ID   ARPC5_DICDI             Reviewed;         138 AA.
AC   O96626; Q54J29;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=arcE; Synonyms=Arc15, arpH; ORFNames=DDB_G0288319;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=AX2;
RX   PubMed=11807934; DOI=10.1002/cm.10005;
RA   Insall R., Mueller-Taubenberger A., Machesky L., Koehler J., Simmeth E.,
RA   Atkinson S.J., Weber I., Gerisch G.;
RT   "Dynamics of the Dictyostelium Arp2/3 complex in endocytosis, cytokinesis,
RT   and chemotaxis.";
RL   Cell Motil. Cytoskeleton 50:115-128(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 34-56, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=11425877; DOI=10.1083/jcb.153.7.1479;
RA   Jung G., Remmert K., Wu X., Volosky J.M., Hammer J.A. III;
RT   "The Dictyostelium CARMIL protein links capping protein and the Arp2/3
RT   complex to type I myosins through their SH3 domains.";
RL   J. Cell Biol. 153:1479-1497(2001).
RN   [4]
RP   IDENTIFICATION IN THE ARP2/3 COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=17296313; DOI=10.1016/j.pep.2007.01.001;
RA   Meima M.E., Weening K.E., Schaap P.;
RT   "Vectors for expression of proteins with single or combinatorial
RT   fluorescent protein and tandem affinity purification tags in
RT   Dictyostelium.";
RL   Protein Expr. Purif. 53:283-288(2007).
CC   -!- FUNCTION: Functions as component of the Arp2/3 complex which is
CC       involved in regulation of actin polymerization and together with an
CC       activating nucleation-promoting factor (NPF) mediates the formation of
CC       branched actin networks. Seems to contact the pointed end of the
CC       daughter actin filament. The Arp2/3 complex is involved in organizing
CC       the actin system in cell motility and chemotaxis, in phagocytosis and
CC       macropinocytosis, at late steps of endosome processing, and in mitosis.
CC       In concert with a group of other proteins, the Arp2/3 complex plays a
CC       general role in the rapid activation and adaptation of the actin system
CC       to its multiple functions. {ECO:0000269|PubMed:11807934}.
CC   -!- SUBUNIT: Component of the Arp2/3 complex composed of arpB/Arp2,
CC       arpC/Arp3, arcA/p41-arc, arcB/p34-arc, arcC/p21-arc, arcD/p20-arc and
CC       arcE/p16-arc. Interacts with carmil (via the region between the LRR
CC       domain and COOH-terminal proline-rich domain); carmil is required for
CC       Arp2/3-dependent actin nucleation. Arp2/3 complex, MyoB, MyoC, and the
CC       alpha and beta subunits of capping protein all form a larger complex
CC       with carmil. {ECO:0000269|PubMed:11425877,
CC       ECO:0000269|PubMed:17296313}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytosol.
CC       Cytoplasm, cell cortex. Cell projection, pseudopodium.
CC   -!- SIMILARITY: Belongs to the ARPC5 family. {ECO:0000305}.
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DR   EMBL; AF095934; AAC99781.1; -; mRNA.
DR   EMBL; AAFI02000111; EAL63256.1; -; Genomic_DNA.
DR   RefSeq; XP_636772.1; XM_631680.1.
DR   AlphaFoldDB; O96626; -.
DR   SMR; O96626; -.
DR   STRING; 44689.DDB0191138; -.
DR   PaxDb; O96626; -.
DR   EnsemblProtists; EAL63256; EAL63256; DDB_G0288319.
DR   GeneID; 8626575; -.
DR   KEGG; ddi:DDB_G0288319; -.
DR   dictyBase; DDB_G0288319; arcE.
DR   eggNOG; KOG3380; Eukaryota.
DR   HOGENOM; CLU_101888_2_0_1; -.
DR   InParanoid; O96626; -.
DR   OMA; SQIQGRN; -.
DR   PhylomeDB; O96626; -.
DR   Reactome; R-DDI-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-DDI-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:O96626; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IDA:dictyBase.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0030041; P:actin filament polymerization; TAS:dictyBase.
DR   GO; GO:0045010; P:actin nucleation; TAS:dictyBase.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IEP:dictyBase.
DR   GO; GO:0006909; P:phagocytosis; IEP:dictyBase.
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   1: Evidence at protein level;
KW   Actin-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..138
FT                   /note="Actin-related protein 2/3 complex subunit 5"
FT                   /id="PRO_0000327632"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   138 AA;  15137 MW;  03E76CC19F87613D CRC64;
     MNYEDDNVES GQAGKSDAEY KADIANREKE VTKALNAGKP QDALNVALAD PPIYTKTGAI
     KDQNATIVLN LLGSFKDKDV ETSVETLNDD QLDILMKYVY RGLATGENSP IFFKWHECVL
     KKGGAGTIIR VISEKKTV