ID   ARPC5_RAT               Reviewed;         151 AA.
AC   Q4KLF8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 110.
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;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [2]
RP   PROTEIN SEQUENCE OF 13-23; 48-60; 82-87; 101-108 AND 132-143, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Diao W., Chen W.-Q.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that
CC       mediates actin polymerization upon stimulation by nucleation-promoting
CC       factor (NPF). The Arp2/3 complex mediates the formation of branched
CC       actin networks in the cytoplasm, providing the force for cell motility.
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. The Arp2/3
CC       complex promotes homologous recombination (HR) repair in response to
CC       DNA damage by promoting nuclear actin polymerization, leading to drive
CC       motility of double-strand breaks (DSBs).
CC       {ECO:0000250|UniProtKB:O15511}.
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:0000250|UniProtKB:O15511}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:O15511}. Cell projection
CC       {ECO:0000250|UniProtKB:O15511}. Nucleus {ECO:0000250|UniProtKB:O15511}.
CC   -!- PTM: Polyubiquitinated by RNF128 with 'Lys-63'-linked chains, leading
CC       to proteasomal degradation. {ECO:0000250|UniProtKB:O15511}.
CC   -!- SIMILARITY: Belongs to the ARPC5 family. {ECO:0000305}.
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DR   EMBL; BC099238; AAH99238.1; -; mRNA.
DR   RefSeq; NP_001020888.1; NM_001025717.1.
DR   AlphaFoldDB; Q4KLF8; -.
DR   SMR; Q4KLF8; -.
DR   BioGRID; 262257; 2.
DR   STRING; 10116.ENSRNOP00000061516; -.
DR   iPTMnet; Q4KLF8; -.
DR   PhosphoSitePlus; Q4KLF8; -.
DR   SwissPalm; Q4KLF8; -.
DR   jPOST; Q4KLF8; -.
DR   PaxDb; Q4KLF8; -.
DR   PRIDE; Q4KLF8; -.
DR   GeneID; 360854; -.
DR   KEGG; rno:360854; -.
DR   UCSC; RGD:1311791; rat.
DR   CTD; 10092; -.
DR   RGD; 1311791; Arpc5.
DR   VEuPathDB; HostDB:ENSRNOG00000028062; -.
DR   eggNOG; KOG3380; Eukaryota.
DR   HOGENOM; CLU_101888_1_1_1; -.
DR   InParanoid; Q4KLF8; -.
DR   OMA; GMALPGW; -.
DR   OrthoDB; 1565115at2759; -.
DR   PhylomeDB; Q4KLF8; -.
DR   TreeFam; TF319716; -.
DR   Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:Q4KLF8; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000028062; Expressed in Ammon's horn and 20 other tissues.
DR   ExpressionAtlas; Q4KLF8; baseline and differential.
DR   Genevisible; Q4KLF8; RN.
DR   GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IDA:RGD.
DR   GO; GO:0030426; C:growth cone; IDA:RGD.
DR   GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISO:RGD.
DR   GO; GO:0051639; P:actin filament network formation; IMP:RGD.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISO:RGD.
DR   GO; GO:0016477; P:cell migration; ISO:RGD.
DR   GO; GO:0097581; P:lamellipodium organization; IMP:RGD.
DR   GO; GO:0030011; P:maintenance of cell polarity; IMP:RGD.
DR   GO; GO:0061842; P:microtubule organizing center localization; IMP:RGD.
DR   GO; GO:0021769; P:orbitofrontal cortex development; IEP:RGD.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR   GO; GO:0014909; P:smooth muscle cell migration; IMP:RGD.
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; Cell projection; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Nucleus; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O15511"
FT   CHAIN           2..151
FT                   /note="Actin-related protein 2/3 complex subunit 5"
FT                   /id="PRO_0000269564"
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:0000250|UniProtKB:O15511"
FT   CONFLICT        103
FT                   /note="V -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  16320 MW;  F050B11774EA6E66 CRC64;
     MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK
     NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN
     SSAMLLQWHE KALAAGGVGS IVRVLTARKT V