ARPC2_DROME
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 03-AUG-2022, entry version 154.
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}.
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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 DIP; DIP-19044N; -.
DR IntAct; Q9VIM5; 3.
DR STRING; 7227.FBpp0080890; -.
DR PaxDb; Q9VIM5; -.
DR PRIDE; Q9VIM5; -.
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 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; GPYIVSP; -.
DR OrthoDB; 1345377at2759; -.
DR PhylomeDB; Q9VIM5; -.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
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 tissues.
DR ExpressionAtlas; Q9VIM5; baseline and differential.
DR Genevisible; Q9VIM5; DM.
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:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
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; PTHR12058; 1.
DR Pfam; PF04045; P34-Arc; 1.
DR SUPFAM; SSF69645; SSF69645; 2.
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
