Actin-related protein 2/3 complex subunit 4 (Arp2/3 complex 20 kDa subunit) (p20-ARC)

 ARPC4_MOUSE             Reviewed;         168 AA.
 P59999; O15509; Q3UWV4;
 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
 23-JAN-2007, sequence version 3.
 07-APR-2021, entry version 136.
 RecName: Full=Actin-related protein 2/3 complex subunit 4;
 AltName: Full=Arp2/3 complex 20 kDa subunit;
          Short=p20-ARC;
 Name=Arpc4; Synonyms=Arc20;
 Mus musculus (Mouse).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
 Murinae; Mus; Mus.
 NCBI_TaxID=10090;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 TISSUE=Skeletal muscle;
 Ievolella C., Campagna D., Lanfranchi G.;
 "Full-length sequencing of some human and murine muscular transcripts
 (Telethon Italy project B41).";
 Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=C57BL/6J;
 TISSUE=Bone marrow, Egg, Hypothalamus, Mammary gland, Pituitary, and
 Thymus;
 PubMed=16141072; DOI=10.1126/science.1112014;
 Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
 Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
 Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
 Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
 Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
 Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
 Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
 Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
 Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
 Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
 Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
 Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
 Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
 Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
 Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
 Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
 Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
 Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
 Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
 Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
 Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
 Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
 Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
 Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
 Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
 van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
 Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
 Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
 Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
 Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
 Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
 Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
 Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
 Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
 "The transcriptional landscape of the mammalian genome.";
 Science 309:1559-1563(2005).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Kidney;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA project:
 the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [4]
 PROTEIN SEQUENCE OF 2-41; 45-55; 61-71; 98-105; 107-128; 131-150 AND
 159-166, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND
 IDENTIFICATION BY MASS SPECTROMETRY.
 TISSUE=Embryonic fibroblast;
 Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.;
 Submitted (MAR-2008) to UniProtKB.
 [5]
 PROTEIN SEQUENCE OF 98-105, AND IDENTIFICATION BY MASS SPECTROMETRY.
 STRAIN=C57BL/6J; TISSUE=Brain;
 Lubec G., Kang S.U.;
 Submitted (APR-2007) to UniProtKB.
 [6]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
 Spleen, and Testis;
 PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
 Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
 Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
 "A tissue-specific atlas of mouse protein phosphorylation and expression.";
 Cell 143:1174-1189(2010).
 -!- FUNCTION: Actin-binding component of the Arp2/3 complex, a multiprotein
     complex that mediates actin polymerization upon stimulation by
     nucleation-promoting factor (NPF). The Arp2/3 complex mediates the
     formation of branched actin networks in the cytoplasm, providing the
     force for cell motility. In addition to its role in the cytoplasmic
     cytoskeleton, the Arp2/3 complex also promotes actin polymerization in
     the nucleus, thereby regulating gene transcription and repair of
     damaged DNA. The Arp2/3 complex promotes homologous recombination (HR)
     repair in response to DNA damage by promoting nuclear actin
     polymerization, leading to drive motility of double-strand breaks
     (DSBs). {ECO:0000250|UniProtKB:P59998}.
 -!- SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2,
     ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC
     and ARPC5/p16-ARC. {ECO:0000250|UniProtKB:P59998}.
 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
     {ECO:0000250|UniProtKB:P59998}. Cell projection
     {ECO:0000250|UniProtKB:P59998}. Nucleus {ECO:0000250|UniProtKB:P59998}.
 -!- SIMILARITY: Belongs to the ARPC4 family. {ECO:0000305}.
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 EMBL; AJ278129; CAC34583.1; -; mRNA.
 EMBL; AK017993; BAB31026.1; -; mRNA.
 EMBL; AK039215; BAC30279.1; -; mRNA.
 EMBL; AK077325; BAC36751.1; -; mRNA.
 EMBL; AK133626; BAE21755.1; -; mRNA.
 EMBL; AK136082; BAE22810.1; -; mRNA.
 EMBL; AK150690; BAE29769.1; -; mRNA.
 EMBL; AK153380; BAE31946.1; -; mRNA.
 EMBL; AK166440; BAE38777.1; -; mRNA.
 EMBL; BC015280; -; NOT_ANNOTATED_CDS; mRNA.
 CCDS; CCDS20417.1; -.
 RefSeq; NP_001163956.1; NM_001170485.1.
 RefSeq; NP_001163957.1; NM_001170486.1.
 RefSeq; NP_080828.1; NM_026552.3.
 SMR; P59999; -.
 BioGRID; 212649; 18.
 IntAct; P59999; 7.
 MINT; P59999; -.
 STRING; 10090.ENSMUSP00000114839; -.
 iPTMnet; P59999; -.
 PhosphoSitePlus; P59999; -.
 SwissPalm; P59999; -.
 EPD; P59999; -.
 jPOST; P59999; -.
 MaxQB; P59999; -.
 PaxDb; P59999; -.
 PeptideAtlas; P59999; -.
 PRIDE; P59999; -.
 ProteomicsDB; 281834; -.
 TopDownProteomics; P59999; -.
 Antibodypedia; 34895; 202 antibodies.
 Ensembl; ENSMUST00000156898; ENSMUSP00000114839; ENSMUSG00000079426.
 GeneID; 68089; -.
 KEGG; mmu:68089; -.
 UCSC; uc009dfs.2; mouse.
 CTD; 10093; -.
 MGI; MGI:1915339; Arpc4.
 eggNOG; KOG1876; Eukaryota.
 GeneTree; ENSGT00390000016233; -.
 HOGENOM; CLU_084855_1_0_1; -.
 InParanoid; P59999; -.
 OMA; RFMMQRA; -.
 OrthoDB; 1351067at2759; -.
 PhylomeDB; P59999; -.
 TreeFam; TF105621; -.
 Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
 Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
 Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
 Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
 BioGRID-ORCS; 68089; 25 hits in 50 CRISPR screens.
 ChiTaRS; Arpc4; mouse.
 PRO; PR:P59999; -.
 Proteomes; UP000000589; Chromosome 6.
 RNAct; P59999; protein.
 Bgee; ENSMUSG00000079426; Expressed in granulocyte and 276 other tissues.
 ExpressionAtlas; P59999; baseline and differential.
 Genevisible; P59999; MM.
 GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
 GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
 GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO; GO:0005634; C:nucleus; ISS:UniProtKB.
 GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
 GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
 GO; GO:0019899; F:enzyme binding; ISO:MGI.
 GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
 GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:MGI.
 GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
 GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISO:MGI.
 Gene3D; 3.30.1460.20; -; 1.
 InterPro; IPR034666; ARPC2/4.
 InterPro; IPR008384; ARPC4.
 PANTHER; PTHR22629; PTHR22629; 1.
 Pfam; PF05856; ARPC4; 1.
 PIRSF; PIRSF039100; ARPC4; 1.
 SUPFAM; SSF69645; SSF69645; 1.
 1: Evidence at protein level;
 Acetylation; Actin-binding; Cell projection; Cytoplasm; Cytoskeleton;
 Direct protein sequencing; Nucleus; Reference proteome.
 INIT_MET        1
                 /note="Removed"
                 /evidence="ECO:0000269|Ref.4"
 CHAIN           2..168
                 /note="Actin-related protein 2/3 complex subunit 4"
                 /id="PRO_0000124050"
 MOD_RES         2
                 /note="N-acetylthreonine"
                 /evidence="ECO:0000269|Ref.4"
 SEQUENCE   168 AA;  19667 MW;  273CCB230AC703DF CRC64;
 MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP VTISRNEKEK
 VLIEGSINSV RVSIAVKQAD EIEKILCHKF MRFMMMRAEN FFILRRKPVE GYDISFLITN
 FHTEQMYKHK LVDFVIHFME EIDKEISEMK LSVNARARIV AEEFLKNF

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