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Protein

Actin, larval muscle

Gene

Act79B

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 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.
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
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiP02574.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, larval muscle
Alternative name(s):
Actin-79B
Gene namesi
Name:Act79B
ORF Names:CG7478
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0000045. Act79B.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000662
Chaini3 – 376374Actin, larval musclePRO_0000000663Add
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

PaxDbiP02574.
PRIDEiP02574.

Expressioni

Developmental stagei

Expressed during larval stages and at a lower level in pupae.1 Publication

Gene expression databases

BgeeiP02574.
ExpressionAtlasiP02574. differential.
GenevisibleiP02574. DM.

Interactioni

Protein-protein interaction databases

BioGridi65684. 27 interactions.
DIPiDIP-23587N.
MINTiMINT-773935.
STRINGi7227.FBpp0078131.

Structurei

3D structure databases

ProteinModelPortaliP02574.
SMRiP02574. Positions 3-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
InParanoidiP02574.
KOiK05692.
OMAiKSKMCDD.
OrthoDBiEOG72RMZ1.
PhylomeDBiP02574.

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.

P02574-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDEEASALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ
60 70 80 90 100
KDCYVGDEAQ SKRGILSLKY PIEHGIITNW DDMEKVWHHT FYNELRVAPE
110 120 130 140 150
EHPVLLTEAP LNPKANREKM TQIMFETFNS PAMYVAIQAV LSLYASGRTT
160 170 180 190 200
GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS
210 220 230 240 250
FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS YELPDGQVIT
260 270 280 290 300
IGNERFRTPE ALFQPSFLGM ESCGIHETVY QSIMKCDVDI RKDLYANNVL
310 320 330 340 350
SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL
360 370
STFQQMWISK QEYDESGPGI VHRKCF
Length:376
Mass (Da):41,787
Last modified:February 21, 2001 - v2
Checksum:iD08BB1B42DE86B94
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851D → H in AAA28318 (PubMed:6405041).Curated
Sequence conflicti326 – 3261I → M in AAA28317 (PubMed:6405041).Curated
Sequence conflicti326 – 3261I → M in AAA28318 (PubMed:6405041).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18827, M18828 Genomic DNA. Translation: AAA28317.1.
M18829 Genomic DNA. Translation: AAA28318.1.
AE014296 Genomic DNA. Translation: AAF51800.1.
AY118735 mRNA. Translation: AAM50595.1.
PIRiA03002. ATFF7.
RefSeqiNP_001262200.1. NM_001275271.1.
NP_524210.1. NM_079486.4.
UniGeneiDm.5748.

Genome annotation databases

EnsemblMetazoaiFBtr0078478; FBpp0078131; FBgn0000045.
FBtr0334090; FBpp0306215; FBgn0000045.
GeneIDi40444.
KEGGidme:Dmel_CG7478.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18827, M18828 Genomic DNA. Translation: AAA28317.1.
M18829 Genomic DNA. Translation: AAA28318.1.
AE014296 Genomic DNA. Translation: AAF51800.1.
AY118735 mRNA. Translation: AAM50595.1.
PIRiA03002. ATFF7.
RefSeqiNP_001262200.1. NM_001275271.1.
NP_524210.1. NM_079486.4.
UniGeneiDm.5748.

3D structure databases

ProteinModelPortaliP02574.
SMRiP02574. Positions 3-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65684. 27 interactions.
DIPiDIP-23587N.
MINTiMINT-773935.
STRINGi7227.FBpp0078131.

Proteomic databases

PaxDbiP02574.
PRIDEiP02574.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078478; FBpp0078131; FBgn0000045.
FBtr0334090; FBpp0306215; FBgn0000045.
GeneIDi40444.
KEGGidme:Dmel_CG7478.

Organism-specific databases

CTDi40444.
FlyBaseiFBgn0000045. Act79B.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
InParanoidiP02574.
KOiK05692.
OMAiKSKMCDD.
OrthoDBiEOG72RMZ1.
PhylomeDBiP02574.

Enzyme and pathway databases

SignaLinkiP02574.

Miscellaneous databases

ChiTaRSiAct79B. fly.
GenomeRNAii40444.
NextBioi818820.
PROiP02574.

Gene expression databases

BgeeiP02574.
ExpressionAtlasiP02574. differential.
GenevisibleiP02574. 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. "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.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. "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 nameiACT4_DROME
AccessioniPrimary (citable) accession number: P02574
Secondary accession number(s): Q540X7, Q9VNW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 21, 2001
Last modified: May 11, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

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.