ACT1_DROME
ID ACT1_DROME Reviewed; 376 AA.
AC P10987; A4V404; Q24227; Q6YN46; Q9U5X7; Q9W460;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Actin-5C;
DE Flags: Precursor;
GN Name=Act5C; ORFNames=CG4027;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.;
RL Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-84 AND 324-376.
RX PubMed=3123314; DOI=10.1101/gad.1.10.1161;
RA Vigoreaux J.O., Tobin S.L.;
RT "Stage-specific selection of alternative transcriptional initiation sites
RT from the 5C actin gene of Drosophila melanogaster.";
RL Genes Dev. 1:1161-1171(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
RX PubMed=6263481; DOI=10.1016/0092-8674(81)90506-7;
RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.;
RT "The actin genes of Drosophila: protein coding regions are highly conserved
RT but intron positions are not.";
RL Cell 24:107-116(1981).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RX PubMed=3097509; DOI=10.1128/mcb.6.6.2080-2088.1986;
RA Bond B.J., Davidson N.;
RT "The Drosophila melanogaster actin 5C gene uses two transcription
RT initiation sites and three polyadenylation sites to express multiple mRNA
RT species.";
RL Mol. Cell. Biol. 6:2080-2088(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 366-376.
RC STRAIN=Canton-S;
RX PubMed=2896018; DOI=10.1016/0167-4781(88)90070-x;
RA Rao J.P., Zafar R.S., Sodja A.;
RT "Transcriptional activity at the 3' end of the actin gene at 5C on the X
RT chromosome of Drosophila melanogaster.";
RL Biochim. Biophys. Acta 950:30-44(1988).
RN [9]
RP OXIDATION AT MET-45 AND MET-48, AND MUTAGENESIS OF MET-45 AND MET-48.
RX PubMed=22116028; DOI=10.1126/science.1211956;
RA Hung R.J., Pak C.W., Terman J.R.;
RT "Direct redox regulation of F-actin assembly and disassembly by Mical.";
RL Science 334:1710-1713(2011).
RN [10]
RP INTERACTION WITH RAB6.
RX PubMed=22928698; DOI=10.1021/pr300274k;
RA Ye T., Tang W., Zhang X.;
RT "Involvement of Rab6 in the regulation of phagocytosis against virus
RT infection in invertebrates.";
RL J. Proteome Res. 11:4834-4846(2012).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells.
CC -!- FUNCTION: Multiple isoforms are involved in various cellular functions
CC such as cytoskeleton structure, cell mobility, chromosome movement and
CC muscle contraction.
CC -!- SUBUNIT: Interacts with Rab6. {ECO:0000269|PubMed:22928698}.
CC -!- INTERACTION:
CC P10987; Q9U1K1-1: spir; NbExp=6; IntAct=EBI-130188, EBI-3431623;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Oxidation of Met-45 by Mical to form methionine sulfoxide promotes
CC actin filament depolymerization. Methionine sulfoxide is produced
CC stereospecifically, but it is not known whether the (S)-S-oxide or the
CC (R)-S-oxide is produced. {ECO:0000269|PubMed:22116028}.
CC -!- MISCELLANEOUS: In Drosophila there are 6 closely related actin genes.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; K00667; AAA28316.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46098.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09154.1; -; Genomic_DNA.
DR EMBL; AE014298; AAX52479.1; -; Genomic_DNA.
DR EMBL; AE014298; AAX52480.1; -; Genomic_DNA.
DR EMBL; AY089562; AAL90300.1; -; mRNA.
DR EMBL; X06383; CAA29681.1; -; Genomic_DNA.
DR EMBL; X06384; CAB61444.1; -; Genomic_DNA.
DR EMBL; M13587; AAA28315.1; -; Genomic_DNA.
DR EMBL; X07627; CAA30474.1; -; Genomic_DNA.
DR PIR; A28258; A28258.
DR RefSeq; NP_001014725.1; NM_001014725.2.
DR RefSeq; NP_001014726.1; NM_001014726.2.
DR RefSeq; NP_001284915.1; NM_001297986.1.
DR RefSeq; NP_511052.1; NM_078497.4.
DR RefSeq; NP_727048.1; NM_167053.2.
DR PDB; 2HF3; X-ray; 1.80 A; A=3-376.
DR PDB; 2HF4; X-ray; 1.80 A; A=3-376.
DR PDB; 3EKS; X-ray; 1.80 A; A=2-376.
DR PDB; 3EKU; X-ray; 2.50 A; A=2-376.
DR PDB; 3EL2; X-ray; 2.50 A; A=2-376.
DR PDB; 3MMV; X-ray; 2.80 A; A=3-376.
DR PDB; 3MN6; X-ray; 2.00 A; A/F/K=3-376.
DR PDB; 3MN7; X-ray; 2.00 A; A=3-376.
DR PDB; 3MN9; X-ray; 2.00 A; A=3-376.
DR PDB; 4JHD; X-ray; 2.91 A; A/B/D/E=1-376.
DR PDB; 4M63; X-ray; 2.75 A; C/D/E=1-376.
DR PDB; 4RWT; X-ray; 2.98 A; A/B=1-376.
DR PDB; 5WFN; X-ray; 3.00 A; A/B=1-376.
DR PDBsum; 2HF3; -.
DR PDBsum; 2HF4; -.
DR PDBsum; 3EKS; -.
DR PDBsum; 3EKU; -.
DR PDBsum; 3EL2; -.
DR PDBsum; 3MMV; -.
DR PDBsum; 3MN6; -.
DR PDBsum; 3MN7; -.
DR PDBsum; 3MN9; -.
DR PDBsum; 4JHD; -.
DR PDBsum; 4M63; -.
DR PDBsum; 4RWT; -.
DR PDBsum; 5WFN; -.
DR AlphaFoldDB; P10987; -.
DR SMR; P10987; -.
DR BioGRID; 58020; 92.
DR DIP; DIP-18961N; -.
DR ELM; P10987; -.
DR IntAct; P10987; 11.
DR MINT; P10987; -.
DR STRING; 7227.FBpp0100124; -.
DR MetOSite; P10987; -.
DR PaxDb; P10987; -.
DR PRIDE; P10987; -.
DR EnsemblMetazoa; FBtr0070822; FBpp0070787; FBgn0000042.
DR EnsemblMetazoa; FBtr0070823; FBpp0070788; FBgn0000042.
DR EnsemblMetazoa; FBtr0100662; FBpp0100124; FBgn0000042.
DR EnsemblMetazoa; FBtr0100663; FBpp0100125; FBgn0000042.
DR EnsemblMetazoa; FBtr0345894; FBpp0311818; FBgn0000042.
DR GeneID; 31521; -.
DR KEGG; dme:Dmel_CG4027; -.
DR CTD; 31521; -.
DR FlyBase; FBgn0000042; Act5C.
DR VEuPathDB; VectorBase:FBgn0000042; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P10987; -.
DR OMA; KCDESIC; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P10987; -.
DR Reactome; R-DME-190873; Gap junction degradation.
DR Reactome; R-DME-196025; Formation of annular gap junctions.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-446353; Cell-extracellular matrix interactions.
DR Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-5689603; UCH proteinases.
DR Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-9035034; RHOF GTPase cycle.
DR SignaLink; P10987; -.
DR BioGRID-ORCS; 31521; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Act5C; fly.
DR EvolutionaryTrace; P10987; -.
DR GenomeRNAi; 31521; -.
DR PRO; PR:P10987; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000042; Expressed in cleaving embryo and 38 other tissues.
DR ExpressionAtlas; P10987; baseline and differential.
DR Genevisible; P10987; DM.
DR GO; GO:0035060; C:brahma complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031011; C:Ino80 complex; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IC:FlyBase.
DR GO; GO:0032507; P:maintenance of protein location in cell; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IEP:FlyBase.
DR GO; GO:0035148; P:tube formation; IGI:FlyBase.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW Methylation; Nucleotide-binding; Oxidation; Reference proteome.
FT PROPEP 1..2
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000656"
FT CHAIN 3..376
FT /note="Actin-5C"
FT /id="PRO_0000000657"
FT MOD_RES 3
FT /note="N-acetylaspartate"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:22116028"
FT MOD_RES 48
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:22116028"
FT MOD_RES 74
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P02572"
FT MUTAGEN 45
FT /note="M->L: Abolishes formation of methionine-sulfoxide
FT and subsequent depolymerization."
FT /evidence="ECO:0000269|PubMed:22116028"
FT MUTAGEN 48
FT /note="M->L: Depolymerizes in the presence of Mical."
FT /evidence="ECO:0000269|PubMed:22116028"
FT CONFLICT 264
FT /note="Q -> H (in Ref. 1; AAA28316)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="A -> S (in Ref. 1; AAA28316)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="L -> S (in Ref. 1; AAA28316)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="I -> T (in Ref. 1; AAA28316)"
FT /evidence="ECO:0000305"
FT CONFLICT 366..367
FT /note="SG -> AW (in Ref. 8; CAA30474)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3MN6"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4RWT"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3EKS"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3MMV"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2HF3"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4M63"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:2HF3"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:2HF3"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 351..356
FT /evidence="ECO:0007829|PDB:2HF3"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:2HF3"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:2HF3"
SQ SEQUENCE 376 AA; 41822 MW; BDAF13C191BB1BBC CRC64;
MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS
YELPDGQVIT IGNERFRCPE ALFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
QEYDESGPSI VHRKCF
