ARC1B_HUMAN
ID ARC1B_HUMAN Reviewed; 372 AA.
AC O15143; Q9BU00;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 199.
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 {ECO:0000312|HGNC:HGNC:704}; Synonyms=ARC41;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN THE ARP2/3 COMPLEX.
RX PubMed=9230079; DOI=10.1083/jcb.138.2.375;
RA Welch M.D., Depace A.H., Verma S., Iwamatsu A., Mitchison T.J.;
RT "The human Arp2/3 complex is composed of evolutionarily conserved subunits
RT and is localized to cellular regions of dynamic actin filament assembly.";
RL J. Cell Biol. 138:375-384(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Placenta, and Skin;
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 [4]
RP PROTEIN SEQUENCE OF 2-20.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE ARP2/3 COMPLEX.
RX PubMed=11741539; DOI=10.1016/s1097-2765(01)00393-8;
RA Gournier H., Goley E.D., Niederstrasser H., Trinh T., Welch M.D.;
RT "Reconstitution of human Arp2/3 complex reveals critical roles of
RT individual subunits in complex structure and activity.";
RL Mol. Cell 8:1041-1052(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP INVOLVEMENT IN IMD71, AND VARIANTS IMD71 VAL-105 AND THR-238.
RX PubMed=28368018; DOI=10.1038/ncomms14816;
RA Kahr W.H., Pluthero F.G., Elkadri A., Warner N., Drobac M., Chen C.H.,
RA Lo R.W., Li L., Li R., Li Q., Thoeni C., Pan J., Leung G.,
RA Lara-Corrales I., Murchie R., Cutz E., Laxer R.M., Upton J., Roifman C.M.,
RA Yeung R.S., Brumell J.H., Muise A.M.;
RT "Loss of the Arp2/3 complex component ARPC1B causes platelet abnormalities
RT and predisposes to inflammatory disease.";
RL Nat. Commun. 8:14816-14816(2017).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29925947; DOI=10.1038/s41586-018-0237-5;
RA Schrank B.R., Aparicio T., Li Y., Chang W., Chait B.T., Gundersen G.G.,
RA Gottesman M.E., Gautier J.;
RT "Nuclear ARP2/3 drives DNA break clustering for homology-directed repair.";
RL Nature 559:61-66(2018).
CC -!- FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that
CC mediates actin polymerization upon stimulation by nucleation-promoting
CC factor (NPF) (PubMed:11741539, PubMed:9230079). The Arp2/3 complex
CC mediates the formation of branched actin networks in the cytoplasm,
CC providing the force for cell motility (PubMed:11741539,
CC PubMed:9230079). In addition to its role in the cytoplasmic
CC cytoskeleton, the Arp2/3 complex also promotes actin polymerization in
CC the nucleus, thereby regulating gene transcription and repair of
CC damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous
CC recombination (HR) repair in response to DNA damage by promoting
CC nuclear actin polymerization, leading to drive motility of double-
CC strand breaks (DSBs) (PubMed:29925947). {ECO:0000269|PubMed:11741539,
CC ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:9230079}.
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:11741539,
CC ECO:0000269|PubMed:9230079}.
CC -!- INTERACTION:
CC O15143; Q5ZTM4: legK2; Xeno; NbExp=3; IntAct=EBI-1044647, EBI-16631153;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11741539, ECO:0000269|PubMed:9230079}. Nucleus
CC {ECO:0000269|PubMed:29925947}.
CC -!- DISEASE: Immunodeficiency 71 with inflammatory disease and congenital
CC thrombocytopenia (IMD71) [MIM:617718]: An autosomal recessive disorder
CC characterized by platelet abnormalities, vasculitis, eosinophilia, and
CC predisposition to inflammatory diseases. {ECO:0000269|PubMed:28368018}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR EMBL; AF006084; AAB64189.1; -; mRNA.
DR EMBL; AC004922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002562; AAH02562.1; -; mRNA.
DR EMBL; BC002988; AAH02988.2; -; mRNA.
DR EMBL; BC007555; AAH07555.1; -; mRNA.
DR CCDS; CCDS5661.1; -.
DR RefSeq; NP_005711.1; NM_005720.3.
DR RefSeq; XP_006715888.1; XM_006715825.1.
DR RefSeq; XP_006715889.1; XM_006715826.1.
DR PDB; 6UHC; EM; 3.90 A; C=1-372.
DR PDB; 6YW6; EM; 4.20 A; C=1-372.
DR PDBsum; 6UHC; -.
DR PDBsum; 6YW6; -.
DR AlphaFoldDB; O15143; -.
DR SMR; O15143; -.
DR BioGRID; 115402; 129.
DR CORUM; O15143; -.
DR DIP; DIP-41254N; -.
DR IntAct; O15143; 63.
DR MINT; O15143; -.
DR STRING; 9606.ENSP00000389631; -.
DR ChEMBL; CHEMBL4295656; -.
DR DrugBank; DB08236; (2S)-2-(3-bromophenyl)-3-(5-chloro-2-hydroxyphenyl)-1,3-thiazolidin-4-one.
DR DrugBank; DB08235; N-[2-(2-methyl-1H-indol-3-yl)ethyl]thiophene-2-carboxamide.
DR iPTMnet; O15143; -.
DR PhosphoSitePlus; O15143; -.
DR SwissPalm; O15143; -.
DR BioMuta; ARPC1B; -.
DR EPD; O15143; -.
DR jPOST; O15143; -.
DR MassIVE; O15143; -.
DR MaxQB; O15143; -.
DR PaxDb; O15143; -.
DR PeptideAtlas; O15143; -.
DR PRIDE; O15143; -.
DR ProteomicsDB; 48468; -.
DR Antibodypedia; 1378; 221 antibodies from 32 providers.
DR DNASU; 10095; -.
DR Ensembl; ENST00000427217.6; ENSP00000403211.2; ENSG00000130429.15.
DR Ensembl; ENST00000431816.6; ENSP00000398110.2; ENSG00000130429.15.
DR Ensembl; ENST00000451682.5; ENSP00000389631.1; ENSG00000130429.15.
DR Ensembl; ENST00000455009.6; ENSP00000410238.2; ENSG00000130429.15.
DR Ensembl; ENST00000458033.6; ENSP00000388802.2; ENSG00000130429.15.
DR Ensembl; ENST00000645391.1; ENSP00000494033.1; ENSG00000130429.15.
DR Ensembl; ENST00000646101.2; ENSP00000496599.1; ENSG00000130429.15.
DR GeneID; 10095; -.
DR KEGG; hsa:10095; -.
DR MANE-Select; ENST00000646101.2; ENSP00000496599.1; NM_005720.4; NP_005711.1.
DR UCSC; uc003upz.4; human.
DR CTD; 10095; -.
DR DisGeNET; 10095; -.
DR GeneCards; ARPC1B; -.
DR HGNC; HGNC:704; ARPC1B.
DR HPA; ENSG00000130429; Tissue enhanced (lymphoid).
DR MalaCards; ARPC1B; -.
DR MIM; 604223; gene.
DR MIM; 617718; phenotype.
DR neXtProt; NX_O15143; -.
DR OpenTargets; ENSG00000130429; -.
DR PharmGKB; PA24998; -.
DR VEuPathDB; HostDB:ENSG00000130429; -.
DR eggNOG; KOG1523; Eukaryota.
DR GeneTree; ENSGT00950000183183; -.
DR HOGENOM; CLU_034396_1_0_1; -.
DR InParanoid; O15143; -.
DR OMA; TLKGSTW; -.
DR OrthoDB; 848569at2759; -.
DR PhylomeDB; O15143; -.
DR TreeFam; TF315041; -.
DR PathwayCommons; O15143; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; O15143; -.
DR SIGNOR; O15143; -.
DR BioGRID-ORCS; 10095; 20 hits in 1080 CRISPR screens.
DR ChiTaRS; ARPC1B; human.
DR GeneWiki; ARPC1B; -.
DR GenomeRNAi; 10095; -.
DR Pharos; O15143; Tbio.
DR PRO; PR:O15143; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O15143; protein.
DR Bgee; ENSG00000130429; Expressed in monocyte and 97 other tissues.
DR ExpressionAtlas; O15143; baseline and differential.
DR Genevisible; O15143; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0036284; C:tubulobulbar complex; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:FlyBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:FlyBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
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; 6.
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;
KW Direct protein sequencing; Disease variant; Nucleus; Reference proteome;
KW Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..372
FT /note="Actin-related protein 2/3 complex subunit 1B"
FT /id="PRO_0000050855"
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 VARIANT 37
FT /note="K -> N (in dbSNP:rs1045012)"
FT /id="VAR_014477"
FT VARIANT 105
FT /note="A -> V (in IMD71; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28368018"
FT /id="VAR_080353"
FT VARIANT 238
FT /note="A -> T (in IMD71; unknown pathological significance;
FT dbSNP:rs147238850)"
FT /evidence="ECO:0000269|PubMed:28368018"
FT /id="VAR_080354"
SQ SEQUENCE 372 AA; 40950 MW; 1939F5B63D40BD27 CRC64;
MAYHSFLVEP ISCHAWNKDR TQIAICPNNH EVHIYEKSGA KWTKVHELKE HNGQVTGIDW
APESNRIVTC GTDRNAYVWT LKGRTWKPTL VILRINRAAR CVRWAPNENK FAVGSGSRVI
SICYFEQEND WWVCKHIKKP IRSTVLSLDW HPNNVLLAAG SCDFKCRIFS AYIKEVEERP
APTPWGSKMP FGELMFESSS SCGWVHGVCF SASGSRVAWV SHDSTVCLAD ADKKMAVATL
ASETLPLLAL TFITDNSLVA AGHDCFPVLF TYDAAAGMLS FGGRLDVPKQ SSQRGLTARE
RFQNLDKKAS SEGGTAAGAG LDSLHKNSVS QISVLSGGKA KCSQFCTTGM DGGMSIWDVK
SLESALKDLK IK
