ARPC3_MOUSE
ID ARPC3_MOUSE Reviewed; 178 AA.
AC Q9JM76; Q3TAT0;
DT 26-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 3;
DE AltName: Full=Arp2/3 complex 21 kDa subunit;
DE Short=p21-ARC;
GN Name=Arpc3;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Peritoneal macrophage;
RA Sugiura S.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Placenta, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, and Mammary tumor;
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 [4]
RP PROTEIN SEQUENCE OF 2-25; 38-50; 94-119; 131-137 AND 148-158, CLEAVAGE OF
RP INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic fibroblast;
RA Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.;
RL Submitted (MAR-2008) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [6]
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:O15145}.
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:O15145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O15145}. Cell projection
CC {ECO:0000250|UniProtKB:O15145}. Nucleus {ECO:0000250|UniProtKB:O15145}.
CC -!- SIMILARITY: Belongs to the ARPC3 family. {ECO:0000305}.
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DR EMBL; AB038243; BAA90788.1; -; mRNA.
DR EMBL; AK003485; BAB22813.1; -; mRNA.
DR EMBL; AK005437; BAB24031.1; -; mRNA.
DR EMBL; AK171651; BAE42588.1; -; mRNA.
DR EMBL; BC013618; AAH13618.1; -; mRNA.
DR EMBL; BC054440; AAH54440.1; -; mRNA.
DR CCDS; CCDS19648.1; -.
DR RefSeq; NP_062798.1; NM_019824.4.
DR PDB; 7AQK; EM; 9.00 A; e=1-178.
DR PDBsum; 7AQK; -.
DR AlphaFoldDB; Q9JM76; -.
DR SMR; Q9JM76; -.
DR BioGRID; 207939; 16.
DR IntAct; Q9JM76; 6.
DR MINT; Q9JM76; -.
DR STRING; 10090.ENSMUSP00000099584; -.
DR iPTMnet; Q9JM76; -.
DR PhosphoSitePlus; Q9JM76; -.
DR SwissPalm; Q9JM76; -.
DR EPD; Q9JM76; -.
DR jPOST; Q9JM76; -.
DR MaxQB; Q9JM76; -.
DR PaxDb; Q9JM76; -.
DR PeptideAtlas; Q9JM76; -.
DR PRIDE; Q9JM76; -.
DR ProteomicsDB; 281833; -.
DR TopDownProteomics; Q9JM76; -.
DR Antibodypedia; 1504; 255 antibodies from 35 providers.
DR DNASU; 56378; -.
DR Ensembl; ENSMUST00000102525; ENSMUSP00000099584; ENSMUSG00000029465.
DR GeneID; 56378; -.
DR KEGG; mmu:56378; -.
DR UCSC; uc008zlf.1; mouse.
DR CTD; 10094; -.
DR MGI; MGI:1928375; Arpc3.
DR VEuPathDB; HostDB:ENSMUSG00000029465; -.
DR eggNOG; KOG3155; Eukaryota.
DR GeneTree; ENSGT00390000018018; -.
DR HOGENOM; CLU_094365_1_0_1; -.
DR InParanoid; Q9JM76; -.
DR OMA; TPSKWWL; -.
DR OrthoDB; 1451115at2759; -.
DR PhylomeDB; Q9JM76; -.
DR TreeFam; TF314598; -.
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; 56378; 13 hits in 71 CRISPR screens.
DR ChiTaRS; Arpc3; mouse.
DR PRO; PR:Q9JM76; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JM76; protein.
DR Bgee; ENSMUSG00000029465; Expressed in granulocyte and 262 other tissues.
DR ExpressionAtlas; Q9JM76; baseline and differential.
DR Genevisible; Q9JM76; MM.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR GO; GO:0061850; C:growth cone leading edge; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA: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:0034314; P:Arp2/3 complex-mediated actin nucleation; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 1.10.1760.10; -; 1.
DR InterPro; IPR007204; ARPC3.
DR InterPro; IPR036753; ARPC3_sf.
DR PANTHER; PTHR12391; PTHR12391; 1.
DR Pfam; PF04062; P21-Arc; 1.
DR PIRSF; PIRSF016315; ARP2/3_P21-Arc; 1.
DR SUPFAM; SSF69060; SSF69060; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..178
FT /note="Actin-related protein 2/3 complex subunit 3"
FT /id="PRO_0000124043"
FT MOD_RES 47
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15145"
FT MOD_RES 61
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15145"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15145"
SQ SEQUENCE 178 AA; 20525 MW; 6B4F467F89BF4BAC CRC64;
MPAYHSSLMD PDTKLIGNMA LLPLRSQFKG PAPRETKDTD IVDEAIYYFK ANVFFKNYEI
KNEADRTLIY ITLYISECLK KLQKCNSKSQ GEKEMYTLGI TNFPIPGEPG FPLNAIYAKP
ASKQEDEMMR AYLQQLRQET GLRLCEKVFD PQSDKPSKWW TCFVKRQFMN KSLSGPGQ
