Reviewed, UniProtKB/Swiss-Prot P83967 (ACT6_DROME)

Names and origin

Protein names

Recommended name:
    Actin, indirect flight muscle
Alternative name(s):
    Actin-88F

Gene names

Name:	Act88F
ORF Names:	CG5178

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. 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	Muscle.
Miscellaneous	Abnormalities in Act88F-ifm(3)7 flight muscles result from incorporation of the mutant actin isoform into assembling myofibrils. 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
Molecular function	Muscle protein Structural protein
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phagocytosis, engulfment Inferred from mutant phenotype. Source: FlyBase
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VWR1	1	EBI-184828,EBI-253979
tsr	P45594	1	EBI-184828,EBI-110774

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Propeptide	1 – 2	2	Removed in mature form By similarity
	Chain	3 – 376	374	Actin, indirect flight muscle
Amino acid modifications
	Modified residue	3	1	N-acetylaspartate By similarity
Experimental info
	Mutagenesis	357 – 376	20	Missing in allele Act88F-ifm(3)7
	Sequence conflict	200	1	S → T in AAA28321. Ref.2
	Sequence conflict	213	1	I → T in AAA28321. Ref.2
	Sequence conflict	226	1	Q → D in AAA28321. Ref.2
	Sequence conflict	320	1	A → T in AAA28321. Ref.2
	Sequence conflict	345	1	S → L in AAA28321. Ref.2
	Sequence conflict	369	1	G → S in AAA28321. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P83967-1 [UniParc]. Last modified June 7, 2004. Version 1. Checksum: C64C33A1674B7886	FASTA	376	41,700
	10 20 30 40 50 60 MCDDDAGALV IDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ 70 80 90 100 110 120 SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM 130 140 150 160 170 180 TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGF ALPHAILRLD 190 200 210 220 230 240 LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS 250 260 270 280 290 300 YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANSVL 310 320 330 340 350 360 SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK 370 QEYDESGPGI 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 (APR-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Two Drosophila actin genes in detail. Gene structure, protein structure and transcription during development." Sanchez F., Tobin S.L., Rdest U., Zulauf E., McCarthy B.J. J. Mol. Biol. 163:533-551(1983) [PubMed: 6405041] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	Okamoto H., Hiromi Y., Ishikawa E., Yamada T., Isoda K., Maekawa H., Hotta Y. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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.
[5]	"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.
[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 1-53.
[7]	"A nonsense mutation within the act88F actin gene disrupts myofibril formation in Drosophila indirect flight muscles." Karlik C.C., Coutu M.D., Fyrberg E.A. Cell 38:711-719(1984) [PubMed: 6488317] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 302-376, MUTAGENESIS OF 357-TRP--PHE-376.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M18826 Genomic DNA. Translation: AAA28323.1. K02065 Genomic DNA. Translation: AAA28322.1. AB003910 Genomic DNA. Translation: BAA20058.1. AE014297 Genomic DNA. Translation: AAF55198.1. M18830 Genomic DNA. Translation: AAA28321.1.
PIR	ATFF8. A03003.
RefSeq	NP_524367.1.
UniGene	Dm.5746
3D structure databases
HSSP	HSSP built from PDB template 1HLU based on UniProtKB P02570.
SMR	P83967. Positions 8-372.
ModBase	Search...
Protein-protein interaction databases
IntAct	P83967.
Genome annotation databases
Ensembl	CG5178. Drosophila melanogaster. [Contig view]
GeneID	41885.
KEGG	dme:Dmel_CG5178.
NMPDR	fig|7227.3.peg.12994.
Organism-specific databases
FlyBase	FBgn0000047. Act88F.
Phylogenomic databases
HOGENOM	P83967.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-011778-MON.
Gene expression databases
ArrayExpress	P83967.
GermOnline	CG5178. Drosophila melanogaster.
Family and domain databases
InterPro	IPR004001. Actin_CS. IPR004000. Actin_like. [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]
ProDom	P83967. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

ACT6_DROME

Accession

Primary (citable) accession number: P83967
Secondary accession number(s): P02575, P45893, Q9VF62

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 7, 2004
Last modified:	July 22, 2008
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project