Full text data of ACTR3
ACTR3
(ARP3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Actin-related protein 3 (Actin-like protein 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Actin-related protein 3 (Actin-like protein 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61158
ID ARP3_HUMAN Reviewed; 418 AA.
AC P61158; P32391; Q53QM2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Actin-related protein 3;
DE AltName: Full=Actin-like protein 3;
GN Name=ACTR3; Synonyms=ARP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE ARP2/2 COMPLEX, AND
RP SUBCELLULAR LOCATION.
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
RT subunits and is localized to cellular regions of dynamic actin
RT filament assembly.";
RL J. Cell Biol. 138:375-384(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Szelei J., Soto A.M., Geck P., Desronvil M., Prechtl N., Weill B.,
RA Sonnenschein C.;
RT "Identification of human estrogen-inducible transcripts from a serum
RT resistant variant of breast cancer MCF7 cells.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN
RP THE ARP2/3 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=9000076; DOI=10.1038/385265a0;
RA Welch M.D., Iwamatsu A., Mitchison T.J.;
RT "Actin polymerization is induced by Arp2/3 protein complex at the
RT surface of Listeria monocytogenes.";
RL Nature 385:265-269(1997).
RN [8]
RP PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 103-123 AND 199-209, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
RP RECONSTITUTION OF 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP INTERACTION WITH WHDC1.
RX PubMed=18614018; DOI=10.1016/j.cell.2008.05.032;
RA Campellone K.G., Webb N.J., Znameroski E.A., Welch M.D.;
RT "WHAMM is an Arp2/3 complex activator that binds microtubules and
RT functions in ER to Golgi transport.";
RL Cell 134:148-161(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-240; LYS-244; LYS-251 AND
RP LYS-254, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP FUNCTION.
RX PubMed=20393563; DOI=10.1038/nature08895;
RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K.,
RA Ideker T., Aza-Blanc P., Gleeson J.G.;
RT "Functional genomic screen for modulators of ciliogenesis and cilium
RT length.";
RL Nature 464:1048-1051(2010).
RN [16]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Functions as ATP-binding component of the Arp2/3 complex
CC which is involved in regulation of actin polymerization and
CC together with an activating nucleation-promoting factor (NPF)
CC mediates the formation of branched actin networks. Seems to
CC contact the pointed end of the daughter actin filament. Plays a
CC role in ciliogenesis.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of ARP2, ARP3,
CC ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and
CC ARPC5/p16-ARC. Interacts with WHDC1.
CC -!- INTERACTION:
CC P17535:JUND; NbExp=2; IntAct=EBI-351428, EBI-2682803;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection.
CC -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily.
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DR EMBL; AF006083; AAB64188.1; -; mRNA.
DR EMBL; AF127773; AAD51904.1; -; mRNA.
DR EMBL; AK312659; BAG35542.1; -; mRNA.
DR EMBL; AC110769; AAX93226.1; -; Genomic_DNA.
DR EMBL; CH471103; EAW95179.1; -; Genomic_DNA.
DR EMBL; BC044590; AAH44590.1; -; mRNA.
DR RefSeq; NP_005712.1; NM_005721.4.
DR UniGene; Hs.433512; -.
DR UniGene; Hs.595349; -.
DR ProteinModelPortal; P61158; -.
DR SMR; P61158; 3-417.
DR DIP; DIP-33140N; -.
DR IntAct; P61158; 14.
DR MINT; MINT-3022340; -.
DR STRING; 9606.ENSP00000263238; -.
DR PhosphoSite; P61158; -.
DR DMDM; 47117647; -.
DR OGP; P32391; -.
DR PeptideAtlas; P61158; -.
DR PRIDE; P61158; -.
DR DNASU; 10096; -.
DR Ensembl; ENST00000263238; ENSP00000263238; ENSG00000115091.
DR GeneID; 10096; -.
DR KEGG; hsa:10096; -.
DR UCSC; uc002tkx.2; human.
DR CTD; 10096; -.
DR GeneCards; GC02P114647; -.
DR HGNC; HGNC:170; ACTR3.
DR HPA; CAB005085; -.
DR MIM; 604222; gene.
DR neXtProt; NX_P61158; -.
DR PharmGKB; PA24489; -.
DR HOGENOM; HOG000233339; -.
DR HOVERGEN; HBG003771; -.
DR InParanoid; P61158; -.
DR OMA; YPIRHGI; -.
DR OrthoDB; EOG7TMZRM; -.
DR PhylomeDB; P61158; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P61158; -.
DR ChiTaRS; ACTR3; human.
DR GeneWiki; ACTR3; -.
DR GenomeRNAi; 10096; -.
DR NextBio; 38185; -.
DR PMAP-CutDB; P61158; -.
DR PRO; PR:P61158; -.
DR ArrayExpress; P61158; -.
DR Bgee; P61158; -.
DR CleanEx; HS_ACTR3; -.
DR Genevestigator; P61158; -.
DR GO; GO:0005885; C:Arp2/3 protein complex; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0030056; C:hemidesmosome; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0002102; C:podosome; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008356; P:asymmetric cell division; IEA:Ensembl.
DR GO; GO:0006928; P:cellular component movement; TAS:UniProtKB.
DR GO; GO:0060271; P:cilium morphogenesis; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0033206; P:meiotic cytokinesis; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0043519; P:regulation of myosin II filament organization; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0009743; P:response to carbohydrate stimulus; IEA:Ensembl.
DR GO; GO:0051653; P:spindle localization; IEA:Ensembl.
DR InterPro; IPR004000; Actin-related.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; ATP-binding; Cell projection;
KW Cilium biogenesis/degradation; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 418 Actin-related protein 3.
FT /FTId=PRO_0000089079.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 240 240 N6-acetyllysine.
FT MOD_RES 244 244 N6-acetyllysine.
FT MOD_RES 251 251 N6-acetyllysine.
FT MOD_RES 254 254 N6-acetyllysine.
SQ SEQUENCE 418 AA; 47371 MW; 23E5564198B81C63 CRC64;
MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF
FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY LRAEPEDHYF LLTEPPLNTP
ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV
AEGYVIGSCI KHIPIAGRDI TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK
EFNKYDTDGS KWIKQYTGIN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV
DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS EELSGGRLKP
KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS
//
ID ARP3_HUMAN Reviewed; 418 AA.
AC P61158; P32391; Q53QM2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Actin-related protein 3;
DE AltName: Full=Actin-like protein 3;
GN Name=ACTR3; Synonyms=ARP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE ARP2/2 COMPLEX, AND
RP SUBCELLULAR LOCATION.
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
RT subunits and is localized to cellular regions of dynamic actin
RT filament assembly.";
RL J. Cell Biol. 138:375-384(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Szelei J., Soto A.M., Geck P., Desronvil M., Prechtl N., Weill B.,
RA Sonnenschein C.;
RT "Identification of human estrogen-inducible transcripts from a serum
RT resistant variant of breast cancer MCF7 cells.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN
RP THE ARP2/3 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=9000076; DOI=10.1038/385265a0;
RA Welch M.D., Iwamatsu A., Mitchison T.J.;
RT "Actin polymerization is induced by Arp2/3 protein complex at the
RT surface of Listeria monocytogenes.";
RL Nature 385:265-269(1997).
RN [8]
RP PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 103-123 AND 199-209, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
RP RECONSTITUTION OF 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP INTERACTION WITH WHDC1.
RX PubMed=18614018; DOI=10.1016/j.cell.2008.05.032;
RA Campellone K.G., Webb N.J., Znameroski E.A., Welch M.D.;
RT "WHAMM is an Arp2/3 complex activator that binds microtubules and
RT functions in ER to Golgi transport.";
RL Cell 134:148-161(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-240; LYS-244; LYS-251 AND
RP LYS-254, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP FUNCTION.
RX PubMed=20393563; DOI=10.1038/nature08895;
RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K.,
RA Ideker T., Aza-Blanc P., Gleeson J.G.;
RT "Functional genomic screen for modulators of ciliogenesis and cilium
RT length.";
RL Nature 464:1048-1051(2010).
RN [16]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Functions as ATP-binding component of the Arp2/3 complex
CC which is involved in regulation of actin polymerization and
CC together with an activating nucleation-promoting factor (NPF)
CC mediates the formation of branched actin networks. Seems to
CC contact the pointed end of the daughter actin filament. Plays a
CC role in ciliogenesis.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of ARP2, ARP3,
CC ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and
CC ARPC5/p16-ARC. Interacts with WHDC1.
CC -!- INTERACTION:
CC P17535:JUND; NbExp=2; IntAct=EBI-351428, EBI-2682803;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection.
CC -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily.
CC -----------------------------------------------------------------------
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DR EMBL; AF006083; AAB64188.1; -; mRNA.
DR EMBL; AF127773; AAD51904.1; -; mRNA.
DR EMBL; AK312659; BAG35542.1; -; mRNA.
DR EMBL; AC110769; AAX93226.1; -; Genomic_DNA.
DR EMBL; CH471103; EAW95179.1; -; Genomic_DNA.
DR EMBL; BC044590; AAH44590.1; -; mRNA.
DR RefSeq; NP_005712.1; NM_005721.4.
DR UniGene; Hs.433512; -.
DR UniGene; Hs.595349; -.
DR ProteinModelPortal; P61158; -.
DR SMR; P61158; 3-417.
DR DIP; DIP-33140N; -.
DR IntAct; P61158; 14.
DR MINT; MINT-3022340; -.
DR STRING; 9606.ENSP00000263238; -.
DR PhosphoSite; P61158; -.
DR DMDM; 47117647; -.
DR OGP; P32391; -.
DR PeptideAtlas; P61158; -.
DR PRIDE; P61158; -.
DR DNASU; 10096; -.
DR Ensembl; ENST00000263238; ENSP00000263238; ENSG00000115091.
DR GeneID; 10096; -.
DR KEGG; hsa:10096; -.
DR UCSC; uc002tkx.2; human.
DR CTD; 10096; -.
DR GeneCards; GC02P114647; -.
DR HGNC; HGNC:170; ACTR3.
DR HPA; CAB005085; -.
DR MIM; 604222; gene.
DR neXtProt; NX_P61158; -.
DR PharmGKB; PA24489; -.
DR HOGENOM; HOG000233339; -.
DR HOVERGEN; HBG003771; -.
DR InParanoid; P61158; -.
DR OMA; YPIRHGI; -.
DR OrthoDB; EOG7TMZRM; -.
DR PhylomeDB; P61158; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P61158; -.
DR ChiTaRS; ACTR3; human.
DR GeneWiki; ACTR3; -.
DR GenomeRNAi; 10096; -.
DR NextBio; 38185; -.
DR PMAP-CutDB; P61158; -.
DR PRO; PR:P61158; -.
DR ArrayExpress; P61158; -.
DR Bgee; P61158; -.
DR CleanEx; HS_ACTR3; -.
DR Genevestigator; P61158; -.
DR GO; GO:0005885; C:Arp2/3 protein complex; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0030056; C:hemidesmosome; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0002102; C:podosome; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008356; P:asymmetric cell division; IEA:Ensembl.
DR GO; GO:0006928; P:cellular component movement; TAS:UniProtKB.
DR GO; GO:0060271; P:cilium morphogenesis; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0033206; P:meiotic cytokinesis; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0043519; P:regulation of myosin II filament organization; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0009743; P:response to carbohydrate stimulus; IEA:Ensembl.
DR GO; GO:0051653; P:spindle localization; IEA:Ensembl.
DR InterPro; IPR004000; Actin-related.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; ATP-binding; Cell projection;
KW Cilium biogenesis/degradation; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 418 Actin-related protein 3.
FT /FTId=PRO_0000089079.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 240 240 N6-acetyllysine.
FT MOD_RES 244 244 N6-acetyllysine.
FT MOD_RES 251 251 N6-acetyllysine.
FT MOD_RES 254 254 N6-acetyllysine.
SQ SEQUENCE 418 AA; 47371 MW; 23E5564198B81C63 CRC64;
MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF
FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY LRAEPEDHYF LLTEPPLNTP
ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV
AEGYVIGSCI KHIPIAGRDI TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK
EFNKYDTDGS KWIKQYTGIN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV
DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS EELSGGRLKP
KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS
//
MIM
604222
*RECORD*
*FIELD* NO
604222
*FIELD* TI
*604222 ACTIN-RELATED PROTEIN 3; ACTR3
;;ARP3
*FIELD* TX
The Arp2/3 protein complex has been implicated in the control of actin
read morepolymerization in cells. The human complex consists of 7 subunits: the
actin-related proteins ARP2 (ACTR2; 604221) and ARP3 (ACTR3), ARC41
(ARPC1B; 604223), ARC34 (ARPC2; 604224), ARC21 (ARPC3; 604225), ARC20
(ARPC4; 604226), and ARC16 (ARPC5; 604227). See ACTR2 for additional
information about the Arp2/3 complex.
CLONING
By searching an EST database with peptide sequences from the 7 subunits
of the human ARP2/3 complex, Welch et al. (1997) identified full-length
human cDNAs encoding each subunit. The ARP3 cDNA encodes a deduced
418-amino acid protein that is identical to bovine Arp3, 59% identical
to S. pombe Arp3, and 58% identical to S. cerevisiae Arp3. ARP3
localizes to the lamellipodia of stationary and locomoting fibroblasts.
It also localizes to the actin tails assembled by moving intracellular
Listeria monocytogenes bacteria and to actin clouds surrounding
stationary L. monocytogenes (Welch et al., 1997). ARP3 was not detected
in cellular bundles of actin filaments.
Machesky et al. (1997) purified the ARP2/3 complex from human
neutrophils and sequenced peptides from each of the subunits. Western
blot analysis detected ARP3 and ARC34 in all human tissues tested.
GENE FUNCTION
In a functional genomic screen using RNA interference to identify human
genes involved in ciliogenesis control, Kim et al. (2010) identified 2
gelsolin family proteins, GSN (137350) and AVIL (613397), which regulate
cytoskeletal actin organization by severing actin filaments. Depletion
of GSN proteins by 2 independent siRNAs significantly reduced ciliated
cell numbers, indicating that actin filament severing is involved in
ciliogenesis. In contrast, silencing of actin-related protein ACTR3,
which is a major constituent of the ARP2/3 complex that is necessary for
nucleating actin polymerization at filament branches, caused a
significant increase in cilium length and also facilitated ciliogenesis
independently of serum starvation. Kim et al. (2010) concluded that
their observations indicated an inhibitory role of branched actin
network formation in ciliogenesis.
BIOCHEMICAL FEATURES
Volkmann et al. (2001) performed electron cryomicroscopy and
3-dimensional reconstruction of Acanthamoeba castellanii and S.
cerevisiae Arp2/3 complexes bound to the WASP (301000) carboxy-terminal
domain. Asymmetric, oblate ellipsoids were revealed. Image analysis of
actin branches indicated that the complex binds the side of the mother
filament, and ARP2 and ARP3 are the first 2 subunits of the daughter
filament. Comparison to the actin-free WASP-activated complexes suggests
that branch initiation involves large-scale structural rearrangements
within ARP2/3.
Robinson et al. (2001) determined the crystal structure of bovine ARP2/3
complex at 2.0-angstrom resolution. ARP2 and ARP3 are folded like actin,
with distinctive surface features. Subunits ARPC2 and ARPC4 in the core
of the complex associate through long carboxy-terminal alpha helices and
have similarly folded amino-terminal alpha/beta domains. ARPC1 is a
7-blade beta propeller with an insertion that may associate with the
side of an actin filament. ARPC3 and ARPC5 are globular alpha-helical
subunits. Robinson et al. (2001) predicted that WASP/SCAR proteins
activate ARP2/3 complex by bringing ARP2 into proximity with ARP3 for
nucleation of a branch on the side of a preexisting actin filament.
*FIELD* RF
1. Kim, J.; Lee, J. E.; Heynen-Genel, S.; Suyama, E.; Ono, K.; Lee,
K.; Ideker, T.; Aza-Blanc, P.; Gleeson, J. G.: Functional genomic
screen for modulators of ciliogenesis and cilium length. Nature 464:
1048-1051, 2010.
2. Machesky, L. M.; Reeves, E.; Wientjes, F.; Mattheyse, F. J.; Grogan,
A.; Totty, N. F.; Burlingame, A. L.; Hsuan, J. J.; Segal, A. W.:
Mammalian actin-related protein 2/3 complex localizes to regions of
lamellipodial protrusion and is composed of evolutionarily conserved
proteins. Biochem. J. 328: 105-112, 1997.
3. Robinson, R. C.; Turbedsky, K.; Kaiser, D. A.; Marchand, J.-B.;
Higgs, H. N.; Choe, S.; Pollard, T. D.: Crystal structure of Arp2/3
complex. Science 294: 1679-1684, 2001.
4. Volkmann, N.; Amann, K. J.; Stoilova-McPhie, S.; Egile, C.; Winter,
D. C.; Hazelwood, L.; Heuser, J. E.; Li, R.; Pollard, T. D.; Hanein,
D.: Structure of Arp2/3 complex in its activated state and in actin
filament branch junctions. Science 293: 2456-2459, 2001.
5. Welch, M. D.; DePace, A. H.; Verma, S.; Iwamatsu, A.; Mitchison,
T. J.: The human Arp2/3 complex is composed of evolutionarily conserved
subunits and is localized to cellular regions of dynamic actin filament
assembly. J. Cell Biol. 138: 375-384, 1997.
6. Welch, M. D.; Iwamatsu, A.; Mitchison, T. J.: Actin polymerization
is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385:
265-269, 1997.
*FIELD* CN
Ada Hamosh - updated: 05/10/2010
Ada Hamosh - updated: 1/10/2002
Ada Hamosh - updated: 10/11/2001
Patti M. Sherman - updated: 10/29/1999
*FIELD* CD
Patti M. Sherman: 10/8/1999
*FIELD* ED
alopez: 05/10/2010
alopez: 4/3/2009
terry: 4/2/2009
alopez: 1/10/2002
alopez: 10/11/2001
mgross: 11/1/1999
psherman: 10/29/1999
mgross: 10/15/1999
psherman: 10/12/1999
*RECORD*
*FIELD* NO
604222
*FIELD* TI
*604222 ACTIN-RELATED PROTEIN 3; ACTR3
;;ARP3
*FIELD* TX
The Arp2/3 protein complex has been implicated in the control of actin
read morepolymerization in cells. The human complex consists of 7 subunits: the
actin-related proteins ARP2 (ACTR2; 604221) and ARP3 (ACTR3), ARC41
(ARPC1B; 604223), ARC34 (ARPC2; 604224), ARC21 (ARPC3; 604225), ARC20
(ARPC4; 604226), and ARC16 (ARPC5; 604227). See ACTR2 for additional
information about the Arp2/3 complex.
CLONING
By searching an EST database with peptide sequences from the 7 subunits
of the human ARP2/3 complex, Welch et al. (1997) identified full-length
human cDNAs encoding each subunit. The ARP3 cDNA encodes a deduced
418-amino acid protein that is identical to bovine Arp3, 59% identical
to S. pombe Arp3, and 58% identical to S. cerevisiae Arp3. ARP3
localizes to the lamellipodia of stationary and locomoting fibroblasts.
It also localizes to the actin tails assembled by moving intracellular
Listeria monocytogenes bacteria and to actin clouds surrounding
stationary L. monocytogenes (Welch et al., 1997). ARP3 was not detected
in cellular bundles of actin filaments.
Machesky et al. (1997) purified the ARP2/3 complex from human
neutrophils and sequenced peptides from each of the subunits. Western
blot analysis detected ARP3 and ARC34 in all human tissues tested.
GENE FUNCTION
In a functional genomic screen using RNA interference to identify human
genes involved in ciliogenesis control, Kim et al. (2010) identified 2
gelsolin family proteins, GSN (137350) and AVIL (613397), which regulate
cytoskeletal actin organization by severing actin filaments. Depletion
of GSN proteins by 2 independent siRNAs significantly reduced ciliated
cell numbers, indicating that actin filament severing is involved in
ciliogenesis. In contrast, silencing of actin-related protein ACTR3,
which is a major constituent of the ARP2/3 complex that is necessary for
nucleating actin polymerization at filament branches, caused a
significant increase in cilium length and also facilitated ciliogenesis
independently of serum starvation. Kim et al. (2010) concluded that
their observations indicated an inhibitory role of branched actin
network formation in ciliogenesis.
BIOCHEMICAL FEATURES
Volkmann et al. (2001) performed electron cryomicroscopy and
3-dimensional reconstruction of Acanthamoeba castellanii and S.
cerevisiae Arp2/3 complexes bound to the WASP (301000) carboxy-terminal
domain. Asymmetric, oblate ellipsoids were revealed. Image analysis of
actin branches indicated that the complex binds the side of the mother
filament, and ARP2 and ARP3 are the first 2 subunits of the daughter
filament. Comparison to the actin-free WASP-activated complexes suggests
that branch initiation involves large-scale structural rearrangements
within ARP2/3.
Robinson et al. (2001) determined the crystal structure of bovine ARP2/3
complex at 2.0-angstrom resolution. ARP2 and ARP3 are folded like actin,
with distinctive surface features. Subunits ARPC2 and ARPC4 in the core
of the complex associate through long carboxy-terminal alpha helices and
have similarly folded amino-terminal alpha/beta domains. ARPC1 is a
7-blade beta propeller with an insertion that may associate with the
side of an actin filament. ARPC3 and ARPC5 are globular alpha-helical
subunits. Robinson et al. (2001) predicted that WASP/SCAR proteins
activate ARP2/3 complex by bringing ARP2 into proximity with ARP3 for
nucleation of a branch on the side of a preexisting actin filament.
*FIELD* RF
1. Kim, J.; Lee, J. E.; Heynen-Genel, S.; Suyama, E.; Ono, K.; Lee,
K.; Ideker, T.; Aza-Blanc, P.; Gleeson, J. G.: Functional genomic
screen for modulators of ciliogenesis and cilium length. Nature 464:
1048-1051, 2010.
2. Machesky, L. M.; Reeves, E.; Wientjes, F.; Mattheyse, F. J.; Grogan,
A.; Totty, N. F.; Burlingame, A. L.; Hsuan, J. J.; Segal, A. W.:
Mammalian actin-related protein 2/3 complex localizes to regions of
lamellipodial protrusion and is composed of evolutionarily conserved
proteins. Biochem. J. 328: 105-112, 1997.
3. Robinson, R. C.; Turbedsky, K.; Kaiser, D. A.; Marchand, J.-B.;
Higgs, H. N.; Choe, S.; Pollard, T. D.: Crystal structure of Arp2/3
complex. Science 294: 1679-1684, 2001.
4. Volkmann, N.; Amann, K. J.; Stoilova-McPhie, S.; Egile, C.; Winter,
D. C.; Hazelwood, L.; Heuser, J. E.; Li, R.; Pollard, T. D.; Hanein,
D.: Structure of Arp2/3 complex in its activated state and in actin
filament branch junctions. Science 293: 2456-2459, 2001.
5. Welch, M. D.; DePace, A. H.; Verma, S.; Iwamatsu, A.; Mitchison,
T. J.: The human Arp2/3 complex is composed of evolutionarily conserved
subunits and is localized to cellular regions of dynamic actin filament
assembly. J. Cell Biol. 138: 375-384, 1997.
6. Welch, M. D.; Iwamatsu, A.; Mitchison, T. J.: Actin polymerization
is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385:
265-269, 1997.
*FIELD* CN
Ada Hamosh - updated: 05/10/2010
Ada Hamosh - updated: 1/10/2002
Ada Hamosh - updated: 10/11/2001
Patti M. Sherman - updated: 10/29/1999
*FIELD* CD
Patti M. Sherman: 10/8/1999
*FIELD* ED
alopez: 05/10/2010
alopez: 4/3/2009
terry: 4/2/2009
alopez: 1/10/2002
alopez: 10/11/2001
mgross: 11/1/1999
psherman: 10/29/1999
mgross: 10/15/1999
psherman: 10/12/1999