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Q28372 (GELS_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Gelsolin
Alternative name(s):
Actin-depolymerizing factor
Short name=ADF
Brevin

Cleaved into the following chain:

  1. Gelsolin, N-terminally processed
Gene names
Name:GSN
OrganismEquus caballus (Horse) [Complete proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Protein attributes

Sequence length731 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 By similarity.

Subcellular location

Cytoplasm › cytoskeleton.

Sequence similarities

Belongs to the villin/gelsolin family.

Contains 6 gelsolin-like repeats.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCytoplasm
Cytoskeleton
   DomainRepeat
   LigandActin-binding
Calcium
   Molecular functionActin capping
   PTMAcetylation
Disulfide bond
   Technical term3D-structure
Complete 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

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 731731Gelsolin
PRO_0000367500
Initiator methionine11Removed; alternate By similarity
Chain2 – 731730Gelsolin, N-terminally processed
PRO_0000218723

Regions

Repeat25 – 7551Gelsolin-like 1
Repeat147 – 18741Gelsolin-like 2
Repeat263 – 30543Gelsolin-like 3
Repeat402 – 45352Gelsolin-like 4
Repeat525 – 56541Gelsolin-like 5
Repeat628 – 67043Gelsolin-like 6
Region2 – 125124Actin-severing Potential
Region72 – 754Actin-actin interfilament contact point
Region111 – 1188Polyphosphoinositide binding By similarity
Region137 – 1459Polyphosphoinositide binding By similarity
Region383 – 731349Actin-binding, Ca-sensitive Potential

Amino acid modifications

Modified residue11N-acetylmethionine; in Gelsolin; alternate By similarity
Disulfide bond164 ↔ 177

Secondary structure

1 ......................................................................................................................................... 731
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q28372 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A72ABEC8015145A5

FASTA73180,827
        10         20         30         40         50         60 
MVVEHPEFLK AGKEPGLQIW RVEKFDLVPV PPNLYGDFFT GDAYVILKTV QLRNGILQYD 

        70         80         90        100        110        120 
LHYWLGNECS QDESGAAAIF TVQLDDYLNG RAVQHREVQG FESATFLGYF KSGLKYKKGG 

       130        140        150        160        170        180 
VASGFKHVVP NEVVVQRLLQ VKGRRVVRAT EVPVSWESFN NGDCFILDLG NNIYQWCGSK 

       190        200        210        220        230        240 
SNRFERLKAT QVSKGIRDNE RSGRAQVSVF EEGAEPEAML QVLGPKPTLP EATEDTVKED 

       250        260        270        280        290        300 
AANRKLAKLY KVSNGAGPMV VSLVADENPF AQGALRSEDC FILDHGKDGK IFVWKGKQAN 

       310        320        330        340        350        360 
MEERKAALKT ASDFISKMDY PKQTQVSVLP EGGETPLFRQ FFKNWRDPDQ TEGLGLAYLS 

       370        380        390        400        410        420 
SHIAHVERVP FDAATLHTST AMAAQHGMDD DGTGQKQIWR VEGSNKVPVD PATYGQFYGG 

       430        440        450        460        470        480 
DSYIILYNYR HGSRQGQIIY NWQGAQSTQD EVAASAILTA QLDEELGGTP VQSRVVQGKE 

       490        500        510        520        530        540 
PAHLMSLFGG KPMIVYKGGT SREGGQTAPA STRLFQVRAS SSGATRAVEI IPKAGALNSN 

       550        560        570        580        590        600 
DAFVLKTPSA AYLWVGAGAS EAEKTGAQEL LRVLRAQPVQ VAEGSEPDSF WEALGGKATY 

       610        620        630        640        650        660 
RTSPRLKDKK MDAHPPRLFA CSNKIGRFVI EEVPGEFMQE DLATDDVMLL DTWDQVFVWV 

       670        680        690        700        710        720 
GKDSQDEEKT EALTSAKRYI DTDPAHRDRR TPITVVKQGF EPPSFVGWFL GWDDSYWSVD 

       730 
PLDRALAELA A

« Hide

References

[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: 9490033] [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: 9288746] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U31699 mRNA. Translation: AAC13353.1.
RefSeqNP_001075422.1. NM_001081953.1.
UniGeneEca.13376.
Eca.2517.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D0NX-ray2.50A/B3-731[»]
1RGIX-ray3.00G2-346[»]
2FGHX-ray2.80A/B2-730[»]
ProteinModelPortalQ28372.
SMRQ28372. Positions 3-731.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ28372.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100034186.
KEGGecb:100034186.

Organism-specific databases

CTD2934.

Phylogenomic databases

HOVERGENHBG004183.

Family and domain databases

InterProIPR007122. Gelsolin.
IPR007123. Gelsolin_dom.
[Graphical view]
KOK05768.
PANTHERPTHR11977. Gelsolin. 1 hit.
PfamPF00626. Gelsolin. 6 hits.
[Graphical view]
PRINTSPR00597. GELSOLIN.
SMARTSM00262. GEL. 6 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGELS_HORSE
AccessionPrimary (citable) accession number: Q28372
Secondary accession number(s): Q95180
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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