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Protein

Actin-87E

Gene

Act87E

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.1 Publication
Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction.1 Publication

GO - Molecular functioni

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

GO - Biological processi

  • cytoskeleton organization Source: FlyBase
  • histone acetylation Source: FlyBase
  • histone exchange Source: FlyBase
Complete GO annotation...

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.
SignaLinkiP10981.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-87E
Gene namesi
Name:Act87E
ORF Names:CG18290
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0000046. Act87E.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: FlyBase
  • cytoplasm Source: UniProtKB-KW
  • lipid particle Source: FlyBase
  • NuA4 histone acetyltransferase complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000664
Chaini3 – 376374Actin-87EPRO_0000000665Add
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

PaxDbiP10981.
PRIDEiP10981.

Expressioni

Gene expression databases

BgeeiP10981.
GenevisibleiP10981. DM.

Interactioni

Subunit structurei

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-1.1 Publication

Protein-protein interaction databases

BioGridi71541. 12 interactions.
DIPiDIP-18091N.
IntActiP10981. 3 interactions.
MINTiMINT-899452.
STRINGi7227.FBpp0082253.

Structurei

3D structure databases

ProteinModelPortaliP10981.
SMRiP10981. Positions 7-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
InParanoidiP10981.
KOiK05692.
OMAiPRRDHEY.
OrthoDBiEOG72RMZ1.
PhylomeDBiP10981.

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.

P10981-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ
60 70 80 90 100
KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE
110 120 130 140 150
EHPVLLTEAP LNPKANREKM TQIMFETFNA 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
IGNERFRCPE SLFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANIVM
310 320 330 340 350
SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL
360 370
STFQQMWISK QEYDESGPGI VHRKCF
Length:376
Mass (Da):41,802
Last modified:July 1, 1989 - v1
Checksum:i60252541882B0A7F
GO

Sequence cautioni

The sequence AAM29410.1 differs from that shown. Reason: Erroneous translation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS04538.
RefSeqiNP_001287314.1. NM_001300385.1.
NP_477091.1. NM_057743.5.
NP_731812.1. NM_169525.2.
UniGeneiDm.4869.

Genome annotation databases

EnsemblMetazoaiFBtr0082785; FBpp0082253; FBgn0000046.
FBtr0082786; FBpp0082254; FBgn0000046.
FBtr0346242; FBpp0312019; FBgn0000046.
GeneIDi48632.
KEGGidme:Dmel_CG18290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS04538.
RefSeqiNP_001287314.1. NM_001300385.1.
NP_477091.1. NM_057743.5.
NP_731812.1. NM_169525.2.
UniGeneiDm.4869.

3D structure databases

ProteinModelPortaliP10981.
SMRiP10981. Positions 7-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi71541. 12 interactions.
DIPiDIP-18091N.
IntActiP10981. 3 interactions.
MINTiMINT-899452.
STRINGi7227.FBpp0082253.

Proteomic databases

PaxDbiP10981.
PRIDEiP10981.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082785; FBpp0082253; FBgn0000046.
FBtr0082786; FBpp0082254; FBgn0000046.
FBtr0346242; FBpp0312019; FBgn0000046.
GeneIDi48632.
KEGGidme:Dmel_CG18290.

Organism-specific databases

CTDi48632.
FlyBaseiFBgn0000046. Act87E.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
InParanoidiP10981.
KOiK05692.
OMAiPRRDHEY.
OrthoDBiEOG72RMZ1.
PhylomeDBiP10981.

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.
SignaLinkiP10981.

Miscellaneous databases

GenomeRNAii48632.
PROiP10981.

Gene expression databases

BgeeiP10981.
GenevisibleiP10981. 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. "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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. 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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TIP60 COMPLEX, FUNCTION.
  8. "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 nameiACT5_DROME
AccessioniPrimary (citable) accession number: P10981
Secondary accession number(s): A4V2T6
, Q5U0U0, Q8MZ23, Q9VFU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 6, 2016
This is version 140 of the entry and version 1 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.