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}.
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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
//
