ARPC3_HUMAN
ID ARPC3_HUMAN Reviewed; 178 AA.
AC O15145; O00554;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
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; Synonyms=ARC21;
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], AND SUBCELLULAR LOCATION.
RX PubMed=9359840; DOI=10.1042/bj3280105;
RA Machesky L.M., Reeves E., Wientjes F., Mattheyse F.J., Grogan A.,
RA Totty N.F., Burlingame A.L., Hsuan J.J., Segal A.W.;
RT "Mammalian actin-related protein 2/3 complex localizes to regions of
RT lamellipodial protrusion and is composed of evolutionarily conserved
RT proteins.";
RL Biochem. J. 328:105-112(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
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 [5]
RP PROTEIN SEQUENCE OF 2-25.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56 AND LYS-61, AND IDENTIFICATION
RP 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 [9]
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 [10]
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 [11]
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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [13]
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: Component of the Arp2/3 complex, a multiprotein complex that
CC mediates actin polymerization upon stimulation by nucleation-promoting
CC factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the
CC formation of branched actin networks in the cytoplasm, providing the
CC force for cell motility (PubMed:9230079). In addition to its role in
CC the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin
CC polymerization in the nucleus, thereby regulating gene transcription
CC and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex
CC promotes homologous recombination (HR) repair in response to DNA damage
CC by promoting nuclear actin polymerization, leading to drive motility of
CC double-strand breaks (DSBs) (PubMed:29925947).
CC {ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:9230079}.
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:0000269|PubMed:11741539,
CC ECO:0000269|PubMed:9230079}.
CC -!- INTERACTION:
CC O15145; P59998: ARPC4; NbExp=4; IntAct=EBI-351829, EBI-351872;
CC O15145; P46092: CCR10; NbExp=3; IntAct=EBI-351829, EBI-348022;
CC O15145; Q68J44: DUSP29; NbExp=3; IntAct=EBI-351829, EBI-1054321;
CC O15145; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-351829, EBI-8468186;
CC O15145; Q08379: GOLGA2; NbExp=6; IntAct=EBI-351829, EBI-618309;
CC O15145; O43365: HOXA3; NbExp=6; IntAct=EBI-351829, EBI-8643838;
CC O15145; O95835-2: LATS1; NbExp=3; IntAct=EBI-351829, EBI-17978514;
CC O15145; P48552: NRIP1; NbExp=3; IntAct=EBI-351829, EBI-746484;
CC O15145; P14859-6: POU2F1; NbExp=3; IntAct=EBI-351829, EBI-11526590;
CC O15145; Q8NC74: RBBP8NL; NbExp=3; IntAct=EBI-351829, EBI-11322432;
CC O15145; Q86VR2: RETREG3; NbExp=5; IntAct=EBI-351829, EBI-10192441;
CC O15145; Q9NX95-5: SYBU; NbExp=3; IntAct=EBI-351829, EBI-12816095;
CC O15145; A2RTX5: TARS3; NbExp=3; IntAct=EBI-351829, EBI-1056629;
CC O15145; O00401: WASL; NbExp=6; IntAct=EBI-351829, EBI-957615;
CC O15145; Q9H609: ZNF576; NbExp=3; IntAct=EBI-351829, EBI-3921014;
CC O15145; P0DTC9: N; Xeno; NbExp=4; IntAct=EBI-351829, EBI-25475856;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9230079, ECO:0000269|PubMed:9359840}. Cell
CC projection {ECO:0000269|PubMed:9230079, ECO:0000269|PubMed:9359840}.
CC Nucleus {ECO:0000269|PubMed:29925947}.
CC -!- SIMILARITY: Belongs to the ARPC3 family. {ECO:0000305}.
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DR EMBL; AF004561; AAB61466.1; -; mRNA.
DR EMBL; AF006086; AAB64191.1; -; mRNA.
DR EMBL; CR407667; CAG28595.1; -; mRNA.
DR EMBL; BC067747; AAH67747.1; -; mRNA.
DR EMBL; BC078162; AAH78162.1; -; mRNA.
DR CCDS; CCDS9146.1; -.
DR RefSeq; NP_001265485.1; NM_001278556.1.
DR RefSeq; NP_001274151.1; NM_001287222.1.
DR PDB; 6UHC; EM; 3.90 A; E=1-178.
DR PDB; 6YW6; EM; 4.20 A; E=1-178.
DR PDB; 6YW7; EM; 4.50 A; E=1-178.
DR PDBsum; 6UHC; -.
DR PDBsum; 6YW6; -.
DR PDBsum; 6YW7; -.
DR AlphaFoldDB; O15145; -.
DR SMR; O15145; -.
DR BioGRID; 115401; 161.
DR CORUM; O15145; -.
DR DIP; DIP-33187N; -.
DR IntAct; O15145; 91.
DR MINT; O15145; -.
DR STRING; 9606.ENSP00000228825; -.
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; O15145; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15145; -.
DR PhosphoSitePlus; O15145; -.
DR SwissPalm; O15145; -.
DR BioMuta; ARPC3; -.
DR OGP; O15145; -.
DR EPD; O15145; -.
DR jPOST; O15145; -.
DR MassIVE; O15145; -.
DR MaxQB; O15145; -.
DR PaxDb; O15145; -.
DR PeptideAtlas; O15145; -.
DR PRIDE; O15145; -.
DR ProteomicsDB; 48470; -.
DR TopDownProteomics; O15145; -.
DR Antibodypedia; 1504; 255 antibodies from 35 providers.
DR DNASU; 10094; -.
DR Ensembl; ENST00000228825.12; ENSP00000228825.7; ENSG00000111229.16.
DR GeneID; 10094; -.
DR KEGG; hsa:10094; -.
DR MANE-Select; ENST00000228825.12; ENSP00000228825.7; NM_001278556.2; NP_001265485.1.
DR UCSC; uc001tqq.5; human.
DR CTD; 10094; -.
DR DisGeNET; 10094; -.
DR GeneCards; ARPC3; -.
DR HGNC; HGNC:706; ARPC3.
DR HPA; ENSG00000111229; Low tissue specificity.
DR MIM; 604225; gene.
DR neXtProt; NX_O15145; -.
DR OpenTargets; ENSG00000111229; -.
DR PharmGKB; PA25000; -.
DR VEuPathDB; HostDB:ENSG00000111229; -.
DR eggNOG; KOG3155; Eukaryota.
DR GeneTree; ENSGT00390000018018; -.
DR HOGENOM; CLU_094365_1_0_1; -.
DR InParanoid; O15145; -.
DR OMA; TPSKWWL; -.
DR OrthoDB; 1451115at2759; -.
DR PhylomeDB; O15145; -.
DR TreeFam; TF314598; -.
DR PathwayCommons; O15145; -.
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; O15145; -.
DR SIGNOR; O15145; -.
DR BioGRID-ORCS; 10094; 472 hits in 1056 CRISPR screens.
DR ChiTaRS; ARPC3; human.
DR GeneWiki; ARPC3; -.
DR GenomeRNAi; 10094; -.
DR Pharos; O15145; Tbio.
DR PRO; PR:O15145; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O15145; protein.
DR Bgee; ENSG00000111229; Expressed in monocyte and 109 other tissues.
DR ExpressionAtlas; O15145; baseline and differential.
DR Genevisible; O15145; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:FlyBase.
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; ISS: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: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:FlyBase.
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|PubMed:12665801"
FT CHAIN 2..178
FT /note="Actin-related protein 2/3 complex subunit 3"
FT /id="PRO_0000124042"
FT MOD_RES 47
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 61
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 134
FT /note="Q -> P (in Ref. 1; AAB61466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 20547 MW; 7149F598B48F0EAC CRC64;
MPAYHSSLMD PDTKLIGNMA LLPIRSQFKG PAPRETKDTD IVDEAIYYFK ANVFFKNYEI
KNEADRTLIY ITLYISECLK KLQKCNSKSQ GEKEMYTLGI TNFPIPGEPG FPLNAIYAKP
ANKQEDEVMR AYLQQLRQET GLRLCEKVFD PQNDKPSKWW TCFVKRQFMN KSLSGPGQ
