ARP2B_DANRE
ID ARP2B_DANRE Reviewed; 394 AA.
AC Q56A35;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Actin-related protein 2-B;
DE AltName: Full=Actin-like protein 2-B;
GN Name=actr2b; Synonyms=arp2b; ORFNames=si:dkey-66m17.2, zgc:110550;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Testis;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-binding component of the Arp2/3 complex, a multiprotein
CC complex that mediates actin polymerization upon stimulation by
CC nucleation-promoting factor (NPF) (By similarity). The Arp2/3 complex
CC mediates the formation of branched actin networks in the cytoplasm,
CC providing the force for cell motility (By similarity). Seems to contact
CC the pointed end of the daughter actin filament (By similarity). In
CC 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 (By
CC similarity). The Arp2/3 complex promotes homologous recombination (HR)
CC repair in response to DNA damage by promoting nuclear actin
CC polymerization, leading to drive motility of double-strand breaks
CC (DSBs) (By similarity). {ECO:0000250|UniProtKB:P61160,
CC ECO:0000250|UniProtKB:Q7ZTP2}.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of actr2/arp2,
CC actr3/arp3, arpc1b, arpc2, arpc3, arpc4 and arpc5.
CC {ECO:0000250|UniProtKB:Q7ZTP2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q7ZTP2}. Cell projection
CC {ECO:0000250|UniProtKB:Q7ZTP2}. Nucleus {ECO:0000250|UniProtKB:Q7ZTP2}.
CC -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {ECO:0000305}.
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DR EMBL; BX629343; CAN88750.1; -; Genomic_DNA.
DR EMBL; BC092187; AAH92187.1; -; mRNA.
DR EMBL; BC153558; AAI53559.1; -; mRNA.
DR RefSeq; NP_001017542.1; NM_001017542.2.
DR RefSeq; XP_005169567.1; XM_005169510.3.
DR AlphaFoldDB; Q56A35; -.
DR SMR; Q56A35; -.
DR STRING; 7955.ENSDARP00000093331; -.
DR PaxDb; Q56A35; -.
DR Ensembl; ENSDART00000102555; ENSDARP00000093331; ENSDARG00000070076.
DR GeneID; 554861; -.
DR KEGG; dre:554861; -.
DR CTD; 554861; -.
DR ZFIN; ZDB-GENE-050410-4; actr2b.
DR eggNOG; KOG0677; Eukaryota.
DR GeneTree; ENSGT00940000154556; -.
DR HOGENOM; CLU_027965_0_0_1; -.
DR InParanoid; Q56A35; -.
DR OMA; WDDMKYL; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; Q56A35; -.
DR TreeFam; TF300467; -.
DR Reactome; R-DRE-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DRE-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DRE-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q56A35; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000070076; Expressed in granulocyte and 20 other tissues.
DR ExpressionAtlas; Q56A35; baseline.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; IMP:ZFIN.
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 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..394
FT /note="Actin-related protein 2-B"
FT /id="PRO_0000327248"
FT BINDING 160..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A7MB62"
FT BINDING 214..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A7MB62"
FT BINDING 305..310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A7MB62"
SQ SEQUENCE 394 AA; 44702 MW; 84C3151B1FD37BE1 CRC64;
MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTAKVGNI EIKDLMVGDE
ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI NSRDCKILLT EPPMNPTKNR
EKIIEVMFET YQFTGVYIAI QAVLTLYAQG LLTGVVVDSG DGVTHICPVY EGFSLPHLTR
RLDIAGRDIT RYLIKLLLLR GYAFNHSADF ETVRMMKENL CYVGYNIEQE QKLALETTVL
VESYTLPDGR VIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRAEFYKH
IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVDKLSKF KIRIEDPPRR KHMVFLGGAV
LADIMKDKDN FWLTREEYQE KGVRVLEKLG VTVR
