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P32392 (ARP3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin-related protein 3
Alternative name(s):
Actin-2
Actin-like protein 3
Actin-like protein 66B
Gene names
Name:Arp66B
Synonyms:Actr66B
ORF Names:CG7558
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament By similarity.

Subunit structure

Component of the Arp2/3 complex By similarity.

Subcellular location

Cytoplasmcytoskeleton By similarity.

Sequence similarities

Belongs to the actin family. ARP3 subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   LigandATP-binding
Actin-binding
Nucleotide-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processregulation of actin filament polymerization

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

actin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Actin-related protein 3
PRO_0000089087

Experimental info

Sequence conflict691A → R in CAA50674. Ref.1
Sequence conflict1761H → D in CAA50674. Ref.1
Sequence conflict2031F → L in CAA50674. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32392 [UniParc].

Last modified May 9, 2003. Version 3.
Checksum: D8EAA080ED81513A

FASTA41847,033
        10         20         30         40         50         60 
MAGRLPACVI DVGTGYSKLG FAGNKEPQFI IPSAIAIKES ARVGDTNTRR ITKGIEDLDF 

        70         80         90        100        110        120 
FIGDEAFDAT GYSIKYPVRH GLVEDWDLME RFLEQCVFKY LRAEPEDHYF LLTEPPLNTP 

       130        140        150        160        170        180 
ENREYTAEIM FETFNVPGLY IAVQAVLALA ASWASRSAEE RTLTGIVVDS GDGVTHVIPV 

       190        200        210        220        230        240 
AEGYVIGSCI KHIPIAGRNI TSFIQSLLRE REVGIPPEQS LETAKAIKEK HCYICPDIAK 

       250        260        270        280        290        300 
EFAKYDTEPG KWIRNFSGVN TVTKAPFNVD VGYERFLGPE IFFHPEFSNP DFTIPLSEIV 

       310        320        330        340        350        360 
DNVIQNCPID VRRPLYNNIV LSGGSTMFKD FGRRLQRDIK RSVDTRLRIS ENLSEGRIKP 

       370        380        390        400        410 
KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKAAY EEYGPSICRH NPVFGTMT 

« Hide

References

« Hide 'large scale' references
[1]"A Drosophila homologue of the Schizosaccharomyces pombe act2 gene."
Fyrberg C., Fyrberg E.A.
Biochem. Genet. 31:329-341(1993) [PubMed: 8274139] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71789 Genomic DNA. Translation: CAA50674.1.
AE014296 Genomic DNA. Translation: AAF50488.1.
AY051859 mRNA. Translation: AAK93283.1.
RefSeqNP_523968.1. NM_079244.2.
UniGeneDm.881.

3D structure databases

ProteinModelPortalP32392.
SMRP32392. Positions 2-415.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-20563N.
IntActP32392. 2 interactions.
MINTMINT-321617.
STRINGP32392.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076737; FBpp0076460; FBgn0262716.
GeneID38898.
KEGGdme:Dmel_CG7558.
NMPDRfig|7227.3.peg.8786.

Organism-specific databases

CTD38898.
FlyBaseFBgn0262716. Arp66B.

Phylogenomic databases

eggNOGinNOG04085.
GeneTreeEMGT00050000003738.
InParanoidP32392.
OMADNVIQNC.
OrthoDBEOG49CNQ1.
PhylomeDBP32392.

Gene expression databases

BgeeP32392.
GermOnlineCG7558. Drosophila melanogaster.

Family and domain databases

InterProIPR004000. Actin-like.
IPR020902. Actin/actin-like_CS.
IPR015623. Arp3.
[Graphical view]
PANTHERPTHR11937. Actin_like. 1 hit.
PTHR11937:SF31. Arp3. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio810922.

Entry information

Entry nameARP3_DROME
AccessionPrimary (citable) accession number: P32392
Secondary accession number(s): Q9VSD5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: May 9, 2003
Last modified: January 25, 2012
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families