Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi420 – 4201Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi421 – 4211Calcium 1By similarity
Metal bindingi451 – 4511Calcium 1By similarity
Metal bindingi500 – 5001Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi540 – 5401Calcium 2By similarity
Metal bindingi540 – 5401Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi541 – 5411Calcium 2By similarity
Metal bindingi563 – 5631Calcium 2By similarity
Metal bindingi645 – 6451Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi646 – 6461Calcium 3By similarity
Metal bindingi668 – 6681Calcium 3By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 731731GelsolinPRO_0000367500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351PhosphotyrosineBy similarity
Disulfide bondi164 ↔ 177
Modified residuei358 – 3581PhosphotyrosineBy similarity
Modified residuei414 – 4141PhosphotyrosineBy similarity
Modified residuei533 – 5331N6-acetyllysineBy similarity
Modified residuei552 – 5521PhosphotyrosineBy similarity
Modified residuei600 – 6001PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

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

1
731
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Beta strandi13 – 2210Combined sources
Beta strandi24 – 296Combined sources
Helixi32 – 343Combined sources
Beta strandi37 – 393Combined sources
Beta strandi43 – 519Combined sources
Beta strandi57 – 659Combined sources
Helixi71 – 8717Combined sources
Turni88 – 903Combined sources
Beta strandi93 – 986Combined sources
Helixi104 – 1085Combined sources
Beta strandi114 – 1185Combined sources
Turni121 – 1244Combined sources
Beta strandi137 – 1426Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi148 – 1525Combined sources
Helixi156 – 1583Combined sources
Beta strandi161 – 1688Combined sources
Beta strandi170 – 1778Combined sources
Helixi183 – 19917Combined sources
Helixi201 – 2033Combined sources
Beta strandi205 – 2117Combined sources
Helixi217 – 2237Combined sources
Helixi234 – 2363Combined sources
Helixi237 – 2437Combined sources
Beta strandi248 – 2536Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi260 – 27011Combined sources
Helixi272 – 2743Combined sources
Beta strandi279 – 2857Combined sources
Helixi286 – 2883Combined sources
Beta strandi290 – 2956Combined sources
Beta strandi297 – 2993Combined sources
Helixi301 – 3044Combined sources
Helixi307 – 31711Combined sources
Beta strandi325 – 3306Combined sources
Helixi336 – 3394Combined sources
Beta strandi342 – 3443Combined sources
Beta strandi351 – 3555Combined sources
Helixi361 – 3633Combined sources
Turni373 – 3753Combined sources
Helixi376 – 3783Combined sources
Helixi380 – 3867Combined sources
Beta strandi396 – 4027Combined sources
Beta strandi405 – 4084Combined sources
Helixi411 – 4133Combined sources
Beta strandi416 – 4183Combined sources
Beta strandi421 – 43111Combined sources
Beta strandi434 – 44310Combined sources
Helixi449 – 46416Combined sources
Turni465 – 4673Combined sources
Beta strandi470 – 4767Combined sources
Helixi482 – 4854Combined sources
Beta strandi493 – 4986Combined sources
Turni503 – 5053Combined sources
Beta strandi511 – 5199Combined sources
Beta strandi525 – 5306Combined sources
Helixi534 – 5363Combined sources
Beta strandi539 – 5468Combined sources
Beta strandi551 – 5555Combined sources
Helixi561 – 57414Combined sources
Beta strandi580 – 5823Combined sources
Helixi588 – 5925Combined sources
Turni593 – 5953Combined sources
Helixi610 – 6134Combined sources
Beta strandi617 – 6226Combined sources
Turni624 – 6263Combined sources
Beta strandi629 – 6324Combined sources
Helixi639 – 6413Combined sources
Beta strandi646 – 6516Combined sources
Beta strandi656 – 6605Combined sources
Helixi666 – 6694Combined sources
Helixi672 – 68211Combined sources
Beta strandi693 – 6975Combined sources
Helixi703 – 7064Combined sources
Helixi714 – 7174Combined sources
Helixi721 – 7299Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D0NX-ray2.50A/B3-731[»]
1RGIX-ray3.00G2-347[»]
2FGHX-ray2.80A/B2-731[»]
ProteinModelPortaliQ28372.
SMRiQ28372. Positions 3-731.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ28372.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati25 – 7551Gelsolin-like 1Add
BLAST
Repeati147 – 18741Gelsolin-like 2Add
BLAST
Repeati263 – 30543Gelsolin-like 3Add
BLAST
Repeati402 – 45352Gelsolin-like 4Add
BLAST
Repeati525 – 56541Gelsolin-like 5Add
BLAST
Repeati628 – 67043Gelsolin-like 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 125124Actin-severingSequence analysisAdd
BLAST
Regioni72 – 754Actin-actin interfilament contact point
Regioni111 – 1188Polyphosphoinositide bindingBy similarity
Regioni137 – 1459Polyphosphoinositide bindingBy similarity
Regioni383 – 731349Actin-binding, Ca-sensitiveSequence analysisAdd
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1D0NX-ray2.50A/B3-731[»]
1RGIX-ray3.00G2-347[»]
2FGHX-ray2.80A/B2-731[»]
ProteinModelPortaliQ28372.
SMRiQ28372. Positions 3-731.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

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.

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. "Equus caballus gelsolin -- cDNA sequence and protein structural implications."
    Koepf E.K., Hewitt J., Vo H., Macgillivray R.T.A., Burtnick L.D.
    Eur. J. Biochem. 251:613-621(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Smooth muscle.
  2. "The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation."
    Burtnick L.D., Koepf E.K., Grimes J., Jones E.Y., Stuart D.I., McLaughlin P.J., Robinson R.C.
    Cell 90:661-670(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

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: December 9, 2015
This is version 106 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.