ID ARP3_HUMAN Reviewed; 418 AA. AC P61158; P32391; Q53QM2; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 05-DEC-2018, entry version 155. DE RecName: Full=Actin-related protein 3; DE AltName: Full=Actin-like protein 3; GN Name=ACTR3; Synonyms=ARP3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE ARP2/2 COMPLEX, AND RP SUBCELLULAR LOCATION. RX PubMed=9230079; DOI=10.1083/jcb.138.2.375; RA Welch M.D., Depace A.H., Verma S., Iwamatsu A., Mitchison T.J.; RT "The human Arp2/3 complex is composed of evolutionarily conserved RT subunits and is localized to cellular regions of dynamic actin RT filament assembly."; RL J. Cell Biol. 138:375-384(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Szelei J., Soto A.M., Geck P., Desronvil M., Prechtl N., Weill B., RA Sonnenschein C.; RT "Identification of human estrogen-inducible transcripts from a serum RT resistant variant of breast cancer MCF7 cells."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN RP THE ARP2/3 COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=9000076; DOI=10.1038/385265a0; RA Welch M.D., Iwamatsu A., Mitchison T.J.; RT "Actin polymerization is induced by Arp2/3 protein complex at the RT surface of Listeria monocytogenes."; RL Nature 385:265-269(1997). RN [8] RP PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=T-cell; RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.; RL Submitted (MAY-2006) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 103-123 AND 199-209, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [10] RP RECONSTITUTION OF THE ARP2/3 COMPLEX. RX PubMed=11741539; DOI=10.1016/S1097-2765(01)00393-8; RA Gournier H., Goley E.D., Niederstrasser H., Trinh T., Welch M.D.; RT "Reconstitution of human Arp2/3 complex reveals critical roles of RT individual subunits in complex structure and activity."; RL Mol. Cell 8:1041-1052(2001). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17220302; DOI=10.1074/jbc.M607596200; RA Yoo Y., Wu X., Guan J.L.; RT "A novel role of the actin-nucleating Arp2/3 complex in the regulation RT of RNA polymerase II-dependent transcription."; RL J. Biol. Chem. 282:7616-7623(2007). RN [13] RP INTERACTION WITH WHDC1. RX PubMed=18614018; DOI=10.1016/j.cell.2008.05.032; RA Campellone K.G., Webb N.J., Znameroski E.A., Welch M.D.; RT "WHAMM is an Arp2/3 complex activator that binds microtubules and RT functions in ER to Golgi transport."; RL Cell 134:148-161(2008). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP SUBCELLULAR LOCATION. RX PubMed=16767080; DOI=10.1038/ncb1433; RA Wu X., Yoo Y., Okuhama N.N., Tucker P.W., Liu G., Guan J.L.; RT "Regulation of RNA-polymerase-II-dependent transcription by N-WASP and RT its nuclear-binding partners."; RL Nat. Cell Biol. 8:756-763(2006). RN [16] RP SUBCELLULAR LOCATION, AND INTERACTION WITH MEFV. RX PubMed=19109554; DOI=10.3181/0806-RM-184; RA Waite A.L., Schaner P., Hu C., Richards N., Balci-Peynircioglu B., RA Hong A., Fox M., Gumucio D.L.; RT "Pyrin and ASC co-localize to cellular sites that are rich in RT polymerizing actin."; RL Exp. Biol. Med. (Maywood) 234:40-52(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-240; LYS-244; LYS-251 AND RP LYS-254, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [18] RP FUNCTION. RX PubMed=20393563; DOI=10.1038/nature08895; RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., RA Ideker T., Aza-Blanc P., Gleeson J.G.; RT "Functional genomic screen for modulators of ciliogenesis and cilium RT length."; RL Nature 464:1048-1051(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=29925947; DOI=10.1038/s41586-018-0237-5; RA Schrank B.R., Aparicio T., Li Y., Chang W., Chait B.T., RA Gundersen G.G., Gottesman M.E., Gautier J.; RT "Nuclear ARP2/3 drives DNA break clustering for homology-directed RT repair."; RL Nature 559:61-66(2018). CC -!- FUNCTION: ATP-binding component of the Arp2/3 complex, a CC multiprotein complex that mediates actin polymerization upon CC stimulation by nucleation-promoting factor (NPF) (PubMed:9000076). CC The Arp2/3 complex mediates the formation of branched actin CC networks in the cytoplasm, providing the force for cell motility CC (PubMed:9000076). Seems to contact the pointed end of the daughter CC actin filament (PubMed:9000076). In addition to its role in the CC cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin CC polymerization in the nucleus, thereby regulating gene CC transcription and repair of damaged DNA (PubMed:17220302, CC PubMed:29925947). The Arp2/3 complex promotes homologous CC recombination (HR) repair in response to DNA damage by promoting CC nuclear actin polymerization, leading to drive motility of double- CC strand breaks (DSBs) (PubMed:29925947). Plays a role in CC ciliogenesis (PubMed:20393563). {ECO:0000269|PubMed:17220302, CC ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:29925947, CC ECO:0000269|PubMed:9000076}. CC -!- SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2, CC ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, CC ARPC4/p20-ARC and ARPC5/p16-ARC (PubMed:9000076, PubMed:9230079, CC PubMed:11741539). Interacts with WHDC1 (PubMed:18614018). CC Interacts weakly with MEFV (PubMed:19109554). CC {ECO:0000269|PubMed:11741539, ECO:0000269|PubMed:18614018, CC ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:9000076, CC ECO:0000269|PubMed:9230079}. CC -!- INTERACTION: CC P17535:JUND; NbExp=2; IntAct=EBI-351428, EBI-2682803; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:19109554}. Cell projection CC {ECO:0000269|PubMed:9230079}. Nucleus CC {ECO:0000269|PubMed:16767080, ECO:0000269|PubMed:17220302, CC ECO:0000269|PubMed:29925947}. Note=In pre-apoptotic cells, CC colocalizes with MEFV in large specks (pyroptosomes) CC (PubMed:19109554). CC -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. CC {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; AF006083; AAB64188.1; -; mRNA. DR EMBL; AF127773; AAD51904.1; -; mRNA. DR EMBL; AK312659; BAG35542.1; -; mRNA. DR EMBL; AC110769; AAX93226.1; -; Genomic_DNA. DR EMBL; CH471103; EAW95179.1; -; Genomic_DNA. DR EMBL; BC044590; AAH44590.1; -; mRNA. DR CCDS; CCDS33277.1; -. DR RefSeq; NP_005712.1; NM_005721.4. DR UniGene; Hs.433512; -. DR UniGene; Hs.595349; -. DR ProteinModelPortal; P61158; -. DR SMR; P61158; -. DR BioGrid; 115403; 106. DR CORUM; P61158; -. DR DIP; DIP-33140N; -. DR IntAct; P61158; 50. DR MINT; P61158; -. DR STRING; 9606.ENSP00000263238; -. DR DrugBank; DB08235; N-[2-(2-methyl-1H-indol-3-yl)ethyl]thiophene-2-carboxamide. DR iPTMnet; P61158; -. DR PhosphoSitePlus; P61158; -. DR SwissPalm; P61158; -. DR DMDM; 47117647; -. DR OGP; P32391; -. DR EPD; P61158; -. DR PaxDb; P61158; -. DR PeptideAtlas; P61158; -. DR PRIDE; P61158; -. DR ProteomicsDB; 57268; -. DR DNASU; 10096; -. DR Ensembl; ENST00000263238; ENSP00000263238; ENSG00000115091. DR GeneID; 10096; -. DR KEGG; hsa:10096; -. DR UCSC; uc002tkx.3; human. DR CTD; 10096; -. DR DisGeNET; 10096; -. DR EuPathDB; HostDB:ENSG00000115091.11; -. DR GeneCards; ACTR3; -. DR HGNC; HGNC:170; ACTR3. DR HPA; CAB005085; -. DR HPA; HPA047016; -. DR HPA; HPA051683; -. DR MIM; 604222; gene. DR neXtProt; NX_P61158; -. DR OpenTargets; ENSG00000115091; -. DR PharmGKB; PA24489; -. DR eggNOG; KOG0678; Eukaryota. DR eggNOG; COG5277; LUCA. DR GeneTree; ENSGT00940000155065; -. DR HOGENOM; HOG000233339; -. DR HOVERGEN; HBG003771; -. DR InParanoid; P61158; -. DR KO; K18584; -. DR OMA; AIKHIPI; -. DR OrthoDB; EOG091G0BPD; -. DR PhylomeDB; P61158; -. DR TreeFam; TF300644; -. DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling. DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR SignaLink; P61158; -. DR SIGNOR; P61158; -. DR ChiTaRS; ACTR3; human. DR GeneWiki; ACTR3; -. DR GenomeRNAi; 10096; -. DR PMAP-CutDB; P61158; -. DR PRO; PR:P61158; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000115091; Expressed in 234 organ(s), highest expression level in esophagus squamous epithelium. DR CleanEx; HS_ACTR3; -. DR ExpressionAtlas; P61158; baseline and differential. DR Genevisible; P61158; HS. DR GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB. DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:UniProtKB. DR GO; GO:0005903; C:brush border; IEA:Ensembl. DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:FlyBase. DR GO; GO:0070358; P:actin polymerization-dependent cell motility; TAS:UniProtKB. DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB. DR GO; GO:0008356; P:asymmetric cell division; IEA:Ensembl. DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl. DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome. DR GO; GO:0016344; P:meiotic chromosome movement towards spindle pole; IEA:Ensembl. DR GO; GO:0033206; P:meiotic cytokinesis; IEA:Ensembl. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0051653; P:spindle localization; IEA:Ensembl. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR015623; Arp3. DR PANTHER; PTHR11937; PTHR11937; 1. DR PANTHER; PTHR11937:SF175; PTHR11937:SF175; 1. DR Pfam; PF00022; Actin; 2. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. PE 1: Evidence at protein level; KW Acetylation; Actin-binding; ATP-binding; Cell projection; KW Cilium biogenesis/degradation; Complete proteome; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Nucleotide-binding; Nucleus; KW Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330, FT ECO:0000269|Ref.8}. FT CHAIN 2 418 Actin-related protein 3. FT /FTId=PRO_0000089079. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000269|Ref.8}. FT MOD_RES 240 240 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 244 244 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 251 251 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 254 254 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. SQ SEQUENCE 418 AA; 47371 MW; 23E5564198B81C63 CRC64; MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY LRAEPEDHYF LLTEPPLNTP ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV AEGYVIGSCI KHIPIAGRDI TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK EFNKYDTDGS KWIKQYTGIN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS EELSGGRLKP KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS //