ID ARP3B_HUMAN Reviewed; 418 AA. AC Q9P1U1; A8MTG1; B4DFW4; Q7Z526; Q96BT2; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 172. DE RecName: Full=Actin-related protein 3B; DE AltName: Full=ARP3-beta; DE AltName: Full=Actin-like protein 3B; DE AltName: Full=Actin-related protein ARP4; GN Name=ACTR3B; Synonyms=ARP11, ARP4; 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] (ISOFORM 1), ALTERNATIVE SPLICING, AND TISSUE RP SPECIFICITY. RC TISSUE=Embryo; RX PubMed=10806390; DOI=10.1046/j.1432-1327.2000.01306.x; RA Jay P., Berge-Lefranc J.-L., Massacrier A., Roessler E., Wallis D., RA Muenke M., Gastaldi M., Taviaux S., Cau P., Berta P.; RT "ARP3beta, the gene encoding a new human actin-related protein, is RT alternatively spliced and predominantly expressed in brain neuronal RT cells."; RL Eur. J. Biochem. 267:2921-2928(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Ding J.B., Yu L., Zhang M., Dai F.Y., Jiang J.X., Zhao S.Y.; RT "Cloning of a novel human cDNA homology to human actin-related protein RT Arp3(ARP3) mRNA."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, and Peripheral blood; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Colon, 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 [6] RP TISSUE SPECIFICITY. RX PubMed=11162478; DOI=10.1006/bbrc.2000.4059; RA Shindo-Okada N., Shimizu K.; RT "Isolation of a novel actin-related gene expressed in low-metastatic PC-14 RT human lung adenocarcinoma."; RL Biochem. Biophys. Res. Commun. 280:61-67(2001). RN [7] RP FUNCTION. RX PubMed=14651955; DOI=10.1016/j.bbrc.2003.10.200; RA Shindo-Okada N., Iigo M.; RT "Expression of the Arp11 gene suppresses the tumorigenicity of PC-14 human RT lung adenocarcinoma cells."; RL Biochem. Biophys. Res. Commun. 312:889-896(2003). CC -!- FUNCTION: Plays a role in the organization of the actin cytoskeleton. CC May function as ATP-binding component of the Arp2/3 complex which is CC involved in regulation of actin polymerization and together with an CC activating nucleation-promoting factor (NPF) mediates the formation of CC branched actin networks. May decrease the metastatic potential of CC tumors. {ECO:0000269|PubMed:14651955}. CC -!- SUBUNIT: Interacts with the Arp2/3 complex composed of ARP2, ARP3, CC ARPC1B, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and CC ARPC5/p16-ARC. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell CC projection {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9P1U1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P1U1-2; Sequence=VSP_034418; CC Name=3; CC IsoId=Q9P1U1-3; Sequence=VSP_041474; CC -!- TISSUE SPECIFICITY: Detected in fetal brain. Detected throughout the CC adult brain, in neurons from gray matter, but not in white matter. CC Detected in liver, skeletal muscle and pancreas. Detected in lung CC adenocarcinoma cells with low metastatic potential, but not in lung CC adenocarcinoma cells with high metastatic potential. CC {ECO:0000269|PubMed:10806390, ECO:0000269|PubMed:11162478}. CC -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAP97150.1; Type=Frameshift; Evidence={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; AF023453; AAC98904.1; -; mRNA. DR EMBL; AF086920; AAP97150.1; ALT_SEQ; mRNA. DR EMBL; AK294292; BAG57575.1; -; mRNA. DR EMBL; AK315534; BAG37914.1; -; mRNA. DR EMBL; AC072057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092180; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015207; AAH15207.1; -; mRNA. DR EMBL; BC008682; AAH08682.1; -; mRNA. DR CCDS; CCDS34782.1; -. [Q9P1U1-3] DR CCDS; CCDS5934.1; -. [Q9P1U1-1] DR CCDS; CCDS87568.1; -. [Q9P1U1-2] DR RefSeq; NP_001035225.1; NM_001040135.2. [Q9P1U1-3] DR RefSeq; NP_065178.1; NM_020445.5. [Q9P1U1-1] DR AlphaFoldDB; Q9P1U1; -. DR SMR; Q9P1U1; -. DR BioGRID; 121429; 148. DR ComplexPortal; CPX-2490; Actin-related protein 2/3 complex, ARPC1A-ACTR3B-ARPC5 variant. DR ComplexPortal; CPX-2580; Actin-related protein 2/3 complex, ARPC1B-ACTR3B-ARPC5L variant. DR ComplexPortal; CPX-2583; Actin-related protein 2/3 complex, ARPC1B-ACTR3B-ARPC5 variant. DR ComplexPortal; CPX-2668; Actin-related protein 2/3 complex, ARPC1B-ACTR3B-ARPC5L variant. DR IntAct; Q9P1U1; 25. DR MINT; Q9P1U1; -. DR STRING; 9606.ENSP00000256001; -. DR GlyGen; Q9P1U1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9P1U1; -. DR MetOSite; Q9P1U1; -. DR PhosphoSitePlus; Q9P1U1; -. DR BioMuta; ACTR3B; -. DR DMDM; 74753111; -. DR EPD; Q9P1U1; -. DR jPOST; Q9P1U1; -. DR MassIVE; Q9P1U1; -. DR MaxQB; Q9P1U1; -. DR PaxDb; 9606-ENSP00000256001; -. DR PeptideAtlas; Q9P1U1; -. DR ProteomicsDB; 83666; -. [Q9P1U1-1] DR ProteomicsDB; 83667; -. [Q9P1U1-2] DR ProteomicsDB; 83668; -. [Q9P1U1-3] DR Pumba; Q9P1U1; -. DR Antibodypedia; 33062; 206 antibodies from 26 providers. DR DNASU; 57180; -. DR Ensembl; ENST00000256001.13; ENSP00000256001.8; ENSG00000133627.18. [Q9P1U1-1] DR Ensembl; ENST00000377776.7; ENSP00000367007.3; ENSG00000133627.18. [Q9P1U1-3] DR Ensembl; ENST00000397282.2; ENSP00000380452.2; ENSG00000133627.18. [Q9P1U1-2] DR GeneID; 57180; -. DR KEGG; hsa:57180; -. DR MANE-Select; ENST00000256001.13; ENSP00000256001.8; NM_020445.6; NP_065178.1. DR UCSC; uc003wle.3; human. [Q9P1U1-1] DR AGR; HGNC:17256; -. DR CTD; 57180; -. DR DisGeNET; 57180; -. DR GeneCards; ACTR3B; -. DR HGNC; HGNC:17256; ACTR3B. DR HPA; ENSG00000133627; Tissue enhanced (brain). DR neXtProt; NX_Q9P1U1; -. DR OpenTargets; ENSG00000133627; -. DR PharmGKB; PA142672645; -. DR VEuPathDB; HostDB:ENSG00000133627; -. DR eggNOG; KOG0678; Eukaryota. DR GeneTree; ENSGT00940000158304; -. DR HOGENOM; CLU_027965_3_2_1; -. DR InParanoid; Q9P1U1; -. DR OMA; PIQRCAV; -. DR OrthoDB; 586415at2759; -. DR PhylomeDB; Q9P1U1; -. DR TreeFam; TF300644; -. DR PathwayCommons; Q9P1U1; -. DR SignaLink; Q9P1U1; -. DR BioGRID-ORCS; 57180; 15 hits in 1162 CRISPR screens. DR ChiTaRS; ACTR3B; human. DR GeneWiki; ACTR3B; -. DR GenomeRNAi; 57180; -. DR Pharos; Q9P1U1; Tbio. DR PRO; PR:Q9P1U1; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9P1U1; Protein. DR Bgee; ENSG00000133627; Expressed in cortical plate and 158 other cell types or tissues. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR043129; ATPase_NBD. DR PANTHER; PTHR11937; ACTIN; 1. DR PANTHER; PTHR11937:SF514; ACTIN-RELATED PROTEIN 3B-RELATED; 1. DR Pfam; PF00022; Actin; 1. DR SMART; SM00268; ACTIN; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. DR Genevisible; Q9P1U1; HS. PE 2: Evidence at transcript level; KW Actin-binding; Alternative splicing; ATP-binding; Cell projection; KW Cytoplasm; Cytoskeleton; Nucleotide-binding; Reference proteome. FT CHAIN 1..418 FT /note="Actin-related protein 3B" FT /id="PRO_0000342358" FT VAR_SEQ 1..88 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2" FT /id="VSP_034418" FT VAR_SEQ 318..387 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_041474" FT VARIANT 250 FT /note="R -> Q (in dbSNP:rs2260545)" FT /id="VAR_048188" SQ SEQUENCE 418 AA; 47608 MW; BC1040ED5D3B832F CRC64; MAGSLPPCVV DCGTGYTKLG YAGNTEPQFI IPSCIAIRES AKVVDQAQRR VLRGVDDLDF FIGDEAIDKP TYATKWPIRH GIIEDWDLME RFMEQVVFKY LRAEPEDHYF LMTEPPLNTP ENREYLAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGIVIDS GDGVTHVIPV AEGYVIGSCI KHIPIAGRDI TYFIQQLLRE REVGIPPEQS LETAKAIKEK YCYICPDIVK EFAKYDVDPR KWIKQYTGIN AINQKKFVID VGYERFLGPE IFFHPEFANP DFMESISDVV DEVIQNCPID VRRPLYKNVV LSGGSTMFRD FGRRLQRDLK RVVDARLRLS EELSGGRIKP KPVEVQVVTH HMQRYAVWFG GSMLASTPEF FQVCHTKKDY EEYGPSICRH NPVFGVMS //