ID   ARP2_ACACA              Reviewed;         388 AA.
AC   P53487;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Actin-related protein 2;
DE   AltName: Full=Actin-like protein 2;
GN   Name=arp2;
OS   Acanthamoeba castellanii (Amoeba).
OC   Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC   Acanthamoebidae; Acanthamoeba.
OX   NCBI_TaxID=5755;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 30010 / Neff;
RX   PubMed=7593166; DOI=10.1083/jcb.131.2.385;
RA   Kelleher J.F., Atkinson S.J., Pollard T.D.;
RT   "Sequences, structural models, and cellular localization of the actin-
RT   related proteins Arp2 and Arp3 from Acanthamoeba.";
RL   J. Cell Biol. 131:385-397(1995).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Arp2/3 complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:O96621}. Cell projection
CC       {ECO:0000250|UniProtKB:O96621}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {ECO:0000305}.
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DR   EMBL; U29609; AAC46911.1; -; mRNA.
DR   AlphaFoldDB; P53487; -.
DR   SMR; P53487; -.
DR   IntAct; P53487; 1.
DR   VEuPathDB; AmoebaDB:ACA1_074650; -.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IEA:InterPro.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProt.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
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.
FT   CHAIN           1..388
FT                   /note="Actin-related protein 2"
FT                   /id="PRO_0000089072"
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   388 AA;  44269 MW;  456C31CDC70B4F70 CRC64;
     MTDSSKVIVC DNGTGFVKCG FARSNFPASI FPSMVGRPIL RSEEKFDNVE IKDIMVGDEA
     SKLRSMLQIT YPLDNGIVRN WEDAEHVWNY TFFEKLKVDP KDCKILLTEP PMNPLANREK
     MVQVMFEKYG FKAAYIAIQA VLTLYAQGLL TGVVVDSGDG VTHIVPVYEG FSLPHLTRRL
     NVAGRDVTRY LIKLLLLRGY VFNRTADFET VRQIKEKFCY VGYDLELEKR LALETTTLVE
     KYTLPDGRVI PIGAERFEAP ECMFNPALVD QESVGVGELV FDCINKADID TRAEFYNHIV
     LSGGSTMYPG LPSRLEKEIK RLYFERVAKG NKVSMQKFKC RIEDPPRRKH MVFLGGAVLA
     EIMKDKTAFW MNKSEYEEQG PRVLRKCF