P02572 (ACT2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin-42A

Gene names

Name:	Act42A
ORF Names:	CG12051

Organism

Drosophila melanogaster (Fruit fly)

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 further processed into a mature form.
Protein existence	Evidence at transcript 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. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction.
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	All cells and tissues of the developing embryo. Later in development, expression is higher in midgut, brain, nerve cord, and gonads. Ref.8
Induction	By 20-hydroxyecdysone.
Miscellaneous	In Drosophila there are 6 closely related actin genes.
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cytokinesis Inferred from mutant phenotype. Source: FlyBase phagocytosis, engulfment Inferred from mutant phenotype. Source: FlyBase
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Inferred from direct assay. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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_0000000658
	Chain	3 – 376	374	Actin-42A		PRO_0000000659
Amino acid modifications
	Modified residue	3	1	N-acetylaspartate By similarity
Experimental info
	Sequence conflict	12 – 287	276	Missing in CAA38618. Ref.2
	Sequence conflict	275	1	I → L in AAA28314. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P02572 [UniParc]. Last modified February 21, 2001. Version 3. Checksum: 7C6D13CC6E42331E	FASTA	376	41,824
	10 20 30 40 50 60 MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ 70 80 90 100 110 120 SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM 130 140 150 160 170 180 TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD 190 200 210 220 230 240 LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS 250 260 270 280 290 300 YELPDGQVIT IGNERFRCPE SLFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL 310 320 330 340 350 360 SGGTTMYPGI ADRMQKEITA LAPSTMKIKI VAPPERKYSV WIGGSILASL STFQQMWISK 370 QEYDESGPSI VHRKCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	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].
[2]	Burn T.C., Tobin S.L. Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Canton-S.
[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. Strain: Berkeley.
[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]	"The actin genes of Drosophila: protein coding regions are highly conserved but intron positions are not." Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N. Cell 24:107-116(1981) [PubMed: 6263481] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160 AND 229-376.
[7]	"20-hydroxyecdysone regulates cytoplasmic actin gene expression in Drosophila cultured cells." Couderc J.-L., Hilal L., Sobier M.L., Dastugue B. Nucleic Acids Res. 15:2549-2561(1987) [PubMed: 2436146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
[8]	"Transcripts of individual Drosophila actin genes are differentially distributed during embryogenesis." Tobin S.L., Cook P.J., Burn T.C. Dev. Genet. 11:15-26(1990) [PubMed: 1694472] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	K00670 Genomic DNA. Translation: AAA28314.1. X54848 Genomic DNA. Translation: CAA38618.1. AE013599 Genomic DNA. Translation: AAF57294.1. AY118907 mRNA. Translation: AAM50767.1. X05176 Genomic DNA. Translation: CAA28809.1.
PIR	A03000. S14851.
RefSeq	NP_523625.1. NM_078901.2.
UniGene	Dm.7040.
3D structure databases
ProteinModelPortal	P02572.
SMR	P02572. Positions 3-376.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-20355N.
IntAct	P02572. 6 interactions.
MINT	MINT-847693.
STRING	P02572.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0086029; FBpp0085365; FBgn0000043.
GeneID	35526.
KEGG	dme:Dmel_CG12051.
Organism-specific databases
CTD	35526.
FlyBase	FBgn0000043. Act42A.
Phylogenomic databases
eggNOG	inNOG08362.
GeneTree	EMGT00050000003737.
InParanoid	P02572.
OMA	DCLMKIL.
OrthoDB	EOG4Z34W3.
PhylomeDB	P02572.
Gene expression databases
Bgee	P02572.
GermOnline	CG12051. Drosophila melanogaster.
Family and domain databases
InterPro	IPR004000. Actin-like. IPR020902. Actin/actin-like_CS. IPR004001. Actin_CS. [Graphical view]
KO	K05692.
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
NextBio	793859.

Entry information

Entry name

ACT2_DROME

Accession

Primary (citable) accession number: P02572
Secondary accession number(s): Q24228, Q540X3, Q9V9J4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 21, 2001
Last modified:	January 25, 2012
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project