ARC1_DROME
ID ARC1_DROME Reviewed; 254 AA.
AC Q7K1U0;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Activity-regulated cytoskeleton associated protein 1 {ECO:0000303|PubMed:29328915};
DE Short=dArc1 {ECO:0000303|PubMed:29328915};
GN Name=Arc1 {ECO:0000303|PubMed:29328915, ECO:0000312|FlyBase:FBgn0033926};
GN ORFNames=CG12505 {ECO:0000312|FlyBase:FBgn0033926};
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=26209258; DOI=10.1016/j.ydbio.2015.07.021;
RA Mosher J., Zhang W., Blumhagen R.Z., D'Alessandro A., Nemkov T.,
RA Hansen K.C., Hesselberth J.R., Reis T.;
RT "Coordination between Drosophila Arc1 and a specific population of brain
RT neurons regulates organismal fat.";
RL Dev. Biol. 405:280-290(2015).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, RNA-BINDING, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29328915; DOI=10.1016/j.cell.2017.12.022;
RA Ashley J., Cordy B., Lucia D., Fradkin L.G., Budnik V., Thomson T.;
RT "Retrovirus-like Gag protein Arc1 binds RNA and traffics across synaptic
RT boutons.";
RL Cell 172:262-274(2018).
RN [6]
RP DOMAIN.
RX PubMed=29328916; DOI=10.1016/j.cell.2017.12.024;
RA Pastuzyn E.D., Day C.E., Kearns R.B., Kyrke-Smith M., Taibi A.V.,
RA McCormick J., Yoder N., Belnap D.M., Erlendsson S., Morado D.R.,
RA Briggs J.A.G., Feschotte C., Shepherd J.D.;
RT "The neuronal gene Arc encodes a repurposed retrotransposon Gag protein
RT that mediates intercellular RNA transfer.";
RL Cell 172:275-288(2018).
CC -!- FUNCTION: Master regulator of synaptic plasticity that self-assembles
CC into virion-like capsids that encapsulate RNAs and mediate
CC intercellular RNA transfer from motorneurons to muscles
CC (PubMed:29328915). Arc1 protein is released from motorneurons in
CC extracellular vesicles that mediate the transfer of Arc1 mRNA into
CC muscle cells, where Arc1 mRNA can undergo activity-dependent
CC translation (PubMed:29328915). Intercellular transfer od Arc1 mRNA is
CC required for synaptic plasticity at the neuromuscular junction
CC (PubMed:29328915). May play a role in energy balance: required for
CC regulation of body fat by a specific population of brain neurons, named
CC E347, that are necessary and sufficient for proper body fat storage
CC (PubMed:26209258). {ECO:0000269|PubMed:26209258,
CC ECO:0000269|PubMed:29328915}.
CC -!- SUBUNIT: Homooligomer; homooligomerizes into virion-like capsids.
CC {ECO:0000250|UniProtKB:Q63053}.
CC -!- INTERACTION:
CC Q7K1U0; Q7K1U0: Arc1; NbExp=4; IntAct=EBI-103780, EBI-103780;
CC Q7K1U0; Q7JV70: Arc2; NbExp=4; IntAct=EBI-103780, EBI-172533;
CC -!- SUBCELLULAR LOCATION: Extracellular vesicle membrane
CC {ECO:0000269|PubMed:29328915}. Synapse {ECO:0000269|PubMed:29328915}.
CC Note=Forms virion-like extracellular vesicles that are released from
CC neurons (PubMed:29328915). Present at pre- and postsynaptic sites of
CC the neuromuscular junction (PubMed:29328915).
CC {ECO:0000269|PubMed:29328915}.
CC -!- TISSUE SPECIFICITY: Expressed in a specific population of brain
CC neurons, named E347, that are necessary and sufficient for proper body
CC fat storage. {ECO:0000269|PubMed:26209258}.
CC -!- INDUCTION: Up-regulated following stimulation of E347 brain neurons.
CC {ECO:0000269|PubMed:26209258}.
CC -!- DOMAIN: The protein is evolutionarily related to retrotransposon Gag
CC proteins (PubMed:29328915, PubMed:29328916). It contains structural
CC elements found within viral Gag polyproteins originated from the
CC Ty3/gypsy retrotransposon family and retains the ability to form
CC virion-like capsid structures that can mediate mRNA transfer between
CC cells (PubMed:29328915, PubMed:29328916). Tetrapod and fly Arc protein-
CC coding genes originated independently from distinct lineages of
CC Ty3/gypsy retrotransposons (PubMed:29328916).
CC {ECO:0000269|PubMed:29328915, ECO:0000269|PubMed:29328916}.
CC -!- DISRUPTION PHENOTYPE: Strong reduction in the number of synaptic
CC boutons at neuromuscular junction in third-instar larvae.
CC {ECO:0000269|PubMed:29328915}.
CC -!- SIMILARITY: Belongs to the ARC/ARG3.1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE013599; AAF58256.1; -; Genomic_DNA.
DR EMBL; AY061464; AAL29012.1; -; mRNA.
DR RefSeq; NP_610955.1; NM_137111.3.
DR PDB; 6S7X; X-ray; 1.70 A; A/B=39-205.
DR PDB; 6S7Y; X-ray; 2.30 A; A/B=39-205.
DR PDB; 6SID; X-ray; 1.05 A; A=123-208.
DR PDB; 6TAP; EM; 3.50 A; A/B/C/D/E=1-254.
DR PDB; 6TAR; EM; 2.80 A; A/B/C/D/E=1-254.
DR PDB; 6TAS; EM; 2.75 A; A/B/C/D/E/F/G/H=1-254.
DR PDBsum; 6S7X; -.
DR PDBsum; 6S7Y; -.
DR PDBsum; 6SID; -.
DR PDBsum; 6TAP; -.
DR PDBsum; 6TAR; -.
DR PDBsum; 6TAS; -.
DR AlphaFoldDB; Q7K1U0; -.
DR SMR; Q7K1U0; -.
DR DIP; DIP-20738N; -.
DR IntAct; Q7K1U0; 3.
DR STRING; 7227.FBpp0086687; -.
DR PaxDb; Q7K1U0; -.
DR PRIDE; Q7K1U0; -.
DR DNASU; 36595; -.
DR EnsemblMetazoa; FBtr0087560; FBpp0086687; FBgn0033926.
DR GeneID; 36595; -.
DR KEGG; dme:Dmel_CG12505; -.
DR UCSC; CG12505-RA; d. melanogaster.
DR CTD; 36595; -.
DR FlyBase; FBgn0033926; Arc1.
DR VEuPathDB; VectorBase:FBgn0033926; -.
DR eggNOG; ENOG502SQYT; Eukaryota.
DR GeneTree; ENSGT00540000073579; -.
DR HOGENOM; CLU_097305_0_0_1; -.
DR InParanoid; Q7K1U0; -.
DR OMA; YRKHITR; -.
DR OrthoDB; 1172550at2759; -.
DR PhylomeDB; Q7K1U0; -.
DR SignaLink; Q7K1U0; -.
DR BioGRID-ORCS; 36595; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Arc1; fly.
DR GenomeRNAi; 36595; -.
DR PRO; PR:Q7K1U0; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033926; Expressed in adult midgut (Drosophila) and 25 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0098975; C:postsynapse of neuromuscular junction; IDA:UniProtKB.
DR GO; GO:0030017; C:sarcomere; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0042595; P:behavioral response to starvation; IDA:FlyBase.
DR GO; GO:0051028; P:mRNA transport; IDA:UniProtKB.
DR GO; GO:0003012; P:muscle system process; IGI:FlyBase.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IDA:UniProtKB.
DR GO; GO:0110077; P:vesicle-mediated intercellular transport; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Reference proteome; RNA-binding; Synapse;
KW Transport.
FT CHAIN 1..254
FT /note="Activity-regulated cytoskeleton associated protein
FT 1"
FT /id="PRO_0000443801"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6S7X"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:6S7X"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:6S7X"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:6S7X"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:6S7X"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:6S7X"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:6S7X"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:6SID"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6S7Y"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:6SID"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:6SID"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:6SID"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:6SID"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:6SID"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6TAS"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6TAS"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:6TAS"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6TAS"
SQ SEQUENCE 254 AA; 28877 MW; 70068526BD89C9CE CRC64;
MAQLTQMTNE QLRELIEAVR AAAVGAAGSA AAAGGADASR GKGNFSACTH SFGGTRDHDV
VEEFIGNIET YKDVEGISDE NALKGISLLF YGMASTWWQG VRKEATTWKE AIALIREHFS
PTKPAYQIYM EFFQNKQDDH DPIDTFVIQK RALLAQLPSG RHDEETELDL LFGLLNIKYR
KHISRHSVHT FKDLLEQGRI IEHNNQEDEE QLATAKNTRG SKRTTRCTYC SFRGHTFDNC
RKRQKDRQEE QHEE
