ID ARPC2_DROME Reviewed; 301 AA. AC Q9VIM5; Q95T07; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 27-JAN-2003, sequence version 2. DT 27-MAR-2024, entry version 161. DE RecName: Full=Actin-related protein 2/3 complex subunit 2; DE AltName: Full=Arp2/3 complex 34 kDa subunit; DE Short=p34-ARC; GN Name=Arpc2; Synonyms=Arc-p34; ORFNames=CG10954; 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). CC -!- FUNCTION: Functions as actin-binding component of the Arp2/3 complex CC which is involved in regulation of actin polymerization and together CC with an activating nucleation-promoting factor (NPF) mediates the CC formation of branched actin networks. Seems to contact the mother actin CC filament (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Component of the Arp2/3 complex. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ARPC2 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; AE014134; AAF53892.2; -; Genomic_DNA. DR EMBL; AY060391; AAL25430.1; -; mRNA. DR RefSeq; NP_001286102.1; NM_001299173.1. DR RefSeq; NP_610033.1; NM_136189.4. DR AlphaFoldDB; Q9VIM5; -. DR SMR; Q9VIM5; -. DR BioGRID; 61277; 15. DR ComplexPortal; CPX-2589; Actin-related protein 2/3 complex, Arpc3B variant. DR ComplexPortal; CPX-2739; Actin-related protein 2/3 complex, Arpc3A variant. DR DIP; DIP-19044N; -. DR IntAct; Q9VIM5; 3. DR STRING; 7227.FBpp0312086; -. DR PaxDb; 7227-FBpp0080890; -. DR DNASU; 35311; -. DR EnsemblMetazoa; FBtr0081358; FBpp0080890; FBgn0032859. DR EnsemblMetazoa; FBtr0346418; FBpp0312086; FBgn0032859. DR GeneID; 35311; -. DR KEGG; dme:Dmel_CG10954; -. DR UCSC; CG10954-RA; d. melanogaster. DR AGR; FB:FBgn0032859; -. DR CTD; 10109; -. DR FlyBase; FBgn0032859; Arpc2. DR VEuPathDB; VectorBase:FBgn0032859; -. DR eggNOG; KOG2826; Eukaryota. DR HOGENOM; CLU_059439_2_0_1; -. DR InParanoid; Q9VIM5; -. DR OMA; FRSYFHY; -. DR OrthoDB; 1275887at2759; -. DR PhylomeDB; Q9VIM5; -. DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-DME-3928662; EPHB-mediated forward signaling. DR Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis. DR BioGRID-ORCS; 35311; 1 hit in 1 CRISPR screen. DR GenomeRNAi; 35311; -. DR PRO; PR:Q9VIM5; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0032859; Expressed in ovary and 14 other cell types or tissues. DR ExpressionAtlas; Q9VIM5; baseline and differential. DR GO; GO:0045179; C:apical cortex; HDA:FlyBase. DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:FlyBase. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:FlyBase. DR GO; GO:0030041; P:actin filament polymerization; IEA:InterPro. DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:FlyBase. DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase. DR GO; GO:0030031; P:cell projection assembly; IMP:FlyBase. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase. DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase. DR Gene3D; 3.30.1460.20; -; 2. DR InterPro; IPR007188; ARPC2. DR InterPro; IPR034666; ARPC2/4. DR PANTHER; PTHR12058:SF0; ACTIN-RELATED PROTEIN 2_3 COMPLEX SUBUNIT 2; 1. DR PANTHER; PTHR12058; ARP2/3 COMPLEX 34 KDA SUBUNIT; 1. DR Pfam; PF04045; P34-Arc; 1. DR SUPFAM; SSF69645; Arp2/3 complex subunits; 2. DR Genevisible; Q9VIM5; DM. PE 2: Evidence at transcript level; KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome. FT CHAIN 1..301 FT /note="Actin-related protein 2/3 complex subunit 2" FT /id="PRO_0000124039" FT REGION 281..301 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 301 AA; 35104 MW; BD1C82C1343CA5AF CRC64; MILLEINNRI IEETLLVKYR NAQAGLKPES IDIRIADFDG VLYHISNVNG DKTKVRISIS LKFYKQLQEH GADELLKREY GSLLTDTEEG YNVSVLINLE EIPEDCEQIA KRIGLLKRNC FASVFEKYFD YQEQGEEGQK RAVINYRNDE TLYVEAKPDR VTVVFSTIFR DEDDVIIGKV FMQELREGRR ASHTAPQVLF SHREPPLELA NTDARVGDNI GYVTFVLFPR HTNKETRDNT INLIHMFRDY LHYHIKCSKA YIHSRMRAKT SDFLKVLNRA RPEPKNTEKK TITGRTFKRI D //