ARPC2_MOUSE
ID ARPC2_MOUSE Reviewed; 300 AA.
AC Q9CVB6; Q3U870;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 3.
DT 03-AUG-2022, entry version 148.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 107-117; 119-136; 148-157; 161-186; 191-203 AND
RP 238-248, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH SHANK3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24153177; DOI=10.1038/nature12630;
RA Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H., Tang J.,
RA Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M., Patel A., Lu H.C.,
RA Zoghbi H.Y.;
RT "SHANK3 overexpression causes manic-like behaviour with unique
RT pharmacogenetic properties.";
RL Nature 503:72-77(2013).
CC -!- FUNCTION: Actin-binding component of the Arp2/3 complex, a multiprotein
CC complex that mediates actin polymerization upon stimulation by
CC nucleation-promoting factor (NPF). The Arp2/3 complex mediates the
CC formation of branched actin networks in the cytoplasm, providing the
CC force for cell motility. Seems to contact the mother actin filament. In
CC addition to its role in the cytoplasmic cytoskeleton, the Arp2/3
CC complex also promotes actin polymerization in the nucleus, thereby
CC regulating gene transcription and repair of damaged DNA. The Arp2/3
CC complex promotes homologous recombination (HR) repair in response to
CC DNA damage by promoting nuclear actin polymerization, leading to drive
CC motility of double-strand breaks (DSBs).
CC {ECO:0000250|UniProtKB:O15144}.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2,
CC ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC
CC and ARPC5/p16-ARC (By similarity). Interacts with SHANK3; the
CC interaction probably mediates the association of SHANK3 with the Arp2/3
CC complex (PubMed:24153177). Interacts with DNAI3; this interaction
CC reduces binding of the Arp2/3 complex to the VCA domain of nucleation
CC promoting factors (By similarity). {ECO:0000250|UniProtKB:O15144,
CC ECO:0000250|UniProtKB:P61160, ECO:0000269|PubMed:24153177}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O15144}. Cell projection
CC {ECO:0000250|UniProtKB:O15144}. Synapse, synaptosome
CC {ECO:0000269|PubMed:24153177}. Nucleus {ECO:0000250|UniProtKB:O15144}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampal neurons (at protein
CC level). {ECO:0000269|PubMed:24153177}.
CC -!- SIMILARITY: Belongs to the ARPC2 family. {ECO:0000305}.
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DR EMBL; AK008777; BAB25889.2; -; mRNA.
DR EMBL; AK152356; BAE31148.1; -; mRNA.
DR EMBL; BC115750; AAI15751.1; -; mRNA.
DR CCDS; CCDS35612.1; -.
DR RefSeq; NP_083987.1; NM_029711.1.
DR RefSeq; XP_006496380.1; XM_006496317.2.
DR PDB; 7AQK; EM; 9.00 A; d=1-300.
DR PDBsum; 7AQK; -.
DR AlphaFoldDB; Q9CVB6; -.
DR SMR; Q9CVB6; -.
DR BioGRID; 218272; 26.
DR IntAct; Q9CVB6; 7.
DR MINT; Q9CVB6; -.
DR STRING; 10090.ENSMUSP00000006467; -.
DR iPTMnet; Q9CVB6; -.
DR PhosphoSitePlus; Q9CVB6; -.
DR SwissPalm; Q9CVB6; -.
DR EPD; Q9CVB6; -.
DR jPOST; Q9CVB6; -.
DR MaxQB; Q9CVB6; -.
DR PaxDb; Q9CVB6; -.
DR PeptideAtlas; Q9CVB6; -.
DR PRIDE; Q9CVB6; -.
DR ProteomicsDB; 281803; -.
DR Antibodypedia; 1901; 373 antibodies from 37 providers.
DR DNASU; 76709; -.
DR Ensembl; ENSMUST00000006467; ENSMUSP00000006467; ENSMUSG00000006304.
DR Ensembl; ENSMUST00000113820; ENSMUSP00000109451; ENSMUSG00000006304.
DR GeneID; 76709; -.
DR KEGG; mmu:76709; -.
DR UCSC; uc007bln.1; mouse.
DR CTD; 10109; -.
DR MGI; MGI:1923959; Arpc2.
DR VEuPathDB; HostDB:ENSMUSG00000006304; -.
DR eggNOG; KOG2826; Eukaryota.
DR GeneTree; ENSGT00390000016794; -.
DR HOGENOM; CLU_059439_2_0_1; -.
DR InParanoid; Q9CVB6; -.
DR OMA; GPYIVSP; -.
DR OrthoDB; 1345377at2759; -.
DR PhylomeDB; Q9CVB6; -.
DR TreeFam; TF315006; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 76709; 20 hits in 73 CRISPR screens.
DR ChiTaRS; Arpc2; mouse.
DR PRO; PR:Q9CVB6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CVB6; protein.
DR Bgee; ENSMUSG00000006304; Expressed in saccule of membranous labyrinth and 261 other tissues.
DR ExpressionAtlas; Q9CVB6; baseline and differential.
DR Genevisible; Q9CVB6; MM.
DR GO; GO:0061834; C:actin filament branch point; ISO:MGI.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0061830; C:concave side of sperm head; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0036195; C:muscle cell projection membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0090725; C:peripheral region of growth cone; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0061825; C:podosome core; ISO:MGI.
DR GO; GO:0061826; C:podosome ring; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0061835; C:ventral surface of cell; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0035254; F:glutamate receptor binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:MGI.
DR GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:MGI.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:MGI.
DR GO; GO:0072752; P:cellular response to rapamycin; ISO:MGI.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:MGI.
DR GO; GO:2000814; P:positive regulation of barbed-end actin filament capping; ISO:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:MGI.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0071803; P:positive regulation of podosome assembly; ISO:MGI.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:MGI.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Nucleus; Reference proteome;
KW Synapse; Synaptosome.
FT CHAIN 1..300
FT /note="Actin-related protein 2/3 complex subunit 2"
FT /id="PRO_0000124034"
FT MOD_RES 275
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15144"
FT MOD_RES 295
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15144"
SQ SEQUENCE 300 AA; 34357 MW; 6A5D8500D641DB60 CRC64;
MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG DKTKVMVSIS
LKFYKELQAH GADELLKRVY GSFLVNPEPG YNVSLLYDLE NLPASKDSIV HQAGMLKRNC
FASVFEKYFQ FQEEGKEGEN RAVIHYRDDE TMYVESKKDR VTVVFSTVFK DDDDVVIGKV
FMQEFKEGRR ASHTAPQVLF SHREPPLELK DTDAAVGDNI GYITFVLFPR HTNATARDNT
INLIHTFRDY LHYHIKCSKA YIHTRMRAKT SDFLKVLNRA RPDAEKKEMK TITGKTFSSR
