ARP2_MOUSE
ID ARP2_MOUSE Reviewed; 394 AA.
AC P61161; O15142; Q6PI31;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Actin-related protein 2;
DE AltName: Full=Actin-like protein 2;
GN Name=Actr2; Synonyms=Arp2;
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, and NOD; TISSUE=Thymus;
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].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 54-65; 300-316; 323-328 AND 352-366, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-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).
CC -!- FUNCTION: ATP-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 pointed end of the
CC daughter actin filament. In podocytes, required for the formation of
CC lamellipodia downstream of AVIL and PLCE1 regulation. In addition to
CC its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also
CC promotes actin polymerization in the nucleus, thereby regulating gene
CC transcription and repair of damaged DNA. The Arp2/3 complex promotes
CC homologous recombination (HR) repair in response to DNA damage by
CC promoting nuclear actin polymerization, leading to drive motility of
CC double-strand breaks (DSBs). {ECO:0000250|UniProtKB:P61160}.
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. Interacts with AVIL. {ECO:0000250|UniProtKB:P61160}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P61160}. Cell projection
CC {ECO:0000250|UniProtKB:P61160}. Nucleus {ECO:0000250|UniProtKB:P61160}.
CC -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {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; AK032832; BAC28048.1; -; mRNA.
DR EMBL; AK088216; BAC40216.1; -; mRNA.
DR EMBL; BC027799; AAH27799.1; -; mRNA.
DR EMBL; BC047530; AAH47530.1; -; mRNA.
DR CCDS; CCDS24455.1; -.
DR RefSeq; NP_666355.1; NM_146243.2.
DR PDB; 7AQK; EM; 9.00 A; b=1-394.
DR PDBsum; 7AQK; -.
DR AlphaFoldDB; P61161; -.
DR SMR; P61161; -.
DR BioGRID; 211665; 44.
DR IntAct; P61161; 6.
DR MINT; P61161; -.
DR STRING; 10090.ENSMUSP00000000137; -.
DR iPTMnet; P61161; -.
DR PhosphoSitePlus; P61161; -.
DR SwissPalm; P61161; -.
DR EPD; P61161; -.
DR jPOST; P61161; -.
DR PaxDb; P61161; -.
DR PeptideAtlas; P61161; -.
DR PRIDE; P61161; -.
DR ProteomicsDB; 283243; -.
DR Antibodypedia; 3912; 301 antibodies from 36 providers.
DR DNASU; 66713; -.
DR Ensembl; ENSMUST00000000137; ENSMUSP00000000137; ENSMUSG00000020152.
DR GeneID; 66713; -.
DR KEGG; mmu:66713; -.
DR UCSC; uc011xrw.1; mouse.
DR CTD; 10097; -.
DR MGI; MGI:1913963; Actr2.
DR VEuPathDB; HostDB:ENSMUSG00000020152; -.
DR eggNOG; KOG0677; Eukaryota.
DR GeneTree; ENSGT00940000154556; -.
DR HOGENOM; CLU_027965_0_0_1; -.
DR InParanoid; P61161; -.
DR OMA; WEDMQHL; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P61161; -.
DR TreeFam; TF300467; -.
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-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 66713; 36 hits in 76 CRISPR screens.
DR ChiTaRS; Actr2; mouse.
DR PRO; PR:P61161; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P61161; protein.
DR Bgee; ENSMUSG00000020152; Expressed in stroma of bone marrow and 253 other tissues.
DR ExpressionAtlas; P61161; baseline and differential.
DR Genevisible; P61161; MM.
DR GO; GO:0030478; C:actin cap; IDA:MGI.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0061825; C:podosome core; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0008356; P:asymmetric cell division; IGI:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IGI:MGI.
DR GO; GO:0035984; P:cellular response to trichostatin A; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0016482; P:cytosolic transport; IMP:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IGI:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IGI:MGI.
DR GO; GO:0016344; P:meiotic chromosome movement towards spindle pole; IGI:MGI.
DR GO; GO:0033206; P:meiotic cytokinesis; IGI:MGI.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:0051653; P:spindle localization; IGI:MGI.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; ATP-binding; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..394
FT /note="Actin-related protein 2"
FT /id="PRO_0000089068"
FT BINDING 160..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A7MB62"
FT BINDING 214..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A7MB62"
FT BINDING 305..310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A7MB62"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61160"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61160"
FT MOD_RES 322
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61160"
SQ SEQUENCE 394 AA; 44761 MW; 1BFA6B442ED1A797 CRC64;
MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI EIKDLMVGDE
ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI DTRNCKILLT EPPMNPTKNR
EKIVEVMFET YQFSGVYVAI QAVLTLYAQG LLTGVVVDSG DGVTHICPVY EGFSLPHLTR
RLDIAGRDIT RYLIKLLLLR GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL
VESYTLPDGR IIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRSEFYKH
IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR KHMVFLGGAV
LADIMKDKDN FWMTRQEYQE KGVRVLEKLG VTVR
