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   02-DEC-2020, entry version 192.
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 PLTEID, AND VARIANTS PLTEID 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; O15145: ARPC3; NbExp=11; IntAct=EBI-1044647, EBI-351829;
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: Platelet abnormalities with eosinophilia and immune-mediated
CC       inflammatory disease (PLTEID) [MIM:617718]: An autosomal recessive
CC       disorder characterized by platelet abnormalities, vasculitis,
CC       eosinophilia, and predisposition to inflammatory diseases.
CC       {ECO:0000269|PubMed:28368018}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
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; 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   SMR; O15143; -.
DR   BioGRID; 115402; 86.
DR   CORUM; O15143; -.
DR   DIP; DIP-41254N; -.
DR   IntAct; O15143; 56.
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; 202 antibodies.
DR   DNASU; 10095; -.
DR   Ensembl; ENST00000427217; ENSP00000403211; ENSG00000130429.
DR   Ensembl; ENST00000431816; ENSP00000398110; ENSG00000130429.
DR   Ensembl; ENST00000451682; ENSP00000389631; ENSG00000130429.
DR   Ensembl; ENST00000455009; ENSP00000410238; ENSG00000130429.
DR   Ensembl; ENST00000458033; ENSP00000388802; ENSG00000130429.
DR   Ensembl; ENST00000645391; ENSP00000494033; ENSG00000130429.
DR   Ensembl; ENST00000646101; ENSP00000496599; ENSG00000130429.
DR   GeneID; 10095; -.
DR   KEGG; hsa:10095; -.
DR   UCSC; uc003upz.4; human.
DR   CTD; 10095; -.
DR   DisGeNET; 10095; -.
DR   EuPathDB; HostDB:ENSG00000130429.12; -.
DR   GeneCards; ARPC1B; -.
DR   HGNC; HGNC:704; ARPC1B.
DR   HPA; ENSG00000130429; Tissue enhanced (blood).
DR   MalaCards; ARPC1B; -.
DR   MIM; 604223; gene.
DR   MIM; 617718; phenotype.
DR   neXtProt; NX_O15143; -.
DR   OpenTargets; ENSG00000130429; -.
DR   PharmGKB; PA24998; -.
DR   eggNOG; KOG1523; Eukaryota.
DR   GeneTree; ENSGT00950000183183; -.
DR   HOGENOM; CLU_034396_1_0_1; -.
DR   InParanoid; O15143; -.
DR   OMA; KWVQVHE; -.
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; 9 hits in 839 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 239 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:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
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; IPR017986; WD40_repeat_dom.
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 mutation; Nucleus; Polymorphism;
KW   Reference proteome; 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 PLTEID; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:28368018"
FT                   /id="VAR_080353"
FT   VARIANT         238
FT                   /note="A -> T (in PLTEID; unknown pathological
FT                   significance; 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
//