ID   ARPC5_PONAB             Reviewed;         151 AA.
AC   Q5R516;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 98.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR926014; CAI29651.1; -; mRNA.
DR   EMBL; CR861069; CAH93150.1; -; mRNA.
DR   RefSeq; NP_001127685.1; NM_001134213.1.
DR   AlphaFoldDB; Q5R516; -.
DR   SMR; Q5R516; -.
DR   STRING; 9601.ENSPPYP00000000483; -.
DR   Ensembl; ENSPPYT00000000503; ENSPPYP00000000483; ENSPPYG00000000425.
DR   GeneID; 100174767; -.
DR   KEGG; pon:100174767; -.
DR   CTD; 10092; -.
DR   eggNOG; KOG3380; Eukaryota.
DR   GeneTree; ENSGT00940000154654; -.
DR   HOGENOM; CLU_101888_1_1_1; -.
DR   InParanoid; Q5R516; -.
DR   OrthoDB; 1565115at2759; -.
DR   TreeFam; TF319716; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:Ensembl.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW   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_0000124056"
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"
SQ   SEQUENCE   151 AA;  16320 MW;  F050B11774EA6E66 CRC64;
     MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK
     NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN
     SSAMLLQWHE KALAAGGVGS IVRVLTARKT V