ARP2_DICDI
ID ARP2_DICDI Reviewed; 392 AA.
AC O96621; Q559Q9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Actin-related protein 2;
DE AltName: Full=Actin-like protein 2;
DE AltName: Full=Actin-related protein B;
GN Name=arpB; Synonyms=arp2; ORFNames=DDB_G0272106;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [4]
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 [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 ATP-binding component of the Arp2/3 complex
CC which is involved in regulation of actin polymerization and together
CC with an activating nucleation-promoting factor (NPF) mediates the
CC formation of branched actin networks. Seems to contact the pointed end
CC of the daughter actin filament. The Arp2/3 complex is involved in
CC organizing the actin system in cell motility and chemotaxis, in
CC phagocytosis and macropinocytosis, at late steps of endosome
CC processing, and in mitosis. In concert with a group of other proteins,
CC the Arp2/3 complex plays a general role in the rapid activation and
CC adaptation of the actin system to its multiple functions.
CC {ECO:0000269|PubMed:11807934, 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
CC {ECO:0000269|PubMed:11807934}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:11425877}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:11425877}. Cell projection, pseudopodium
CC {ECO:0000269|PubMed:11425877}.
CC -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {ECO:0000305}.
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DR EMBL; AF095929; AAC99776.1; -; mRNA.
DR EMBL; AAFI02000008; EAL71205.1; -; Genomic_DNA.
DR RefSeq; XP_645275.1; XM_640183.1.
DR AlphaFoldDB; O96621; -.
DR SMR; O96621; -.
DR STRING; 44689.DDB0185179; -.
DR PaxDb; O96621; -.
DR EnsemblProtists; EAL71205; EAL71205; DDB_G0272106.
DR GeneID; 8618441; -.
DR KEGG; ddi:DDB_G0272106; -.
DR dictyBase; DDB_G0272106; arpB.
DR eggNOG; KOG0677; Eukaryota.
DR HOGENOM; CLU_027965_0_0_1; -.
DR InParanoid; O96621; -.
DR OMA; WEDMQHL; -.
DR PhylomeDB; O96621; -.
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:O96621; -.
DR Proteomes; UP000002195; Chromosome 2.
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:0009358; C:polyphosphate kinase complex; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; TAS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030041; P:actin filament polymerization; IMP:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:dictyBase.
DR GO; GO:0032060; P:bleb assembly; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0006887; P:exocytosis; IEP:dictyBase.
DR GO; GO:0006972; P:hyperosmotic response; IEP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IEP:dictyBase.
DR GO; GO:0046689; P:response to mercury ion; IDA:dictyBase.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR027306; Arp2.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF149; PTHR11937:SF149; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..392
FT /note="Actin-related protein 2"
FT /id="PRO_0000327509"
FT BINDING 158..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 212..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 303..308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 392 AA; 44238 MW; 1BC8D7C0C3222304 CRC64;
MDSNKVIVMD NGTGFVKCGF AGANFPTAIF PSMVGRPILR SEEKVENVEI KDIMVGDEAA
KLRSMLQITY PLENGIIRNW DDITHVWDYA LKEKLKVSDP TECKILLTEP PMNPVANRQK
MIECMFEKYG FQAVYVAIQA VLTLYAQGLL TGVVVDSGDG VTHIIPVYEG YSIPHLTRRL
DVAGRDVTRY LIKLLLLRGY AFNRTADFET IRQIKEKLCY VAYDVQQEMK LASETTVLVE
NYTLPDGRVI KVGQERFQAS EALFNPSLVD VEGGGVHEQL FDCITKADRD LQQGFYQHIV
LSGGSSMYPG LPSRLEKEIR SLYLERVLKG NKEGLAKFKC RIEDPPRRKH MVFLGGAVLA
DLTKDRDDFW ITKAEYMEKG FGALDKLTKL SV
