ARPC2_DICDI
ID ARPC2_DICDI Reviewed; 293 AA.
AC O96623; Q54RY9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Actin-related protein 2/3 complex subunit 2;
DE AltName: Full=Arp2/3 complex 34 kDa subunit;
DE Short=p34-ARC;
GN Name=arcB; Synonyms=Arc35, arpE; ORFNames=DDB_G0282813;
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=AX3;
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 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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16782229; DOI=10.1016/j.ejcb.2006.05.008;
RA Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R.;
RT "Identification and isolation of Dictyostelium microtubule-associated
RT protein interactors by tandem affinity purification.";
RL Eur. J. Cell Biol. 85:1079-1090(2006).
RN [5]
RP FUNCTION, AND MUTAGENESIS.
RX PubMed=17553489; DOI=10.1016/j.yexcr.2007.04.029;
RA Langridge P.D., Kay R.R.;
RT "Mutants in the Dictyostelium Arp2/3 complex and chemoattractant-induced
RT actin polymerization.";
RL Exp. Cell Res. 313:2563-2574(2007).
RN [6]
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 ECO:0000269|PubMed:17553489}.
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. Cell projection.
CC Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection,
CC pseudopodium.
CC -!- SIMILARITY: Belongs to the ARPC2 family. {ECO:0000305}.
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DR EMBL; AF095931; AAC99778.1; -; mRNA.
DR EMBL; AAFI02000047; EAL65986.1; -; Genomic_DNA.
DR RefSeq; XP_639348.1; XM_634256.1.
DR AlphaFoldDB; O96623; -.
DR SMR; O96623; -.
DR STRING; 44689.DDB0214935; -.
DR PaxDb; O96623; -.
DR EnsemblProtists; EAL65986; EAL65986; DDB_G0282813.
DR GeneID; 8623789; -.
DR KEGG; ddi:DDB_G0282813; -.
DR dictyBase; DDB_G0282813; arcB.
DR eggNOG; KOG2826; Eukaryota.
DR HOGENOM; CLU_059439_1_0_1; -.
DR InParanoid; O96623; -.
DR OMA; GPYIVSP; -.
DR PhylomeDB; O96623; -.
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-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:O96623; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:dictyBase.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
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:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; TAS:dictyBase.
DR GO; GO:0030041; P:actin filament polymerization; IMP: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; 3.30.1460.20; -; 2.
DR InterPro; IPR007188; ARPC2.
DR InterPro; IPR034666; ARPC2/4.
DR PANTHER; PTHR12058; PTHR12058; 1.
DR Pfam; PF04045; P34-Arc; 1.
DR SUPFAM; SSF69645; SSF69645; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..293
FT /note="Actin-related protein 2/3 complex subunit 2"
FT /id="PRO_0000124036"
SQ SEQUENCE 293 AA; 32932 MW; A3220726D708CBD8 CRC64;
MLLLETHNRI LYDEVISHFE GDRRVNNIFA DFDGVKFNVQ TSDDKSSLMV SVSLHAAADL
LKNGGSALLK SVYGDMLQAK PEGGYDVTLV IQSSFSGNKE ELAKKVSLLK RHLVAAPFLM
VFEGIEAKKP LPEIIAINYR TDETFYLKPQ GDNVIVIFDI AFKDADDVIL SKIFLQSFVD
VRKTISNVPS ITFSQKDPPL ELKGVKGVRA GQANHGFVSF VLFPAHIKKP QESADLIQTF
RDYLHYHIKC AKGYMHTSMR NRVESLIQVL NRAKPEPVNT VKRTITGKFF KQN
