGTP VQSRVVQGKE PAHLMSLFGG KPMIVYKGGT
510 520 530 540 550
SREGGQTAPA STRLFQVRAS SSGATRAVEI IPKAGALNSN DAFVLKTPSA
560 570 580 590 600
AYLWVGAGAS EAEKTGAQEL LRVLRAQPVQ VAEGSEPDSF WEALGGKATY
610 620 630 640 650
RTSPRLKDKK MDAHPPRLFA CSNKIGRFVI EEVPGEFMQE DLATDDVMLL
660 670 680 690 700
DTWDQVFVWV GKDSQDEEKT EALTSAKRYI DTDPAHRDRR TPITVVKQGF
710 720 730
EPPSFVGWFL GWDDSYWSVD PLDRALAELA A
Length:731
Mass (Da):80,827
Last modified:January 23, 2007 - v2
Checksum:iA72ABEC8015145A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31699 mRNA. Translation: AAC13353.1.
RefSeqiNP_001075422.1. NM_001081953.1.
UniGeneiEca.2517.

Genome annotation databases

GeneIDi100034186.
KEGGiecb:100034186.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31699 mRNA. Translation: AAC13353.1.
RefSeqiNP_001075422.1. NM_001081953.1.
UniGeneiEca.2517.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D0NX-ray2.50A/B3-731[»]
1RGIX-ray3.00G2-347[»]
2FGHX-ray2.80A/B2-731[»]
ProteinModelPortaliQ28372.
SMRiQ28372.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PeptideAtlasiQ28372.
PRIDEiQ28372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100034186.
KEGGiecb:100034186.

Organism-specific databases

CTDi2934.

Phylogenomic databases

HOVERGENiHBG004183.
InParanoidiQ28372.
KOiK05768.

Miscellaneous databases

EvolutionaryTraceiQ28372.
PROiQ28372.

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_HORSE
AccessioniPrimary (citable) accession number: Q28372
Secondary accession number(s): Q95180
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.