ARP3_BOVIN
ID ARP3_BOVIN Reviewed; 418 AA.
AC P61157; A5PJ90; P32391; Q08DS8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Actin-related protein 3;
DE AltName: Full=Actin-2;
DE AltName: Full=Actin-like protein 3;
GN Name=ACTR3; Synonyms=ARP3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=1530599; DOI=10.1016/0006-291x(92)91299-6;
RA Tanaka T., Shibasaki F., Ishikawa M., Hirano N., Sakai R., Nishida J.,
RA Takenawa T., Hirai H.;
RT "Molecular cloning of bovine actin-like protein, actin2.";
RL Biochem. Biophys. Res. Commun. 187:1022-1028(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF ARP2/3 COMPLEX.
RX PubMed=11721045; DOI=10.1126/science.1066333;
RA Robinson R.C., Turbedsky K., Kaiser D.A., Marchand J.-B., Higgs H.N.,
RA Choe S., Pollard T.D.;
RT "Crystal structure of Arp2/3 complex.";
RL Science 294:1679-1684(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF ARP2/3 COMPLEX WITH BOUND ATP.
RX PubMed=15505213; DOI=10.1073/pnas.0407149101;
RA Nolen B.J., Littlefield R.S., Pollard T.D.;
RT "Crystal structures of actin-related protein 2/3 complex with bound ATP or
RT ADP.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15627-15632(2004).
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). The Arp2/3 complex mediates the
CC formation of branched actin networks in the cytoplasm, providing the
CC force for cell motility. Seems to contact the pointed end of the
CC daughter actin filament. In podocytes, required for the formation of
CC lamellipodia downstream of AVIL and PLCE1 regulation. In addition to
CC its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also
CC promotes actin polymerization in the nucleus, thereby regulating gene
CC transcription and repair of damaged DNA. The Arp2/3 complex promotes
CC homologous recombination (HR) repair in response to DNA damage by
CC promoting nuclear actin polymerization, leading to drive motility of
CC double-strand breaks (DSBs). Plays a role in ciliogenesis.
CC {ECO:0000250|UniProtKB:P61158}.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2,
CC ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC
CC and ARPC5/p16-ARC (PubMed:11721045, PubMed:15505213). Interacts with
CC WHDC1. Interacts weakly with MEFV. Interacts with AVIL (By similarity).
CC {ECO:0000250|UniProtKB:P61158, ECO:0000269|PubMed:11721045,
CC ECO:0000269|PubMed:15505213}.
CC -!- INTERACTION:
CC P61157; Q60598: Cttn; Xeno; NbExp=4; IntAct=EBI-351419, EBI-397955;
CC P61157; Q00944: PTK2; Xeno; NbExp=5; IntAct=EBI-351419, EBI-2896409;
CC P61157; O00401: WASL; Xeno; NbExp=3; IntAct=EBI-351419, EBI-957615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P61158}. Cell projection
CC {ECO:0000250|UniProtKB:P61158}. Nucleus {ECO:0000250|UniProtKB:P61158}.
CC Note=In pre-apoptotic cells, colocalizes with MEFV in large specks
CC (pyroptosomes). {ECO:0000250|UniProtKB:P61158}.
CC -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. {ECO:0000305}.
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DR EMBL; D12816; BAA02249.1; -; mRNA.
DR EMBL; BC123582; AAI23583.1; -; mRNA.
DR EMBL; BC142009; AAI42010.1; -; mRNA.
DR PIR; JQ1616; JQ1616.
DR RefSeq; NP_776651.1; NM_174226.2.
DR PDB; 1K8K; X-ray; 2.00 A; A=1-418.
DR PDB; 1TYQ; X-ray; 2.55 A; A=1-418.
DR PDB; 1U2V; X-ray; 2.55 A; A=1-418.
DR PDB; 2P9I; X-ray; 2.46 A; A=1-418.
DR PDB; 2P9K; X-ray; 2.59 A; A=1-418.
DR PDB; 2P9L; X-ray; 2.65 A; A=1-418.
DR PDB; 2P9N; X-ray; 2.85 A; A=1-418.
DR PDB; 2P9P; X-ray; 2.90 A; A=1-418.
DR PDB; 2P9S; X-ray; 2.68 A; A=1-418.
DR PDB; 2P9U; X-ray; 2.75 A; A=1-418.
DR PDB; 3DXK; X-ray; 2.70 A; A=1-418.
DR PDB; 3DXM; X-ray; 2.85 A; A=1-418.
DR PDB; 3RSE; X-ray; 2.65 A; A=1-418.
DR PDB; 3UKR; X-ray; 2.48 A; A=1-418.
DR PDB; 3UKU; X-ray; 2.75 A; A=1-418.
DR PDB; 3ULE; X-ray; 2.50 A; A=1-418.
DR PDB; 4JD2; X-ray; 3.08 A; A=1-418.
DR PDB; 4XEI; X-ray; 3.87 A; A=1-418.
DR PDB; 4XF2; X-ray; 5.00 A; A/T=1-418.
DR PDB; 6DEC; X-ray; 4.60 A; A/H=1-418.
DR PDB; 7JPN; EM; 3.24 A; A=3-415.
DR PDBsum; 1K8K; -.
DR PDBsum; 1TYQ; -.
DR PDBsum; 1U2V; -.
DR PDBsum; 2P9I; -.
DR PDBsum; 2P9K; -.
DR PDBsum; 2P9L; -.
DR PDBsum; 2P9N; -.
DR PDBsum; 2P9P; -.
DR PDBsum; 2P9S; -.
DR PDBsum; 2P9U; -.
DR PDBsum; 3DXK; -.
DR PDBsum; 3DXM; -.
DR PDBsum; 3RSE; -.
DR PDBsum; 3UKR; -.
DR PDBsum; 3UKU; -.
DR PDBsum; 3ULE; -.
DR PDBsum; 4JD2; -.
DR PDBsum; 4XEI; -.
DR PDBsum; 4XF2; -.
DR PDBsum; 6DEC; -.
DR PDBsum; 7JPN; -.
DR AlphaFoldDB; P61157; -.
DR SMR; P61157; -.
DR BioGRID; 158917; 3.
DR DIP; DIP-29790N; -.
DR IntAct; P61157; 7.
DR STRING; 9913.ENSBTAP00000004410; -.
DR PaxDb; P61157; -.
DR PeptideAtlas; P61157; -.
DR PRIDE; P61157; -.
DR Ensembl; ENSBTAT00000070638; ENSBTAP00000066597; ENSBTAG00000003401.
DR GeneID; 281597; -.
DR KEGG; bta:281597; -.
DR CTD; 10096; -.
DR VEuPathDB; HostDB:ENSBTAG00000003401; -.
DR VGNC; VGNC:50033; ACTR3.
DR eggNOG; KOG0678; Eukaryota.
DR GeneTree; ENSGT00940000155065; -.
DR HOGENOM; CLU_027965_3_0_1; -.
DR InParanoid; P61157; -.
DR OMA; TAEFKSY; -.
DR OrthoDB; 649708at2759; -.
DR EvolutionaryTrace; P61157; -.
DR PRO; PR:P61157; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000003401; Expressed in diaphragm and 107 other tissues.
DR ExpressionAtlas; P61157; baseline and differential.
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:0005829; C:cytosol; TAS:Reactome.
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:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR015623; Arp3.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF175; PTHR11937:SF175; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; ATP-binding; Cell projection;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61158"
FT CHAIN 2..418
FT /note="Actin-related protein 3"
FT /id="PRO_0000089078"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P61158"
FT MOD_RES 240
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61158"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61158"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61158"
FT MOD_RES 254
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61158"
FT CONFLICT 344
FT /note="D -> G (in Ref. 2; AAI23583)"
FT /evidence="ECO:0000305"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:2P9I"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3ULE"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 220..231
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 331..353
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 372..375
FT /evidence="ECO:0007829|PDB:2P9I"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 388..393
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 397..403
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 405..409
FT /evidence="ECO:0007829|PDB:1K8K"
SQ SEQUENCE 418 AA; 47371 MW; 23E5564198B81C63 CRC64;
MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF
FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY LRAEPEDHYF LLTEPPLNTP
ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV
AEGYVIGSCI KHIPIAGRDI TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK
EFNKYDTDGS KWIKQYTGIN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV
DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS EELSGGRLKP
KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS
