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Protein

Actin, indirect flight muscle

Gene

Act88F

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Required for proper formation of indirect flight muscle (IFM) myofibrils.
Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • structural constituent of cytoskeleton Source: FlyBase

GO - Biological processi

  • cytoskeleton organization Source: FlyBase
  • muscle thin filament assembly Source: FlyBase
  • phagocytosis Source: FlyBase
  • skeletal myofibril assembly Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-190873. Gap junction degradation.
R-DME-196025. Formation of annular gap junctions.
R-DME-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DME-3928662. EPHB-mediated forward signaling.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-445095. Interaction between L1 and Ankyrins.
R-DME-5663213. RHO GTPases Activate WASPs and WAVEs.
SignaLinkiP83967.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, indirect flight muscle
Alternative name(s):
Actin-88F
Gene namesi
Name:Act88F
ORF Names:CG5178
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0000047. Act88F.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: FlyBase
  • cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

Homozygous mutants are viable and fertile, but fail to form proper IFMs and are flightless. The IFMs of these mutants display mislocalized Smn and Actn.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi357 – 37620Missing in allele Act88F-ifm(3)7. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000668
Chaini3 – 376374Actin, indirect flight musclePRO_0000000669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylaspartateBy similarity
Modified residuei45 – 451Methionine sulfoxide1 Publication
Modified residuei48 – 481Methionine sulfoxide1 Publication

Post-translational modificationi

Oxidation of Met-45 by Mical to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced.1 Publication

Keywords - PTMi

Acetylation, Oxidation

Proteomic databases

PaxDbiP83967.
PRIDEiP83967.

Expressioni

Tissue specificityi

In adult thorax, expressed in the IFMs.1 Publication

Developmental stagei

Expressed throughout development. Expression is weak during embryonic stages and peaks during larval and pupal stages.1 Publication

Gene expression databases

BgeeiP83967.
ExpressionAtlasiP83967. differential.
GenevisibleiP83967. DM.

Interactioni

Protein-protein interaction databases

BioGridi66947. 17 interactions.
IntActiP83967. 2 interactions.
MINTiMINT-901261.
STRINGi7227.FBpp0082597.

Structurei

3D structure databases

ProteinModelPortaliP83967.
SMRiP83967. Positions 7-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
InParanoidiP83967.
KOiK05692.
OMAiNQMADGE.
OrthoDBiEOG72RMZ1.
PhylomeDBiP83967.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P83967-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDDDAGALV IDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ
60 70 80 90 100
KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE
110 120 130 140 150
EHPVLLTEAP LNPKANREKM TQIMFETFNS PAMYVAIQAV LSLYASGRTT
160 170 180 190 200
GIVLDSGDGV SHTVPIYEGF ALPHAILRLD LAGRDLTDYL MKILTERGYS
210 220 230 240 250
FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS YELPDGQVIT
260 270 280 290 300
IGNERFRCPE ALFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANSVL
310 320 330 340 350
SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL
360 370
STFQQMWISK QEYDESGPGI VHRKCF
Length:376
Mass (Da):41,700
Last modified:June 7, 2004 - v1
Checksum:iC64C33A1674B7886
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti200 – 2001S → T in AAA28321 (PubMed:6405041).Curated
Sequence conflicti213 – 2131I → T in AAA28321 (PubMed:6405041).Curated
Sequence conflicti226 – 2261Q → D in AAA28321 (PubMed:6405041).Curated
Sequence conflicti320 – 3201A → T in AAA28321 (PubMed:6405041).Curated
Sequence conflicti345 – 3451S → L in AAA28321 (PubMed:6405041).Curated
Sequence conflicti369 – 3691G → S in AAA28321 (PubMed:6405041).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA03003. ATFF8.
RefSeqiNP_524367.1. NM_079643.2.
UniGeneiDm.5746.

Genome annotation databases

EnsemblMetazoaiFBtr0083143; FBpp0082597; FBgn0000047.
GeneIDi41885.
KEGGidme:Dmel_CG5178.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA03003. ATFF8.
RefSeqiNP_524367.1. NM_079643.2.
UniGeneiDm.5746.

3D structure databases

ProteinModelPortaliP83967.
SMRiP83967. Positions 7-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66947. 17 interactions.
IntActiP83967. 2 interactions.
MINTiMINT-901261.
STRINGi7227.FBpp0082597.

Proteomic databases

PaxDbiP83967.
PRIDEiP83967.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083143; FBpp0082597; FBgn0000047.
GeneIDi41885.
KEGGidme:Dmel_CG5178.

Organism-specific databases

CTDi41885.
FlyBaseiFBgn0000047. Act88F.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
InParanoidiP83967.
KOiK05692.
OMAiNQMADGE.
OrthoDBiEOG72RMZ1.
PhylomeDBiP83967.

Enzyme and pathway databases

ReactomeiR-DME-190873. Gap junction degradation.
R-DME-196025. Formation of annular gap junctions.
R-DME-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DME-3928662. EPHB-mediated forward signaling.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-445095. Interaction between L1 and Ankyrins.
R-DME-5663213. RHO GTPases Activate WASPs and WAVEs.
SignaLinkiP83967.

Miscellaneous databases

ChiTaRSiAct88F. fly.
GenomeRNAii41885.
PROiP83967.

Gene expression databases

BgeeiP83967.
ExpressionAtlasiP83967. differential.
GenevisibleiP83967. DM.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 302-376, FUNCTION, MUTAGENESIS OF 357-TRP--PHE-376.
  8. "A Drosophila melanogaster model of spinal muscular atrophy reveals a function for SMN in striated muscle."
    Rajendra T.K., Gonsalvez G.B., Walker M.P., Shpargel K.B., Salz H.K., Matera A.G.
    J. Cell Biol. 176:831-841(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  9. "Direct redox regulation of F-actin assembly and disassembly by Mical."
    Hung R.J., Pak C.W., Terman J.R.
    Science 334:1710-1713(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: OXIDATION AT MET-45 AND MET-48.

Entry informationi

Entry nameiACT6_DROME
AccessioniPrimary (citable) accession number: P83967
Secondary accession number(s): P02575, P45893, Q9VF62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2004
Last modified: June 8, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Abnormalities in Act88F-ifm37 flight muscles result from incorporation of the mutant actin isoform into assembling myofibrils.
In Drosophila there are 6 closely related actin genes.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.