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 24-MAR-2009, entry version 51. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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 MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S.; RL Submitted (MAR-2007) to UniProtKB. CC -!- FUNCTION: Functions as actin-binding component of the Arp2/3 CC complex which is involved in regulation of actin polymerization CC and together with an activating nucleation-promoting factor (NPF) CC mediates the formation of branched actin networks. Seems to CC contact the mother actin filament (By similarity). CC -!- SUBUNIT: Component of the Arp2/3 complex composed of ARP2, ARP3, CC ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and CC ARPC5/p16-ARC (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity). CC Cell projection (By similarity). CC -!- SIMILARITY: Belongs to the ARPC2 family. 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; AK008777; BAB25889.2; -; mRNA. DR EMBL; AK152356; BAE31148.1; -; mRNA. DR EMBL; BC115750; AAI15751.1; -; mRNA. DR IPI; IPI00661414; -. DR RefSeq; NP_083987.1; -. DR UniGene; Mm.337038; -. DR SMR; Q9CVB6; 1-283. DR PRIDE; Q9CVB6; -. DR Ensembl; ENSMUSG00000006304; Mus musculus. DR GeneID; 76709; -. DR KEGG; mmu:76709; -. DR MGI; MGI:1923959; Arpc2. DR HOVERGEN; Q9CVB6; -. DR NextBio; 345665; -. DR ArrayExpress; Q9CVB6; -. DR Bgee; Q9CVB6; -. DR CleanEx; MM_ARPC2; -. DR GO; GO:0005885; C:Arp2/3 protein complex; TAS:MGI. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005925; C:focal adhesion; IDA:MGI. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro. DR InterPro; IPR007188; P34-arc. DR PANTHER; PTHR12058; P34-arc; 1. DR Pfam; PF04045; P34-Arc; 1. PE 1: Evidence at protein level; KW Actin-binding; Cell projection; Cytoplasm; Cytoskeleton; KW Direct protein sequencing. FT CHAIN 1 300 Actin-related protein 2/3 complex subunit FT 2. FT /FTId=PRO_0000124034. 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 //