Reviewed, UniProtKB/Swiss-Prot P10981 (ACT5_DROME)

Names and origin

Protein names

Recommended name:
    Actin-87E

Gene names

Name:	Act87E
ORF Names:	CG18290

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	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Ref.7 Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. Ref.7
Subunit structure	Component of the Tip60 chromatin-remodeling complex which contains the catalytic subunit Tip60 and the subunits Domino, Tra1, Brd8, E(Pc), DMAP1, Pontin, Reptin, Ing3, Act87E, BAP55, Mrg15, MrgBP, Gas41 and YL-1.
Subcellular location	Cytoplasm › cytoskeleton.
Miscellaneous	In Drosophila there are 6 closely related actin genes.
Sequence similarities	Belongs to the actin family.
Sequence caution	The sequence AAM29410.1 differs from that shown. Reason: Erroneous translation.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell lipid particle Inferred from direct assay. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CG6873-RA	Q9VWR1	1	EBI-135521,EBI-253979
ref(2)P	P14199	1	EBI-135521,EBI-128642
tsr	P45594	1	EBI-135521,EBI-110774

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 2	2	Removed in mature form By similarity		PRO_0000000664
	Chain	3 – 376	374	Actin-87E		PRO_0000000665
Amino acid modifications
	Modified residue	3	1	N-acetylaspartate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P10981-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 60252541882B0A7F	FASTA	376	41,802
	10 20 30 40 50 60 MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ 70 80 90 100 110 120 SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM 130 140 150 160 170 180 TQIMFETFNA PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD 190 200 210 220 230 240 LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS 250 260 270 280 290 300 YELPDGQVIT IGNERFRCPE SLFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANIVM 310 320 330 340 350 360 SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK 370 QEYDESGPGI VHRKCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular and genetic characterization of the Drosophila melanogaster 87E actin gene region." Manseau L.J., Ganetzky B., Craig E.A. Genetics 119:407-420(1988) [PubMed: 2840338] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Canton-S.
[2]	Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N. Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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.
[4]	"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.
[5]	"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.
[6]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Testis.
[7]	"Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions." Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L., Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L. Science 306:2084-2087(2004) [PubMed: 15528408] [Abstract] Cited for: IDENTIFICATION IN THE TIP60 COMPLEX, FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X12452 Genomic DNA. Translation: CAA30982.1. K00674 Genomic DNA. Translation: AAA28320.1. AE014297 Genomic DNA. Translation: AAF54950.2. AE014297 Genomic DNA. Translation: AAN13567.1. AY089587 mRNA. Translation: AAL90325.1. AY113405 mRNA. Translation: AAM29410.1. Sequence problems. BT016152 mRNA. Translation: AAV37037.1.
PIR	S04538.
RefSeq	NP_477091.1. NP_731812.1.
UniGene	Dm.4869
3D structure databases
HSSP	HSSP built from PDB template 1D4X based on UniProtKB P10983.
SMR	P10981. Positions 5-372.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:18091N.
IntAct	P10981. 11 interactions.
Proteomic databases
PRIDE	P10981.
Genome annotation databases
Ensembl	FBgn0000046. Drosophila melanogaster. [Contig view]
GeneID	48632.
KEGG	dme:Dmel_CG18290.
Organism-specific databases
FlyBase	FBgn0000046. Act87E.
Phylogenomic databases
HOGENOM	P10981.
OMA	P10981. HGILRID.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-011438-MON. DMEL-XXX-02:DMEL-XXX-02-011439-MON.
Gene expression databases
ArrayExpress	P10981.
GermOnline	CG18290. Drosophila melanogaster.
Family and domain databases
InterPro	IPR004000. Actin-like. IPR004001. Actin_CS. [Graphical view]
PANTHER	PTHR11937. Actin_like. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
PRINTS	PR00190. ACTIN.
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS00406. ACTINS_1. 1 hit. PS00432. ACTINS_2. 1 hit. PS01132. ACTINS_ACT_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	839531.

Entry information

Entry name

ACT5_DROME

Accession

Primary (citable) accession number: P10981
Secondary accession number(s): A4V2T6 , Q5U0U0, Q8MZ23, Q9VFU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project