ARPC5_HUMAN
ID ARPC5_HUMAN Reviewed; 151 AA.
AC O15511; A6NEC4; Q6PG42;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Actin-related protein 2/3 complex subunit 5;
DE AltName: Full=Arp2/3 complex 16 kDa subunit;
DE Short=p16-ARC;
GN Name=ARPC5; Synonyms=ARC16;
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] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN THE ARP2/2 COMPLEX.
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] (ISOFORM 1), AND IDENTIFICATION IN THE ARP2/2
RP COMPLEX.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [6]
RP PROTEIN SEQUENCE OF 2-10.
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 [7]
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 [8]
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 [9]
RP UBIQUITINATION BY RNF128.
RX PubMed=22016387; DOI=10.1074/jbc.m111.222711;
RA Ichikawa D., Mizuno M., Yamamura T., Miyake S.;
RT "GRAIL (gene related to anergy in lymphocytes) regulates cytoskeletal
RT reorganization through ubiquitination and degradation of Arp2/3 subunit 5
RT and coronin 1A.";
RL J. Biol. Chem. 286:43465-43474(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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 [12]
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 [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, ECO:0000269|PubMed:9359840}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9230079}. Cell projection
CC {ECO:0000269|PubMed:9230079}. Nucleus {ECO:0000269|PubMed:29925947}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15511-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15511-2; Sequence=VSP_024028;
CC -!- PTM: Polyubiquitinated by RNF128 with 'Lys-63'-linked chains, leading
CC to proteasomal degradation. {ECO:0000269|PubMed:22016387}.
CC -!- SIMILARITY: Belongs to the ARPC5 family. {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; AF006088; AAB64193.1; -; mRNA.
DR EMBL; AF017807; AAB70561.1; -; mRNA.
DR EMBL; AL137800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91163.1; -; Genomic_DNA.
DR EMBL; BC057237; AAH57237.1; -; mRNA.
DR CCDS; CCDS1357.1; -. [O15511-1]
DR CCDS; CCDS58050.1; -. [O15511-2]
DR RefSeq; NP_001257368.1; NM_001270439.1. [O15511-2]
DR RefSeq; NP_005708.1; NM_005717.3. [O15511-1]
DR PDB; 6UHC; EM; 3.90 A; G=1-151.
DR PDB; 6YW7; EM; 4.50 A; G=1-151.
DR PDBsum; 6UHC; -.
DR PDBsum; 6YW7; -.
DR AlphaFoldDB; O15511; -.
DR SMR; O15511; -.
DR BioGRID; 115399; 86.
DR CORUM; O15511; -.
DR DIP; DIP-33144N; -.
DR IntAct; O15511; 50.
DR MINT; O15511; -.
DR STRING; 9606.ENSP00000294742; -.
DR ChEMBL; CHEMBL4295658; -.
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; O15511; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15511; -.
DR MetOSite; O15511; -.
DR PhosphoSitePlus; O15511; -.
DR BioMuta; ARPC5; -.
DR OGP; O15511; -.
DR SWISS-2DPAGE; O15511; -.
DR EPD; O15511; -.
DR jPOST; O15511; -.
DR MassIVE; O15511; -.
DR MaxQB; O15511; -.
DR PaxDb; O15511; -.
DR PeptideAtlas; O15511; -.
DR PRIDE; O15511; -.
DR ProteomicsDB; 48703; -. [O15511-1]
DR ProteomicsDB; 48704; -. [O15511-2]
DR TopDownProteomics; O15511-1; -. [O15511-1]
DR TopDownProteomics; O15511-2; -. [O15511-2]
DR Antibodypedia; 34448; 191 antibodies from 29 providers.
DR DNASU; 10092; -.
DR Ensembl; ENST00000294742.6; ENSP00000294742.6; ENSG00000162704.16. [O15511-2]
DR Ensembl; ENST00000359856.11; ENSP00000352918.6; ENSG00000162704.16. [O15511-1]
DR GeneID; 10092; -.
DR KEGG; hsa:10092; -.
DR MANE-Select; ENST00000359856.11; ENSP00000352918.6; NM_005717.4; NP_005708.1.
DR UCSC; uc021pgb.3; human. [O15511-1]
DR CTD; 10092; -.
DR DisGeNET; 10092; -.
DR GeneCards; ARPC5; -.
DR HGNC; HGNC:708; ARPC5.
DR HPA; ENSG00000162704; Low tissue specificity.
DR MIM; 604227; gene.
DR neXtProt; NX_O15511; -.
DR OpenTargets; ENSG00000162704; -.
DR PharmGKB; PA25003; -.
DR VEuPathDB; HostDB:ENSG00000162704; -.
DR eggNOG; KOG3380; Eukaryota.
DR GeneTree; ENSGT00940000154654; -.
DR HOGENOM; CLU_101888_1_1_1; -.
DR InParanoid; O15511; -.
DR OMA; GMALPGW; -.
DR OrthoDB; 1565115at2759; -.
DR PhylomeDB; O15511; -.
DR TreeFam; TF319716; -.
DR PathwayCommons; O15511; -.
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-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; O15511; -.
DR SIGNOR; O15511; -.
DR BioGRID-ORCS; 10092; 21 hits in 1089 CRISPR screens.
DR ChiTaRS; ARPC5; human.
DR GeneWiki; ARPC5; -.
DR GenomeRNAi; 10092; -.
DR Pharos; O15511; Tbio.
DR PRO; PR:O15511; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O15511; protein.
DR Bgee; ENSG00000162704; Expressed in monocyte and 205 other tissues.
DR ExpressionAtlas; O15511; baseline and differential.
DR Genevisible; O15511; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
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:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0051639; P:actin filament network formation; IEA:Ensembl.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:FlyBase.
DR GO; GO:0016477; P:cell migration; IMP:CACAO.
DR GO; GO:0097581; P:lamellipodium organization; IEA:Ensembl.
DR GO; GO:0030011; P:maintenance of cell polarity; IEA:Ensembl.
DR GO; GO:0061842; P:microtubule organizing center localization; IEA:Ensembl.
DR GO; GO:0021769; P:orbitofrontal cortex development; IEA:Ensembl.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
DR Gene3D; 1.25.40.190; -; 1.
DR InterPro; IPR006789; ARPC5.
DR InterPro; IPR036743; ARPC5_sf.
DR PANTHER; PTHR12644; PTHR12644; 1.
DR Pfam; PF04699; P16-Arc; 1.
DR PIRSF; PIRSF039096; p16-ARC; 1.
DR SUPFAM; SSF69103; SSF69103; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..151
FT /note="Actin-related protein 2/3 complex subunit 5"
FT /id="PRO_0000124054"
FT REGION 21..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 48
FT /note="Q -> HSIT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024028"
SQ SEQUENCE 151 AA; 16320 MW; F050B11774EA6E66 CRC64;
MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK
NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN
SSAMLLQWHE KALAAGGVGS IVRVLTARKT V
