ID ARC1B_BOVIN Reviewed; 372 AA. AC Q58CQ2; Q0V8Q8; Q58DS1; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 138. DE RecName: Full=Actin-related protein 2/3 complex subunit 1B; DE AltName: Full=Arp2/3 complex 41 kDa subunit; DE AltName: Full=p41-ARC; GN Name=ARPC1B; 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 [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF THE 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 THE ARP2/3 COMPLEX WITH BOUND RP 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: Component of the Arp2/3 complex, a multiprotein complex that CC mediates actin polymerization upon stimulation by nucleation-promoting CC factor (NPF). The Arp2/3 complex mediates the formation of branched CC actin networks in the cytoplasm, providing the force for cell motility. CC In 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. The Arp2/3 CC complex promotes homologous recombination (HR) repair in response to CC DNA damage by promoting nuclear actin polymerization, leading to drive CC motility of double-strand breaks (DSBs). CC {ECO:0000250|UniProtKB:O15143}. 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. {ECO:0000269|PubMed:11721045, CC ECO:0000269|PubMed:15505213}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:O15143}. Nucleus {ECO:0000250|UniProtKB:O15143}. CC -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BT021526; AAX46373.1; -; mRNA. DR EMBL; BT021895; AAX46742.1; -; mRNA. DR EMBL; BT026160; ABG66999.1; -; mRNA. DR EMBL; BC102942; AAI02943.1; -; mRNA. DR RefSeq; NP_001014844.1; NM_001014844.3. DR PDB; 1K8K; X-ray; 2.00 A; C=1-372. DR PDB; 1TYQ; X-ray; 2.55 A; C=1-372. DR PDB; 1U2V; X-ray; 2.55 A; C=1-372. DR PDB; 2P9I; X-ray; 2.46 A; C=1-372. DR PDB; 2P9K; X-ray; 2.59 A; C=1-372. DR PDB; 2P9L; X-ray; 2.65 A; C=1-372. DR PDB; 2P9N; X-ray; 2.85 A; C=1-372. DR PDB; 2P9P; X-ray; 2.90 A; C=1-372. DR PDB; 2P9S; X-ray; 2.68 A; C=1-372. DR PDB; 2P9U; X-ray; 2.75 A; C=1-372. DR PDB; 3DXK; X-ray; 2.70 A; C=1-372. DR PDB; 3DXM; X-ray; 2.85 A; C=1-372. DR PDB; 3RSE; X-ray; 2.65 A; C=1-372. DR PDB; 3UKR; X-ray; 2.48 A; C=1-372. DR PDB; 3UKU; X-ray; 2.75 A; C=1-372. DR PDB; 3ULE; X-ray; 2.50 A; C=1-372. DR PDB; 4JD2; X-ray; 3.08 A; C=1-372. DR PDB; 4XEI; X-ray; 3.87 A; C=1-372. DR PDB; 4XF2; X-ray; 5.00 A; C/V=1-372. DR PDB; 6DEC; X-ray; 4.60 A; C/J=1-372. DR PDB; 7JPN; EM; 3.24 A; C=1-372. DR PDB; 7TPT; EM; 3.90 A; C=1-372. 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 PDBsum; 7TPT; -. DR AlphaFoldDB; Q58CQ2; -. DR EMDB; EMD-22416; -. DR EMDB; EMD-26063; -. DR SMR; Q58CQ2; -. DR DIP; DIP-29791N; -. DR IntAct; Q58CQ2; 8. DR STRING; 9913.ENSBTAP00000056302; -. DR PaxDb; 9913-ENSBTAP00000056302; -. DR PeptideAtlas; Q58CQ2; -. DR Ensembl; ENSBTAT00000064158.2; ENSBTAP00000056302.1; ENSBTAG00000046248.2. DR GeneID; 326600; -. DR KEGG; bta:326600; -. DR CTD; 10095; -. DR VEuPathDB; HostDB:ENSBTAG00000046248; -. DR VGNC; VGNC:26164; ARPC1B. DR eggNOG; KOG1523; Eukaryota. DR GeneTree; ENSGT00950000183183; -. DR HOGENOM; CLU_034396_1_0_1; -. DR InParanoid; Q58CQ2; -. DR OMA; TLKGSTW; -. DR OrthoDB; 5471154at2759; -. DR TreeFam; TF315041; -. DR Reactome; R-BTA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-BTA-3928662; EPHB-mediated forward signaling. DR Reactome; R-BTA-5663213; RHO GTPases Activate WASPs and WAVEs. DR EvolutionaryTrace; Q58CQ2; -. DR Proteomes; UP000009136; Chromosome 25. DR Bgee; ENSBTAG00000046248; Expressed in blood and 106 other cell types or tissues. DR GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl. DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR017383; ARPC1. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR10709; ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 1; 1. DR PANTHER; PTHR10709:SF10; ACTIN-RELATED PROTEIN 2_3 COMPLEX SUBUNIT 1B; 1. DR Pfam; PF00400; WD40; 2. DR PIRSF; PIRSF038093; ARP2/3_su1; 1. DR SMART; SM00320; WD40; 5. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Nucleus; KW Reference proteome; Repeat; WD repeat. FT CHAIN 1..372 FT /note="Actin-related protein 2/3 complex subunit 1B" FT /id="PRO_0000239701" FT REPEAT 6..45 FT /note="WD 1" FT REPEAT 50..89 FT /note="WD 2" FT REPEAT 94..135 FT /note="WD 3" FT REPEAT 140..179 FT /note="WD 4" FT REPEAT 242..280 FT /note="WD 5" FT REPEAT 324..367 FT /note="WD 6" FT CONFLICT 66 FT /note="R -> H (in Ref. 1; AAX46742)" FT /evidence="ECO:0000305" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 20..25 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 28..38 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 41..49 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 62..65 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:3UKU" FT STRAND 76..82 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 99..104 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 108..115 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 118..126 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 127..130 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 131..137 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 154..161 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 166..170 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 194..197 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:2P9K" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 212..221 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:2P9I" FT STRAND 247..254 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 257..262 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 268..273 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 274..277 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 278..281 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 298..304 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 322..327 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 329..337 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 338..340 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 343..349 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 352..358 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 359..365 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 366..368 FT /evidence="ECO:0007829|PDB:7JPN" SQ SEQUENCE 372 AA; 40976 MW; B412F9C50DC93748 CRC64; MAYHSFLVEP ISCHAWNKDR TQIAICPNNH EVHIYEKSGN KWVQVHELKE HNGQVTGIDW APDSNRIVTC GTDRNAYVWT LKGRTWKPTL VILRINRAAR CVRWAPNEKK FAVGSGSRVI SICYFEQEND WWVCKHIKKP IRSTVLSLDW HPNSVLLAAG SCDFKCRIFS AYIKEVEERP APTPWGSKMP FGELMFESSS SCGWVHGVCF SANGSRVAWV SHDSTVCLAD ADKKMAVATL ASETLPLLAV TFITESSLVA AGHDCFPVLF TYDSAAGKLS FGGRLDVPKQ SSQRGLTARE RFQNLDKKAS SEGSAAAGAG LDSLHKNSVS QISVLSGGKA KCSQFCTTGM DGGMSIWDVR SLESALKDLK IV //