Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P10987 (ACT1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subunit structure

Interacts with Rab6. Ref.10

Subcellular location

Cytoplasmcytoskeleton.

Post-translational modification

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.

Miscellaneous

In Drosophila there are 6 closely related actin genes.

Sequence similarities

Belongs to the actin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Oxidation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytoskeleton organization

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

inter-male aggressive behavior

Inferred from mutant phenotype PubMed 19519879. Source: FlyBase

maintenance of protein location in cell

Inferred from mutant phenotype PubMed 16174742. Source: FlyBase

mitotic cytokinesis

Inferred from mutant phenotype PubMed 15380073PubMed 15547975PubMed 16174742. Source: FlyBase

mushroom body development

Inferred from mutant phenotype PubMed 19519879. Source: FlyBase

phagocytosis

Inferred from mutant phenotype PubMed 16336044. Source: FlyBase

sperm individualization

Inferred from expression pattern PubMed 12642486. Source: FlyBase

   Cellular_componentIno80 complex

Inferred from direct assay PubMed 16618800. Source: FlyBase

actin filament

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

lipid particle

Inferred from direct assay PubMed 16543254. Source: FlyBase

microtubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of cytoskeleton

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22Removed in mature form By similarity
PRO_0000000656
Chain3 – 376374Actin-5C
PRO_0000000657

Amino acid modifications

Modified residue31N-acetylaspartate By similarity
Modified residue451Methionine sulfoxide
Modified residue481Methionine sulfoxide

Experimental info

Mutagenesis451M → L: Abolishes formation of methionine-sulfoxide and subsequent depolymerization. Ref.9
Mutagenesis481M → L: Depolymerizes in the presence of Mical. Ref.9
Sequence conflict2641Q → H in AAA28316. Ref.1
Sequence conflict2721A → S in AAA28316. Ref.1
Sequence conflict3501L → S in AAA28316. Ref.1
Sequence conflict3581I → T in AAA28316. Ref.1
Sequence conflict366 – 3672SG → AW in CAA30474. Ref.8

Secondary structure

............................................................................. 376
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10987 [UniParc].

Last modified December 1, 2000. Version 4.
Checksum: BDAF13C191BB1BBC

FASTA37641,822
        10         20         30         40         50         60 
MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ 

        70         80         90        100        110        120 
SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM 

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

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

       250        260        270        280        290        300 
YELPDGQVIT IGNERFRCPE ALFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL 

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

       370 
QEYDESGPSI VHRKCF 

« Hide

References

« Hide 'large scale' references
[1]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].
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Stage-specific selection of alternative transcriptional initiation sites from the 5C actin gene of Drosophila melanogaster."
Vigoreaux J.O., Tobin S.L.
Genes Dev. 1:1161-1171(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-84 AND 324-376.
[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 1-75.
[7]"The Drosophila melanogaster actin 5C gene uses two transcription initiation sites and three polyadenylation sites to express multiple mRNA species."
Bond B.J., Davidson N.
Mol. Cell. Biol. 6:2080-2088(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
[8]"Transcriptional activity at the 3' end of the actin gene at 5C on the X chromosome of Drosophila melanogaster."
Rao J.P., Zafar R.S., Sodja A.
Biochim. Biophys. Acta 950:30-44(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 366-376.
Strain: Canton-S.
[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, MUTAGENESIS OF MET-45 AND MET-48.
[10]"Involvement of Rab6 in the regulation of phagocytosis against virus infection in invertebrates."
Ye T., Tang W., Zhang X.
J. Proteome Res. 11:4834-4846(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K00667 Genomic DNA. Translation: AAA28316.1.
AE014298 Genomic DNA. Translation: AAF46098.1.
AE014298 Genomic DNA. Translation: AAN09154.1.
AE014298 Genomic DNA. Translation: AAX52479.1.
AE014298 Genomic DNA. Translation: AAX52480.1.
AY089562 mRNA. Translation: AAL90300.1.
X06383 Genomic DNA. Translation: CAA29681.1.
X06384 Genomic DNA. Translation: CAB61444.1.
M13587 Genomic DNA. Translation: AAA28315.1.
X07627 Genomic DNA. Translation: CAA30474.1.
PIRA28258.
RefSeqNP_001014725.1. NM_001014725.2.
NP_001014726.1. NM_001014726.2.
NP_511052.1. NM_078497.3.
NP_727048.1. NM_167053.2.
UniGeneDm.2951.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N58model-A1-376[»]
2HF3X-ray1.80A3-376[»]
2HF4X-ray1.80A3-376[»]
3EKSX-ray1.80A2-376[»]
3EKUX-ray2.50A2-376[»]
3EL2X-ray2.50A2-376[»]
3MMVX-ray2.80A3-376[»]
3MN6X-ray2.00A/F/K3-376[»]
3MN7X-ray2.00A3-376[»]
3MN9X-ray2.00A3-376[»]
4JHDX-ray2.91A/B/D/E1-376[»]
4M63X-ray2.75C/D/E1-376[»]
ProteinModelPortalP10987.
SMRP10987. Positions 3-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58020. 61 interactions.
DIPDIP-18961N.
IntActP10987. 10 interactions.
MINTMINT-799448.

Proteomic databases

PaxDbP10987.
PRIDEP10987.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070822; FBpp0070787; FBgn0000042.
FBtr0070823; FBpp0070788; FBgn0000042.
FBtr0100662; FBpp0100124; FBgn0000042.
FBtr0100663; FBpp0100125; FBgn0000042.
GeneID31521.
KEGGdme:Dmel_CG4027.

Organism-specific databases

CTD31521.
FlyBaseFBgn0000042. Act5C.

Phylogenomic databases

eggNOGCOG5277.
GeneTreeENSGT00710000106384.
InParanoidP10987.
KOK05692.
OMADARAPIM.
OrthoDBEOG72RMZ1.
PhylomeDBP10987.

Enzyme and pathway databases

SignaLinkP10987.

Gene expression databases

BgeeP10987.

Family and domain databases

InterProIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 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]
ProtoNetSearch...

Other

ChiTaRSAct5C. drosophila.
EvolutionaryTraceP10987.
GenomeRNAi31521.
NextBio774032.

Entry information

Entry nameACT1_DROME
AccessionPrimary (citable) accession number: P10987
Secondary accession number(s): A4V404 expand/collapse secondary AC list , Q24227, Q6YN46, Q9U5X7, Q9W460
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

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