ARP3_HUMAN
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 03-AUG-2022, entry version 178.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 subunits
RT and is localized to cellular regions of dynamic actin 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 THE
RP 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 surface
RT of Listeria monocytogenes.";
RL Nature 385:265-269(1997).
RN [8]
RP PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP 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 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 of
RT 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 functions
RT 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 SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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 its
RT 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., Hong A.,
RA Fox M., Gumucio D.L.;
RT "Pyrin and ASC co-localize to cellular sites that are rich in polymerizing
RT 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 ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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., Ideker T.,
RA 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., Buerckstuemmer T.,
RA 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT 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., Ayoub D.,
RA 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 INTERACTION WITH AVIL.
RX PubMed=29058690; DOI=10.1172/jci94138;
RA Rao J., Ashraf S., Tan W., van der Ven A.T., Gee H.Y., Braun D.A.,
RA Feher K., George S.P., Esmaeilniakooshkghazi A., Choi W.I.,
RA Jobst-Schwan T., Schneider R., Schmidt J.M., Widmeier E., Warejko J.K.,
RA Hermle T., Schapiro D., Lovric S., Shril S., Daga A., Nayir A., Shenoy M.,
RA Tse Y., Bald M., Helmchen U., Mir S., Berdeli A., Kari J.A., El Desoky S.,
RA Soliman N.A., Bagga A., Mane S., Jairajpuri M.A., Lifton R.P., Khurana S.,
RA Martins J.C., Hildebrandt F.;
RT "Advillin acts upstream of phospholipase C 1 in steroid-resistant nephrotic
RT syndrome.";
RL J. Clin. Invest. 127:4257-4269(2017).
RN [23]
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., Gundersen G.G.,
RA Gottesman M.E., Gautier J.;
RT "Nuclear ARP2/3 drives DNA break clustering for homology-directed repair.";
RL Nature 559:61-66(2018).
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) (PubMed:9000076). The Arp2/3 complex
CC mediates the formation of branched actin networks in the cytoplasm,
CC providing the force for cell motility (PubMed:9000076). Seems to
CC contact the pointed end of the daughter actin filament
CC (PubMed:9000076). In podocytes, required for the formation of
CC lamellipodia downstream of AVIL and PLCE1 regulation (PubMed:29058690).
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
CC (PubMed:17220302, PubMed:29925947). The Arp2/3 complex promotes
CC homologous recombination (HR) repair in response to DNA damage by
CC promoting nuclear actin polymerization, leading to drive motility of
CC double-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:29058690,
CC ECO:0000269|PubMed:29925947, 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, ARPC4/p20-ARC
CC and ARPC5/p16-ARC (PubMed:9000076, PubMed:9230079, PubMed:11741539).
CC Interacts with WHDC1 (PubMed:18614018). Interacts weakly with MEFV
CC (PubMed:19109554). Interacts with AVIL (PubMed:29058690).
CC {ECO:0000269|PubMed:11741539, ECO:0000269|PubMed:18614018,
CC ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:29058690,
CC ECO:0000269|PubMed:9000076, ECO:0000269|PubMed:9230079}.
CC -!- INTERACTION:
CC P61158; Q96BI3-2: APH1A; NbExp=3; IntAct=EBI-351428, EBI-25922794;
CC P61158; P05067: APP; NbExp=3; IntAct=EBI-351428, EBI-77613;
CC P61158; Q9ULD4-2: BRPF3; NbExp=3; IntAct=EBI-351428, EBI-23662416;
CC P61158; Q00535: CDK5; NbExp=3; IntAct=EBI-351428, EBI-1041567;
CC P61158; Q9H3R5: CENPH; NbExp=3; IntAct=EBI-351428, EBI-1003700;
CC P61158; P10809: HSPD1; NbExp=3; IntAct=EBI-351428, EBI-352528;
CC P61158; P17535: JUND; NbExp=2; IntAct=EBI-351428, EBI-2682803;
CC P61158; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-351428, EBI-357085;
CC P61158; P13051-2: UNG; NbExp=3; IntAct=EBI-351428, EBI-25834258;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19109554}. Cell projection
CC {ECO:0000269|PubMed:9230079}. Nucleus {ECO:0000269|PubMed:16767080,
CC ECO:0000269|PubMed:17220302, ECO:0000269|PubMed:29925947}. Note=In pre-
CC apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes)
CC (PubMed:19109554).
CC -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On mar and motion - Issue
CC 208 of November 2018;
CC URL="https://web.expasy.org/spotlight/back_issues/208/";
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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 PDB; 6UHC; EM; 3.90 A; A=1-418.
DR PDB; 6YW6; EM; 4.20 A; A=1-418.
DR PDB; 6YW7; EM; 4.50 A; A=1-418.
DR PDBsum; 6UHC; -.
DR PDBsum; 6YW6; -.
DR PDBsum; 6YW7; -.
DR AlphaFoldDB; P61158; -.
DR SMR; P61158; -.
DR BioGRID; 115403; 253.
DR CORUM; P61158; -.
DR DIP; DIP-33140N; -.
DR IntAct; P61158; 92.
DR MINT; P61158; -.
DR STRING; 9606.ENSP00000263238; -.
DR ChEMBL; CHEMBL4105857; -.
DR DrugBank; DB08236; (2S)-2-(3-bromophenyl)-3-(5-chloro-2-hydroxyphenyl)-1,3-thiazolidin-4-one.
DR DrugBank; DB08235; N-[2-(2-methyl-1H-indol-3-yl)ethyl]thiophene-2-carboxamide.
DR GlyGen; P61158; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61158; -.
DR MetOSite; P61158; -.
DR PhosphoSitePlus; P61158; -.
DR SwissPalm; P61158; -.
DR BioMuta; ACTR3; -.
DR DMDM; 47117647; -.
DR OGP; P32391; -.
DR CPTAC; CPTAC-160; -.
DR CPTAC; CPTAC-161; -.
DR EPD; P61158; -.
DR jPOST; P61158; -.
DR MassIVE; P61158; -.
DR PaxDb; P61158; -.
DR PeptideAtlas; P61158; -.
DR PRIDE; P61158; -.
DR ProteomicsDB; 57268; -.
DR Antibodypedia; 3913; 348 antibodies from 36 providers.
DR DNASU; 10096; -.
DR Ensembl; ENST00000263238.7; ENSP00000263238.2; ENSG00000115091.12.
DR GeneID; 10096; -.
DR KEGG; hsa:10096; -.
DR MANE-Select; ENST00000263238.7; ENSP00000263238.2; NM_005721.5; NP_005712.1.
DR UCSC; uc002tkx.3; human.
DR CTD; 10096; -.
DR DisGeNET; 10096; -.
DR GeneCards; ACTR3; -.
DR HGNC; HGNC:170; ACTR3.
DR HPA; ENSG00000115091; Low tissue specificity.
DR MIM; 604222; gene.
DR neXtProt; NX_P61158; -.
DR OpenTargets; ENSG00000115091; -.
DR PharmGKB; PA24489; -.
DR VEuPathDB; HostDB:ENSG00000115091; -.
DR eggNOG; KOG0678; Eukaryota.
DR GeneTree; ENSGT00940000155065; -.
DR InParanoid; P61158; -.
DR OMA; TAEFKSY; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P61158; -.
DR TreeFam; TF300644; -.
DR PathwayCommons; P61158; -.
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 Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; P61158; -.
DR SIGNOR; P61158; -.
DR BioGRID-ORCS; 10096; 378 hits in 1092 CRISPR screens.
DR ChiTaRS; ACTR3; human.
DR GeneWiki; ACTR3; -.
DR GenomeRNAi; 10096; -.
DR Pharos; P61158; Tchem.
DR PRO; PR:P61158; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P61158; protein.
DR Bgee; ENSG00000115091; Expressed in esophagus squamous epithelium and 205 other tissues.
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:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
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:0010592; P:positive regulation of lamellipodium assembly; IDA:UniProtKB.
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 InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF175; PTHR11937:SF175; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; ATP-binding; Cell projection;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT CHAIN 2..418
FT /note="Actin-related protein 3"
FT /id="PRO_0000089079"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT MOD_RES 240
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 254
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|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
