Reviewed, UniProtKB/Swiss-Prot P32392 (ARP3_DROME)

Names and origin

Protein names

Recommended name:
    Actin-related protein 3
Alternative name(s):
    Actin-like protein 3
    Actin-like protein 66B
    Actin-2

Gene names

Name:	Arp66B
Synonyms:	Actr66B
ORF Names:	CG7558

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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	Cytoplasm › cytoskeleton By similarity.
Sequence similarities	Belongs to the actin family. ARP3 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Actin-binding Nucleotide-binding
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	actin filament reorganization during cell cycle Inferred from physical interaction. Source: FlyBase axonal fasciculation Inferred from mutant phenotype. Source: FlyBase cytoplasmic transport, nurse cell to oocyte Inferred from mutant phenotype. Source: FlyBase ovarian ring canal stabilization Inferred from mutant phenotype. Source: FlyBase phagocytosis, engulfment Inferred from mutant phenotype. Source: FlyBase pseudocleavage during syncytial blastoderm formation Inferred from physical interaction. Source: FlyBase regulation of actin filament polymerization Inferred from electronic annotation. Source: InterPro
Cellular component	Arp2/3 protein complex Non-traceable author statement. Source: FlyBase cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from direct assay. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cog3	Q961G1	1	EBI-176768,EBI-119125
woc	Q9VB55	1	EBI-176768,EBI-184355

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 418	418	Actin-related protein 3		PRO_0000089087
Experimental info
	Sequence conflict	69	1	A → R in CAA50674. Ref.1
	Sequence conflict	176	1	H → D in CAA50674. Ref.1
	Sequence conflict	203	1	F → L in CAA50674. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32392-1 [UniParc]. Last modified May 9, 2003. Version 3. Checksum: D8EAA080ED81513A	FASTA	418	47,033
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
[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
EMBLGenBankDDBJ	X71789 Genomic DNA. Translation: CAA50674.1. AE014296 Genomic DNA. Translation: AAF50488.1. AY051859 mRNA. Translation: AAK93283.1.
RefSeq	NP_523968.1.
UniGene	Dm.881
3D structure databases
HSSP	HSSP built from PDB template 1K8K based on UniProtKB P32391.
SMR	P32392. Positions 3-417.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:20563N.
IntAct	P32392. 7 interactions.
Genome annotation databases
Ensembl	FBgn0011744. Drosophila melanogaster. [Contig view]
GeneID	38898.
KEGG	dme:Dmel_CG7558.
NMPDR	fig|7227.3.peg.8786.
Organism-specific databases
FlyBase	FBgn0011744. Arp66B.
Phylogenomic databases
HOGENOM	P32392.
OMA	P32392. TEDLDFF.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-015686-MON.
Gene expression databases
ArrayExpress	P32392.
GermOnline	CG7558. Drosophila melanogaster.
Family and domain databases
InterPro	IPR004000. Actin-like. IPR015623. Arp3. [Graphical view]
PANTHER	PTHR11937. Actin_like. 1 hit. PTHR11937:SF31. Arp3. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS01132. ACTINS_ACT_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	810922.

Entry information

Entry name

ARP3_DROME

Accession

Primary (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:	June 16, 2009
This is version 74 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project