ARP2_RAT
ID ARP2_RAT Reviewed; 394 AA.
AC Q5M7U6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Actin-related protein 2;
DE AltName: Full=Actin-like protein 2;
GN Name=Actr2; Synonyms=Arp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
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 addition to its role in the cytoplasmic
CC cytoskeleton, the Arp2/3 complex also promotes actin polymerization in
CC the nucleus, thereby regulating gene transcription and repair of
CC damaged DNA. The Arp2/3 complex promotes homologous recombination (HR)
CC repair in response to DNA damage by promoting nuclear actin
CC polymerization, leading to drive motility of double-strand breaks
CC (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. {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}.
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DR EMBL; BC088442; AAH88442.1; -; mRNA.
DR RefSeq; NP_001009268.1; NM_001009268.1.
DR AlphaFoldDB; Q5M7U6; -.
DR SMR; Q5M7U6; -.
DR BioGRID; 253032; 4.
DR IntAct; Q5M7U6; 3.
DR MINT; Q5M7U6; -.
DR STRING; 10116.ENSRNOP00000006607; -.
DR iPTMnet; Q5M7U6; -.
DR PhosphoSitePlus; Q5M7U6; -.
DR World-2DPAGE; 0004:Q5M7U6; -.
DR jPOST; Q5M7U6; -.
DR PaxDb; Q5M7U6; -.
DR PRIDE; Q5M7U6; -.
DR GeneID; 289820; -.
DR KEGG; rno:289820; -.
DR UCSC; RGD:1310826; rat.
DR CTD; 10097; -.
DR RGD; 1310826; Actr2.
DR VEuPathDB; HostDB:ENSRNOG00000004959; -.
DR eggNOG; KOG0677; Eukaryota.
DR HOGENOM; CLU_027965_0_0_1; -.
DR InParanoid; Q5M7U6; -.
DR OMA; WEDMQHL; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; Q5M7U6; -.
DR TreeFam; TF300467; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q5M7U6; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000004959; Expressed in spleen and 19 other tissues.
DR Genevisible; Q5M7U6; RN.
DR GO; GO:0030478; C:actin cap; ISO:RGD.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0061825; C:podosome core; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0008306; P:associative learning; IEP:RGD.
DR GO; GO:0008356; P:asymmetric cell division; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0035984; P:cellular response to trichostatin A; IEP:RGD.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0016482; P:cytosolic transport; ISO:RGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISO:RGD.
DR GO; GO:0051321; P:meiotic cell cycle; ISO:RGD.
DR GO; GO:0016344; P:meiotic chromosome movement towards spindle pole; ISO:RGD.
DR GO; GO:0033206; P:meiotic cytokinesis; ISO:RGD.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
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; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0051653; P:spindle localization; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Actin-binding; ATP-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..394
FT /note="Actin-related protein 2"
FT /id="PRO_0000089070"
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; 44734 MW; 283A5F2CFB589CF3 CRC64;
MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI EIKDLMVGDE
ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI DTRSCKILLT 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
