ARPC5_MOUSE
ID ARPC5_MOUSE Reviewed; 151 AA.
AC Q9CPW4; Q3U9T3; Q9D8E7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Actin-related protein 2/3 complex subunit 5;
DE AltName: Full=Arp2/3 complex 16 kDa subunit;
DE Short=p16-ARC;
GN Name=Arpc5;
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=BALB/cJ, and C57BL/6J;
RC TISSUE=Amnion, Bone marrow, Eye, Mammary gland, and Small intestine;
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=C57BL/6J; TISSUE=Brain;
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 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: Component of the Arp2/3 complex, a multiprotein complex that
CC mediates actin polymerization upon stimulation by nucleation-promoting
CC factor (NPF). The Arp2/3 complex mediates the formation of branched
CC actin networks in the cytoplasm, providing the force for cell motility.
CC In 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:O15511}.
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:O15511}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O15511}. Cell projection
CC {ECO:0000250|UniProtKB:O15511}. Nucleus {ECO:0000250|UniProtKB:O15511}.
CC -!- PTM: Polyubiquitinated by RNF128 with 'Lys-63'-linked chains, leading
CC to proteasomal degradation. {ECO:0000250|UniProtKB:O15511}.
CC -!- SIMILARITY: Belongs to the ARPC5 family. {ECO:0000305}.
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DR EMBL; AK008097; BAB25457.1; -; mRNA.
DR EMBL; AK011348; BAB27558.1; -; mRNA.
DR EMBL; AK011911; BAB27911.1; -; mRNA.
DR EMBL; AK017669; BAB30864.1; -; mRNA.
DR EMBL; AK019149; BAB31570.1; -; mRNA.
DR EMBL; AK087427; BAC39870.1; -; mRNA.
DR EMBL; AK149756; BAE29064.1; -; mRNA.
DR EMBL; AK151654; BAE30583.1; -; mRNA.
DR EMBL; AK151656; BAE30585.1; -; mRNA.
DR EMBL; AK152281; BAE31095.1; -; mRNA.
DR EMBL; AK153262; BAE31852.1; -; mRNA.
DR EMBL; AK159407; BAE35058.1; -; mRNA.
DR EMBL; AK159438; BAE35084.1; -; mRNA.
DR EMBL; AK159738; BAE35332.1; -; mRNA.
DR EMBL; AK166284; BAE38681.1; -; mRNA.
DR EMBL; AK166335; BAE38714.1; -; mRNA.
DR EMBL; AK166725; BAE38972.1; -; mRNA.
DR EMBL; AK167916; BAE39923.1; -; mRNA.
DR EMBL; AK168264; BAE40212.1; -; mRNA.
DR EMBL; AK168986; BAE40786.1; -; mRNA.
DR EMBL; BC060143; AAH60143.1; -; mRNA.
DR CCDS; CCDS35739.1; -.
DR RefSeq; NP_080645.2; NM_026369.2.
DR PDB; 7AQK; EM; 9.00 A; g=1-151.
DR PDBsum; 7AQK; -.
DR AlphaFoldDB; Q9CPW4; -.
DR SMR; Q9CPW4; -.
DR BioGRID; 212431; 15.
DR DIP; DIP-60589N; -.
DR IntAct; Q9CPW4; 3.
DR STRING; 10090.ENSMUSP00000076933; -.
DR iPTMnet; Q9CPW4; -.
DR PhosphoSitePlus; Q9CPW4; -.
DR SwissPalm; Q9CPW4; -.
DR EPD; Q9CPW4; -.
DR jPOST; Q9CPW4; -.
DR MaxQB; Q9CPW4; -.
DR PaxDb; Q9CPW4; -.
DR PRIDE; Q9CPW4; -.
DR ProteomicsDB; 281835; -.
DR TopDownProteomics; Q9CPW4; -.
DR Antibodypedia; 34448; 191 antibodies from 29 providers.
DR DNASU; 67771; -.
DR Ensembl; ENSMUST00000077755; ENSMUSP00000076933; ENSMUSG00000008475.
DR GeneID; 67771; -.
DR KEGG; mmu:67771; -.
DR UCSC; uc007czj.2; mouse.
DR CTD; 10092; -.
DR MGI; MGI:1915021; Arpc5.
DR VEuPathDB; HostDB:ENSMUSG00000008475; -.
DR eggNOG; KOG3380; Eukaryota.
DR GeneTree; ENSGT00940000154654; -.
DR HOGENOM; CLU_101888_1_1_1; -.
DR InParanoid; Q9CPW4; -.
DR OMA; GMALPGW; -.
DR OrthoDB; 1565115at2759; -.
DR PhylomeDB; Q9CPW4; -.
DR TreeFam; TF319716; -.
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; 67771; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Arpc5; mouse.
DR PRO; PR:Q9CPW4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CPW4; protein.
DR Bgee; ENSMUSG00000008475; Expressed in granulocyte and 62 other tissues.
DR ExpressionAtlas; Q9CPW4; baseline and differential.
DR Genevisible; Q9CPW4; MM.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0005200; F:structural constituent of cytoskeleton; ISO:MGI.
DR GO; GO:0051639; P:actin filament network formation; ISO:MGI.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0097581; P:lamellipodium organization; ISO:MGI.
DR GO; GO:0030011; P:maintenance of cell polarity; ISO:MGI.
DR GO; GO:0061842; P:microtubule organizing center localization; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0014909; P:smooth muscle cell migration; ISO:MGI.
DR Gene3D; 1.25.40.190; -; 1.
DR InterPro; IPR006789; ARPC5.
DR InterPro; IPR036743; ARPC5_sf.
DR PANTHER; PTHR12644; PTHR12644; 1.
DR Pfam; PF04699; P16-Arc; 1.
DR PIRSF; PIRSF039096; p16-ARC; 1.
DR SUPFAM; SSF69103; SSF69103; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15511"
FT CHAIN 2..151
FT /note="Actin-related protein 2/3 complex subunit 5"
FT /id="PRO_0000124055"
FT REGION 21..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O15511"
FT CONFLICT 59
FT /note="L -> Q (in Ref. 1; BAB25457)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 151 AA; 16288 MW; F050B10DC5416E66 CRC64;
MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK
NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN
SSAVLLQWHE KALAAGGVGS IVRVLTARKT V
