ARC1B_MOUSE
ID ARC1B_MOUSE Reviewed; 372 AA.
AC Q9WV32; Q9CRC4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 165.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Mann M., Okano K., Oppedisano L., Truscott E., Varmuza S.;
RT "Analysis of parental allele-specific expression of genes showing altered
RT expression in parthenogenetic embryos.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Cerebellum, Heart, Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:O15143}.
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; AF162768; AAD43352.1; -; mRNA.
DR EMBL; AK002274; BAB21980.1; -; mRNA.
DR EMBL; AK005378; BAB23985.1; -; mRNA.
DR EMBL; AK147731; BAE28101.1; -; mRNA.
DR EMBL; AK148145; BAE28373.1; -; mRNA.
DR EMBL; AK159371; BAE35028.1; -; mRNA.
DR EMBL; AK167978; BAE39970.1; -; mRNA.
DR EMBL; AK168774; BAE40610.1; -; mRNA.
DR EMBL; AK172124; BAE42835.1; -; mRNA.
DR EMBL; CH466529; EDL19001.1; -; Genomic_DNA.
DR EMBL; CH466529; EDL19002.1; -; Genomic_DNA.
DR EMBL; BC003441; AAH03441.1; -; mRNA.
DR CCDS; CCDS19856.1; -.
DR RefSeq; NP_075631.2; NM_023142.2.
DR PDB; 7AQK; EM; 9.00 A; c=1-371.
DR PDBsum; 7AQK; -.
DR AlphaFoldDB; Q9WV32; -.
DR SMR; Q9WV32; -.
DR BioGRID; 198208; 20.
DR IntAct; Q9WV32; 4.
DR MINT; Q9WV32; -.
DR STRING; 10090.ENSMUSP00000082822; -.
DR iPTMnet; Q9WV32; -.
DR PhosphoSitePlus; Q9WV32; -.
DR SwissPalm; Q9WV32; -.
DR EPD; Q9WV32; -.
DR jPOST; Q9WV32; -.
DR MaxQB; Q9WV32; -.
DR PaxDb; Q9WV32; -.
DR PRIDE; Q9WV32; -.
DR ProteomicsDB; 283198; -.
DR Antibodypedia; 1378; 221 antibodies from 32 providers.
DR DNASU; 11867; -.
DR Ensembl; ENSMUST00000085679; ENSMUSP00000082822; ENSMUSG00000029622.
DR GeneID; 11867; -.
DR KEGG; mmu:11867; -.
DR UCSC; uc009amb.2; mouse.
DR CTD; 10095; -.
DR MGI; MGI:1343142; Arpc1b.
DR VEuPathDB; HostDB:ENSMUSG00000029622; -.
DR eggNOG; KOG1523; Eukaryota.
DR GeneTree; ENSGT00950000183183; -.
DR HOGENOM; CLU_034396_1_0_1; -.
DR InParanoid; Q9WV32; -.
DR OMA; TLKGSTW; -.
DR OrthoDB; 848569at2759; -.
DR PhylomeDB; Q9WV32; -.
DR TreeFam; TF315041; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR BioGRID-ORCS; 11867; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Arpc1b; mouse.
DR PRO; PR:Q9WV32; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9WV32; protein.
DR Bgee; ENSMUSG00000029622; Expressed in granulocyte and 241 other tissues.
DR ExpressionAtlas; Q9WV32; baseline and differential.
DR Genevisible; Q9WV32; MM.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0036284; C:tubulobulbar complex; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:MGI.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR030141; ARC1B.
DR InterPro; IPR017383; ARPC1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10709; PTHR10709; 1.
DR PANTHER; PTHR10709:SF10; PTHR10709:SF10; 1.
DR Pfam; PF00400; WD40; 2.
DR PIRSF; PIRSF038093; ARP2/3_su1; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 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_0000050856"
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 112
FT /note="A -> R (in Ref. 1; AAD43352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41064 MW; 0315BFB6E8697D89 CRC64;
MAYHSFLVEP ISCHAWNKDR TQIAICPNNH EVHIYEKSGA KWNKVHELKE HNGQVTGIDW
APESNRIVTC GTDRNAYVWT LKGRTWKPTL VILRINRAAR CVRWAPNENK FAVGSGSRVI
SICYFEQEND WWVCKHIKKP IRSTVLSLDW HPNNVLLAAG SCDFKCRIFS AYIKEVEERP
APTPWGSKMP FGELMFESSS SCGWVHGVCF SASGSRVAWV SHDSTVCLVD ADKKMAVATL
ASETLPLLAV TFITENSLVA AGHDCFPVLF TYDNAAVTLS FGGRLDVPKQ SSQRGMTARE
RFQNLDKKAS SEGGAATGAG LDSLHKNSVS QISVLSGGKA KCSQFCTTGM DGGMSIWDVK
SLESALKDLK IK
