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Reviewed, UniProtKB/Swiss-Prot P02574 (ACT4_DROME)

Last modified July 22, 2008. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Actin, larval muscle
Alternative name(s):
    Actin-79B
Gene names
Name: Act79B
ORF Names: CG7478
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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.

Developmental stage

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

Miscellaneous

In Drosophila there are 6 closely related actin genes.

Sequence similarities

Belongs to the actin family.

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Ontologies

Keywords

   Cellular componentCytoplasm
Cytoskeleton
   LigandATP-binding
Nucleotide-binding
   Molecular functionMuscle protein
Structural protein
   PTMAcetylation
   Technical termComplete proteome

Gene Ontology (GO)

None. [Check GOA]

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Propeptide1 – 22Removed in mature form By similarity
Chain3 – 376374Actin, larval muscle

Amino acid modifications

Modified residue31N-acetylaspartate By similarity

Experimental info

Sequence conflict1851D → H in AAA28318. Ref.1
Sequence conflict3261I → M in AAA28317 and AAA28318. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P02574-1 [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: D08BB1B42DE86B94

FASTA37641,787
        10         20         30         40         50         60 
MCDEEASALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDCYVGDEAQ 

        70         80         90        100        110        120 
SKRGILSLKY PIEHGIITNW DDMEKVWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM 

       130        140        150        160        170        180 
TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD 

       190        200        210        220        230        240 
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS 

       250        260        270        280        290        300 
YELPDGQVIT IGNERFRTPE ALFQPSFLGM ESCGIHETVY QSIMKCDVDI RKDLYANNVL 

       310        320        330        340        350        360 
SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK 

       370 
QEYDESGPGI VHRKCF

« Hide

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References

« Hide 'large scale' references
[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: 6405041] [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. expand/collapse author list , 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.
[3]"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. expand/collapse author list , 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.
[4]"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: Head.

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Cross-references

Sequence databases

M18827, M18828 Genomic DNA. Translation: AAA28317.1.
M18829 Genomic DNA. Translation: AAA28318.1.
AE014296 Genomic DNA. Translation: AAF51800.1.
AY118735 mRNA. Translation: AAM50595.1.
PIRATFF7. A03002.
RefSeqNP_524210.1.
UniGeneDm.5748

3D structure databases

HSSPHSSP built from PDB template 2BTF based on UniProtKB P02570.
SMRP02574. Positions 5-372.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:23587N.

Genome annotation databases

EnsemblCG7478. Drosophila melanogaster. [Contig view]
GeneID40444.
KEGGdme:Dmel_CG7478.
NMPDRfig|7227.3.peg.11022.

Organism-specific databases

FlyBaseFBgn0000045. Act79B.

Phylogenomic databases

HOGENOMP02574.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-017813-MON.

Gene expression databases

ArrayExpressP02574.
GermOnlineCG7478. Drosophila melanogaster.

Family and domain databases

InterProIPR004001. Actin_CS.
IPR004000. Actin_like.
[Graphical view]
PANTHERPTHR11937. Actin_like. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
PRINTSPR00190. ACTIN.
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProDomP02574.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameACT4_DROME
AccessionPrimary (citable) accession number: P02574
Secondary accession number(s): Q540X7, Q9VNW5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 21, 2001
Last modified: July 22, 2008
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents