ARP3B_HUMAN
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 03-AUG-2022, entry version 163.
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};
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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; 143.
DR IntAct; Q9P1U1; 23.
DR MINT; Q9P1U1; -.
DR STRING; 9606.ENSP00000256001; -.
DR iPTMnet; Q9P1U1; -.
DR PhosphoSitePlus; Q9P1U1; -.
DR BioMuta; ACTR3B; -.
DR DMDM; 74753111; -.
DR EPD; Q9P1U1; -.
DR jPOST; Q9P1U1; -.
DR MassIVE; Q9P1U1; -.
DR MaxQB; Q9P1U1; -.
DR PaxDb; Q9P1U1; -.
DR PeptideAtlas; Q9P1U1; -.
DR PRIDE; Q9P1U1; -.
DR ProteomicsDB; 83666; -. [Q9P1U1-1]
DR ProteomicsDB; 83667; -. [Q9P1U1-2]
DR ProteomicsDB; 83668; -. [Q9P1U1-3]
DR Antibodypedia; 33062; 194 antibodies from 25 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 CTD; 57180; -.
DR DisGeNET; 57180; -.
DR GeneCards; ACTR3B; -.
DR HGNC; HGNC:17256; ACTR3B.
DR HPA; ENSG00000133627; Low tissue specificity.
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; YLPPCVV; -.
DR PhylomeDB; Q9P1U1; -.
DR TreeFam; TF300644; -.
DR PathwayCommons; Q9P1U1; -.
DR SignaLink; Q9P1U1; -.
DR BioGRID-ORCS; 57180; 15 hits in 1084 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 156 other tissues.
DR Genevisible; Q9P1U1; HS.
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 InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
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
