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 05-DEC-2018, entry version 162. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 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] (ISOFORM 1), AND IDENTIFICATION IN THE RP ARP2/2 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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., 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 [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 RT project: 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., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric 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., 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 [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 RT subunit 5 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 RP SPECTROMETRY [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., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal 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., 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 [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., 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 [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., 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: Component of the Arp2/3 complex, a multiprotein complex CC that mediates actin polymerization upon stimulation by nucleation- CC promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex CC mediates the formation of branched actin networks in the CC cytoplasm, providing the force for cell motility (PubMed:9230079). CC In addition to its role in the cytoplasmic cytoskeleton, the CC Arp2/3 complex also promotes actin polymerization in the nucleus, CC thereby regulating gene transcription and repair of damaged DNA 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). 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, CC ARPC4/p20-ARC 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 CC {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 Note=No experimental confirmation available.; CC -!- PTM: Polyubiquitinated by RNF128 with 'Lys-63'-linked chains, CC leading 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 UniGene; Hs.518609; -. DR ProteinModelPortal; O15511; -. DR SMR; O15511; -. DR BioGrid; 115399; 61. DR CORUM; O15511; -. DR DIP; DIP-33144N; -. DR IntAct; O15511; 27. DR STRING; 9606.ENSP00000352918; -. DR DrugBank; DB08235; N-[2-(2-methyl-1H-indol-3-yl)ethyl]thiophene-2-carboxamide. DR iPTMnet; O15511; -. DR PhosphoSitePlus; O15511; -. DR BioMuta; ARPC5; -. DR OGP; O15511; -. DR SWISS-2DPAGE; O15511; -. DR EPD; O15511; -. DR MaxQB; O15511; -. DR PaxDb; O15511; -. DR PeptideAtlas; O15511; -. DR PRIDE; O15511; -. DR ProteomicsDB; 48703; -. DR ProteomicsDB; 48704; -. [O15511-2] DR TopDownProteomics; O15511-1; -. [O15511-1] DR TopDownProteomics; O15511-2; -. [O15511-2] DR DNASU; 10092; -. DR Ensembl; ENST00000294742; ENSP00000294742; ENSG00000162704. [O15511-2] DR Ensembl; ENST00000359856; ENSP00000352918; ENSG00000162704. [O15511-1] DR GeneID; 10092; -. DR KEGG; hsa:10092; -. DR UCSC; uc021pgb.3; human. [O15511-1] DR CTD; 10092; -. DR DisGeNET; 10092; -. DR EuPathDB; HostDB:ENSG00000162704.15; -. DR GeneCards; ARPC5; -. DR HGNC; HGNC:708; ARPC5. DR HPA; HPA022013; -. DR HPA; HPA031972; -. DR MIM; 604227; gene. DR neXtProt; NX_O15511; -. DR OpenTargets; ENSG00000162704; -. DR PharmGKB; PA25003; -. DR eggNOG; KOG3380; Eukaryota. DR eggNOG; ENOG4111FGV; LUCA. DR GeneTree; ENSGT00940000154654; -. DR HOGENOM; HOG000197215; -. DR HOVERGEN; HBG050583; -. DR InParanoid; O15511; -. DR KO; K05754; -. DR OMA; GCIVRAM; -. DR OrthoDB; EOG091G0R2J; -. DR PhylomeDB; O15511; -. DR TreeFam; TF319716; -. 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 SIGNOR; O15511; -. DR ChiTaRS; ARPC5; human. DR GeneWiki; ARPC5; -. DR GenomeRNAi; 10092; -. DR PRO; PR:O15511; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000162704; Expressed in 234 organ(s), highest expression level in bone marrow. DR CleanEx; HS_ARPC5; -. 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:0051015; F:actin filament binding; IBA:GO_Central. 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:0048013; P:ephrin receptor signaling pathway; TAS:Reactome. DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome. DR GO; GO:0097581; P:lamellipodium organization; IEA:Ensembl. DR GO; GO:0030011; P:maintenance of cell polarity; IEA:Ensembl. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0061842; P:microtubule organizing center localization; IEA:Ensembl. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0021769; P:orbitofrontal cortex development; IEA:Ensembl. 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 Acetylation; Actin-binding; Alternative splicing; Cell projection; KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW Nucleus; Reference proteome; Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378, FT ECO:0000269|PubMed:12665801}. FT CHAIN 2 151 Actin-related protein 2/3 complex subunit FT 5. FT /FTId=PRO_0000124054. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000244|PubMed:22814378}. FT VAR_SEQ 48 48 Q -> HSIT (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=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 //