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Protein

Actin-5C

Gene

Act5C

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.
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
  • inter-male aggressive behavior Source: FlyBase
  • maintenance of protein location in cell Source: FlyBase
  • mitotic cytokinesis Source: FlyBase
  • mushroom body development Source: FlyBase
  • phagocytosis Source: FlyBase
  • sperm individualization Source: FlyBase
  • tube formation Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_280501. Formation of annular gap junctions.
REACT_282671. Regulation of actin dynamics for phagocytic cup formation.
REACT_287092. Factors involved in megakaryocyte development and platelet production.
REACT_293536. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_303345. EPHB-mediated forward signaling.
REACT_310206. Translocation of GLUT4 to the plasma membrane.
REACT_320402. Gap junction degradation.
REACT_331500. EPH-ephrin mediated repulsion of cells.
REACT_334212. Folding of actin by CCT/TriC.
REACT_346571. VEGFA-VEGFR2 Pathway.
REACT_351101. Adherens junctions interactions.
REACT_359184. RHO GTPases Activate WASPs and WAVEs.
SignaLinkiP10987.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-5C
Gene namesi
Name:Act5C
ORF Names:CG4027
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000042. Act5C.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: FlyBase
  • cytoplasm Source: UniProtKB-KW
  • Ino80 complex Source: FlyBase
  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451M → L: Abolishes formation of methionine-sulfoxide and subsequent depolymerization. 1 Publication
Mutagenesisi48 – 481M → L: Depolymerizes in the presence of Mical. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000656
Chaini3 – 376374Actin-5CPRO_0000000657Add
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

PaxDbiP10987.
PRIDEiP10987.

Expressioni

Gene expression databases

BgeeiP10987.
GenevisibleiP10987. DM.

Interactioni

Subunit structurei

Interacts with Rab6.1 Publication

Protein-protein interaction databases

BioGridi58020. 61 interactions.
DIPiDIP-18961N.
IntActiP10987. 10 interactions.
MINTiMINT-799448.
STRINGi7227.FBpp0100124.

Structurei

Secondary structure

1
376
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124Combined sources
Beta strandi15 – 228Combined sources
Beta strandi25 – 273Combined sources
Beta strandi29 – 346Combined sources
Beta strandi36 – 394Combined sources
Beta strandi46 – 483Combined sources
Beta strandi54 – 563Combined sources
Helixi57 – 615Combined sources
Helixi63 – 653Combined sources
Beta strandi66 – 694Combined sources
Turni71 – 744Combined sources
Beta strandi76 – 783Combined sources
Helixi80 – 9213Combined sources
Turni93 – 953Combined sources
Helixi99 – 1013Combined sources
Beta strandi104 – 1085Combined sources
Helixi114 – 12613Combined sources
Beta strandi131 – 1377Combined sources
Helixi138 – 1458Combined sources
Beta strandi149 – 1568Combined sources
Beta strandi161 – 1677Combined sources
Helixi173 – 1753Combined sources
Beta strandi177 – 1804Combined sources
Helixi183 – 19715Combined sources
Helixi204 – 21714Combined sources
Helixi224 – 23310Combined sources
Beta strandi239 – 2424Combined sources
Beta strandi248 – 2514Combined sources
Helixi254 – 2607Combined sources
Turni261 – 2633Combined sources
Helixi265 – 2684Combined sources
Helixi275 – 28410Combined sources
Helixi288 – 2903Combined sources
Helixi291 – 2955Combined sources
Beta strandi298 – 3025Combined sources
Helixi303 – 3053Combined sources
Helixi310 – 32112Combined sources
Helixi336 – 3383Combined sources
Helixi339 – 34810Combined sources
Helixi351 – 3566Combined sources
Beta strandi357 – 3593Combined sources
Helixi360 – 3667Combined sources
Helixi370 – 3745Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP10987.
SMRiP10987. Positions 3-376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10987.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiCOG5277.
InParanoidiP10987.
KOiK05692.
OMAiASMLQMW.
OrthoDBiEOG72RMZ1.
PhylomeDBiP10987.

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.

P10987-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ
60 70 80 90 100
KDSYVGDEAQ SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE
110 120 130 140 150
EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT
160 170 180 190 200
GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS
210 220 230 240 250
FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS YELPDGQVIT
260 270 280 290 300
IGNERFRCPE ALFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL
310 320 330 340 350
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL
360 370
STFQQMWISK QEYDESGPSI VHRKCF
Length:376
Mass (Da):41,822
Last modified:December 1, 2000 - v4
Checksum:iBDAF13C191BB1BBC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti264 – 2641Q → H in AAA28316 (Ref. 1) Curated
Sequence conflicti272 – 2721A → S in AAA28316 (Ref. 1) Curated
Sequence conflicti350 – 3501L → S in AAA28316 (Ref. 1) Curated
Sequence conflicti358 – 3581I → T in AAA28316 (Ref. 1) Curated
Sequence conflicti366 – 3672SG → AW in CAA30474 (PubMed:2896018).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA28258.
RefSeqiNP_001014725.1. NM_001014725.2.
NP_001014726.1. NM_001014726.2.
NP_001284915.1. NM_001297986.1.
NP_511052.1. NM_078497.4.
NP_727048.1. NM_167053.2.
UniGeneiDm.2951.

Genome annotation databases

EnsemblMetazoaiFBtr0070822; FBpp0070787; FBgn0000042.
FBtr0070823; FBpp0070788; FBgn0000042.
FBtr0100662; FBpp0100124; FBgn0000042.
FBtr0100663; FBpp0100125; FBgn0000042.
FBtr0345894; FBpp0311818; FBgn0000042.
GeneIDi31521.
KEGGidme:Dmel_CG4027.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA28258.
RefSeqiNP_001014725.1. NM_001014725.2.
NP_001014726.1. NM_001014726.2.
NP_001284915.1. NM_001297986.1.
NP_511052.1. NM_078497.4.
NP_727048.1. NM_167053.2.
UniGeneiDm.2951.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP10987.
SMRiP10987. Positions 3-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58020. 61 interactions.
DIPiDIP-18961N.
IntActiP10987. 10 interactions.
MINTiMINT-799448.
STRINGi7227.FBpp0100124.

Proteomic databases

PaxDbiP10987.
PRIDEiP10987.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070822; FBpp0070787; FBgn0000042.
FBtr0070823; FBpp0070788; FBgn0000042.
FBtr0100662; FBpp0100124; FBgn0000042.
FBtr0100663; FBpp0100125; FBgn0000042.
FBtr0345894; FBpp0311818; FBgn0000042.
GeneIDi31521.
KEGGidme:Dmel_CG4027.

Organism-specific databases

CTDi31521.
FlyBaseiFBgn0000042. Act5C.

Phylogenomic databases

eggNOGiCOG5277.
InParanoidiP10987.
KOiK05692.
OMAiASMLQMW.
OrthoDBiEOG72RMZ1.
PhylomeDBiP10987.

Enzyme and pathway databases

ReactomeiREACT_280501. Formation of annular gap junctions.
REACT_282671. Regulation of actin dynamics for phagocytic cup formation.
REACT_287092. Factors involved in megakaryocyte development and platelet production.
REACT_293536. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_303345. EPHB-mediated forward signaling.
REACT_310206. Translocation of GLUT4 to the plasma membrane.
REACT_320402. Gap junction degradation.
REACT_331500. EPH-ephrin mediated repulsion of cells.
REACT_334212. Folding of actin by CCT/TriC.
REACT_346571. VEGFA-VEGFR2 Pathway.
REACT_351101. Adherens junctions interactions.
REACT_359184. RHO GTPases Activate WASPs and WAVEs.
SignaLinkiP10987.

Miscellaneous databases

ChiTaRSiAct5C. fly.
EvolutionaryTraceiP10987.
GenomeRNAii31521.
NextBioi774032.
PROiP10987.

Gene expression databases

BgeeiP10987.
GenevisibleiP10987. 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 (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.
    , 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: 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.

Entry informationi

Entry nameiACT1_DROME
AccessioniPrimary (citable) accession number: P10987
Secondary accession number(s): A4V404
, Q24227, Q6YN46, Q9U5X7, Q9W460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 2000
Last modified: June 24, 2015
This is version 150 of the entry and version 4 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.