Full text data of ARPC2
ARPC2
(ARC34)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Actin-related protein 2/3 complex subunit 2 (Arp2/3 complex 34 kDa subunit; p34-ARC)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Actin-related protein 2/3 complex subunit 2 (Arp2/3 complex 34 kDa subunit; p34-ARC)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O15144
ID ARPC2_HUMAN Reviewed; 300 AA.
AC O15144; Q92801; Q9P1D4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Actin-related protein 2/3 complex subunit 2;
DE AltName: Full=Arp2/3 complex 34 kDa subunit;
DE Short=p34-ARC;
GN Name=ARPC2; Synonyms=ARC34; ORFNames=PRO2446;
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].
RX PubMed=8812419; DOI=10.1006/geno.1996.0428;
RA Couch F.J., Rommens J.M., Neuhausen S.L., Belanger C., Dumont M.,
RA Kenneth A., Bell R., Berry S., Bogden R., Cannon-Albright L.,
RA Farid L., Frye C., Hattier T., Janecki T., Jiang P., Kehrer R.,
RA Leblanc J.F., McArthur-Morrison J., McSweeney D., Miki Y., Peng Y.,
RA Samson C., Schroeder M., Snyder S.C., Stringfellow M., Stroup C.,
RA Swedlund B., Swensen J., Teng D., Thakur S., Tran T., Tranchant M.,
RA Welver-Feldhaus J., Wong A.K.C., Shizuya H., Labrie F., Skolnick M.H.,
RA Goldgar D.E., Kamb A., Weber B.L., Tavtigian S.V., Simard J.;
RT "Generation of an integrated transcription map of the BRCA2 region on
RT chromosome 13q12-q13.";
RL Genomics 36:86-99(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-9.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-290.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 191-203, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP ACTIN-BINDING, AND 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275 AND LYS-295, AND MASS
RP 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 [10]
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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Functions as actin-binding component of the Arp2/3
CC complex which is involved in regulation of actin polymerization
CC and together with an activating nucleation-promoting factor (NPF)
CC mediates the formation of branched actin networks. Seems to
CC contact the mother actin filament.
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.
CC -!- INTERACTION:
CC Q9BR76:CORO1B; NbExp=2; IntAct=EBI-352356, EBI-351152;
CC P18206:VCL; NbExp=2; IntAct=EBI-352356, EBI-716775;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection.
CC -!- SIMILARITY: Belongs to the ARPC2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50874.1; Type=Frameshift; Positions=14;
CC Sequence=AAF71122.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF006085; AAB64190.1; -; mRNA.
DR EMBL; U50523; AAC50874.1; ALT_FRAME; mRNA.
DR EMBL; BT006898; AAP35544.1; -; mRNA.
DR EMBL; BC000590; AAH00590.1; -; mRNA.
DR EMBL; AF116702; AAF71122.1; ALT_INIT; mRNA.
DR RefSeq; NP_005722.1; NM_005731.3.
DR RefSeq; NP_690601.1; NM_152862.2.
DR UniGene; Hs.529303; -.
DR ProteinModelPortal; O15144; -.
DR SMR; O15144; 1-283.
DR DIP; DIP-33197N; -.
DR IntAct; O15144; 9.
DR MINT; MINT-5000439; -.
DR STRING; 9606.ENSP00000295685; -.
DR PhosphoSite; O15144; -.
DR OGP; O15144; -.
DR PaxDb; O15144; -.
DR PeptideAtlas; O15144; -.
DR PRIDE; O15144; -.
DR DNASU; 10109; -.
DR Ensembl; ENST00000295685; ENSP00000295685; ENSG00000163466.
DR Ensembl; ENST00000315717; ENSP00000327137; ENSG00000163466.
DR GeneID; 10109; -.
DR KEGG; hsa:10109; -.
DR UCSC; uc002vhd.4; human.
DR CTD; 10109; -.
DR GeneCards; GC02P219081; -.
DR HGNC; HGNC:705; ARPC2.
DR HPA; CAB001994; -.
DR HPA; HPA008352; -.
DR MIM; 604224; gene.
DR neXtProt; NX_O15144; -.
DR PharmGKB; PA24999; -.
DR eggNOG; NOG327379; -.
DR HOGENOM; HOG000212535; -.
DR HOVERGEN; HBG050580; -.
DR InParanoid; O15144; -.
DR KO; K05758; -.
DR OMA; YFKFQEE; -.
DR OrthoDB; EOG73JKVS; -.
DR PhylomeDB; O15144; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; ARPC2; human.
DR GeneWiki; ARPC2; -.
DR GenomeRNAi; 10109; -.
DR NextBio; 38237; -.
DR PRO; PR:O15144; -.
DR ArrayExpress; O15144; -.
DR Bgee; O15144; -.
DR CleanEx; HS_ARPC2; -.
DR Genevestigator; O15144; -.
DR GO; GO:0005885; C:Arp2/3 protein complex; TAS:ProtInc.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0006928; P:cellular component movement; TAS:ProtInc.
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:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR InterPro; IPR007188; P34-arc.
DR PANTHER; PTHR12058; PTHR12058; 1.
DR Pfam; PF04045; P34-Arc; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cell projection; Complete proteome;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT CHAIN 1 300 Actin-related protein 2/3 complex subunit
FT 2.
FT /FTId=PRO_0000124033.
FT MOD_RES 275 275 N6-acetyllysine.
FT MOD_RES 295 295 N6-acetyllysine.
FT CONFLICT 72 72 A -> C (in Ref. 2; AAC50874).
FT CONFLICT 289 300 MKTITGKTFSSR -> KI (in Ref. 6; AAF71122).
SQ SEQUENCE 300 AA; 34333 MW; 3BA57121BE9A05F2 CRC64;
MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG DKTKVMVSIS
LKFYKELQAH GADELLKRVY GSFLVNPESG YNVSLLYDLE NLPASKDSIV HQAGMLKRNC
FASVFEKYFQ FQEEGKEGEN RAVIHYRDDE TMYVESKKDR VTVVFSTVFK DDDDVVIGKV
FMQEFKEGRR ASHTAPQVLF SHREPPLELK DTDAAVGDNI GYITFVLFPR HTNASARDNT
INLIHTFRDY LHYHIKCSKA YIHTRMRAKT SDFLKVLNRA RPDAEKKEMK TITGKTFSSR
//
ID ARPC2_HUMAN Reviewed; 300 AA.
AC O15144; Q92801; Q9P1D4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Actin-related protein 2/3 complex subunit 2;
DE AltName: Full=Arp2/3 complex 34 kDa subunit;
DE Short=p34-ARC;
GN Name=ARPC2; Synonyms=ARC34; ORFNames=PRO2446;
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].
RX PubMed=8812419; DOI=10.1006/geno.1996.0428;
RA Couch F.J., Rommens J.M., Neuhausen S.L., Belanger C., Dumont M.,
RA Kenneth A., Bell R., Berry S., Bogden R., Cannon-Albright L.,
RA Farid L., Frye C., Hattier T., Janecki T., Jiang P., Kehrer R.,
RA Leblanc J.F., McArthur-Morrison J., McSweeney D., Miki Y., Peng Y.,
RA Samson C., Schroeder M., Snyder S.C., Stringfellow M., Stroup C.,
RA Swedlund B., Swensen J., Teng D., Thakur S., Tran T., Tranchant M.,
RA Welver-Feldhaus J., Wong A.K.C., Shizuya H., Labrie F., Skolnick M.H.,
RA Goldgar D.E., Kamb A., Weber B.L., Tavtigian S.V., Simard J.;
RT "Generation of an integrated transcription map of the BRCA2 region on
RT chromosome 13q12-q13.";
RL Genomics 36:86-99(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-9.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-290.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 191-203, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP ACTIN-BINDING, AND 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275 AND LYS-295, AND MASS
RP 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 [10]
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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Functions as actin-binding component of the Arp2/3
CC complex which is involved in regulation of actin polymerization
CC and together with an activating nucleation-promoting factor (NPF)
CC mediates the formation of branched actin networks. Seems to
CC contact the mother actin filament.
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.
CC -!- INTERACTION:
CC Q9BR76:CORO1B; NbExp=2; IntAct=EBI-352356, EBI-351152;
CC P18206:VCL; NbExp=2; IntAct=EBI-352356, EBI-716775;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection.
CC -!- SIMILARITY: Belongs to the ARPC2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50874.1; Type=Frameshift; Positions=14;
CC Sequence=AAF71122.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF006085; AAB64190.1; -; mRNA.
DR EMBL; U50523; AAC50874.1; ALT_FRAME; mRNA.
DR EMBL; BT006898; AAP35544.1; -; mRNA.
DR EMBL; BC000590; AAH00590.1; -; mRNA.
DR EMBL; AF116702; AAF71122.1; ALT_INIT; mRNA.
DR RefSeq; NP_005722.1; NM_005731.3.
DR RefSeq; NP_690601.1; NM_152862.2.
DR UniGene; Hs.529303; -.
DR ProteinModelPortal; O15144; -.
DR SMR; O15144; 1-283.
DR DIP; DIP-33197N; -.
DR IntAct; O15144; 9.
DR MINT; MINT-5000439; -.
DR STRING; 9606.ENSP00000295685; -.
DR PhosphoSite; O15144; -.
DR OGP; O15144; -.
DR PaxDb; O15144; -.
DR PeptideAtlas; O15144; -.
DR PRIDE; O15144; -.
DR DNASU; 10109; -.
DR Ensembl; ENST00000295685; ENSP00000295685; ENSG00000163466.
DR Ensembl; ENST00000315717; ENSP00000327137; ENSG00000163466.
DR GeneID; 10109; -.
DR KEGG; hsa:10109; -.
DR UCSC; uc002vhd.4; human.
DR CTD; 10109; -.
DR GeneCards; GC02P219081; -.
DR HGNC; HGNC:705; ARPC2.
DR HPA; CAB001994; -.
DR HPA; HPA008352; -.
DR MIM; 604224; gene.
DR neXtProt; NX_O15144; -.
DR PharmGKB; PA24999; -.
DR eggNOG; NOG327379; -.
DR HOGENOM; HOG000212535; -.
DR HOVERGEN; HBG050580; -.
DR InParanoid; O15144; -.
DR KO; K05758; -.
DR OMA; YFKFQEE; -.
DR OrthoDB; EOG73JKVS; -.
DR PhylomeDB; O15144; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; ARPC2; human.
DR GeneWiki; ARPC2; -.
DR GenomeRNAi; 10109; -.
DR NextBio; 38237; -.
DR PRO; PR:O15144; -.
DR ArrayExpress; O15144; -.
DR Bgee; O15144; -.
DR CleanEx; HS_ARPC2; -.
DR Genevestigator; O15144; -.
DR GO; GO:0005885; C:Arp2/3 protein complex; TAS:ProtInc.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0006928; P:cellular component movement; TAS:ProtInc.
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:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR InterPro; IPR007188; P34-arc.
DR PANTHER; PTHR12058; PTHR12058; 1.
DR Pfam; PF04045; P34-Arc; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cell projection; Complete proteome;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT CHAIN 1 300 Actin-related protein 2/3 complex subunit
FT 2.
FT /FTId=PRO_0000124033.
FT MOD_RES 275 275 N6-acetyllysine.
FT MOD_RES 295 295 N6-acetyllysine.
FT CONFLICT 72 72 A -> C (in Ref. 2; AAC50874).
FT CONFLICT 289 300 MKTITGKTFSSR -> KI (in Ref. 6; AAF71122).
SQ SEQUENCE 300 AA; 34333 MW; 3BA57121BE9A05F2 CRC64;
MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG DKTKVMVSIS
LKFYKELQAH GADELLKRVY GSFLVNPESG YNVSLLYDLE NLPASKDSIV HQAGMLKRNC
FASVFEKYFQ FQEEGKEGEN RAVIHYRDDE TMYVESKKDR VTVVFSTVFK DDDDVVIGKV
FMQEFKEGRR ASHTAPQVLF SHREPPLELK DTDAAVGDNI GYITFVLFPR HTNASARDNT
INLIHTFRDY LHYHIKCSKA YIHTRMRAKT SDFLKVLNRA RPDAEKKEMK TITGKTFSSR
//
MIM
604224
*RECORD*
*FIELD* NO
604224
*FIELD* TI
*604224 ACTIN-RELATED PROTEIN 2/3 COMPLEX, SUBUNIT 2; ARPC2
;;ACTIN-RELATED PROTEIN 2/3 COMPLEX, 34-KD SUBUNIT; ARC34;;
read morep34-ARC
*FIELD* TX
DESCRIPTION
The Arp2/3 protein complex has been implicated in the control of actin
polymerization in cells. The human complex consists of 7 subunits: the
actin-related proteins ARP2 (ACTR2; 604221) and ARP3 (ACTR3; 604222),
ARC41 (ARPC1B; 604223), ARC34 (ARPC2), ARC21 (ARPC3; 604225), ARC20
(ARPC4; 604226), and ARC16 (ARPC5; 604227) (summary by Welch et al.,
1997). 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 ARC34 cDNA encodes a deduced
300-amino acid protein that is 34% identical to its homolog in S.
cerevisiae. ARC34 localizes to the lamellipodia of stationary and motile
fibroblasts, as well as to the actin tails assembled by Listeria
monocytogenes. ARC34 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. They
identified full-length human cDNAs encoding ARC34, ARC21, and ARC16.
Western blot analysis detected ARP3 and ARC34 in all human tissues
tested. ARC34 and ARC21 were localized in the cytoplasm of fibroblasts
lacking lamellipodia, but became enriched in the lamellipodia of
stimulated fibroblasts.
GENE FUNCTION
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.
BIOCHEMICAL FEATURES
- Crystal Structure
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.
MAPPING
Welch et al. (1997) noted that a partial sequence of ARC34 (GenBank
GENBANK U50523) was mapped to the BRCA2 (600185) region on chromosome
13q12-q13 by Couch et al. (1996). However, Gross (2011) mapped the ARPC2
gene to chromosome 2q35 based on an alignment of the ARPC2 sequence
(GenBank GENBANK BC000590) with the genomic sequence (GRCh37).
*FIELD* RF
1. Couch, F. J.; Rommens, J. M.; Neuhausen, S. L.; Belanger, C.; Dumont,
M.; Abel, K.; Bell, R.; Berry, S.; Bogden, R.; Cannon-Albright, L.;
Farid, L.; Frye, C.; and 30 others: Generation of an integrated
transcription map of the BRCA2 region on chromosome 13q12-q13. Genomics 36:
86-99, 1996.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 2/25/2011.
3. 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.
4. 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.
5. 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.
6. 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.
*FIELD* CN
Matthew B. Gross - updated: 02/25/2011
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
mgross: 02/25/2011
alopez: 1/10/2002
alopez: 10/11/2001
mgross: 11/1/1999
psherman: 10/29/1999
mgross: 10/15/1999
psherman: 10/13/1999
*RECORD*
*FIELD* NO
604224
*FIELD* TI
*604224 ACTIN-RELATED PROTEIN 2/3 COMPLEX, SUBUNIT 2; ARPC2
;;ACTIN-RELATED PROTEIN 2/3 COMPLEX, 34-KD SUBUNIT; ARC34;;
read morep34-ARC
*FIELD* TX
DESCRIPTION
The Arp2/3 protein complex has been implicated in the control of actin
polymerization in cells. The human complex consists of 7 subunits: the
actin-related proteins ARP2 (ACTR2; 604221) and ARP3 (ACTR3; 604222),
ARC41 (ARPC1B; 604223), ARC34 (ARPC2), ARC21 (ARPC3; 604225), ARC20
(ARPC4; 604226), and ARC16 (ARPC5; 604227) (summary by Welch et al.,
1997). 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 ARC34 cDNA encodes a deduced
300-amino acid protein that is 34% identical to its homolog in S.
cerevisiae. ARC34 localizes to the lamellipodia of stationary and motile
fibroblasts, as well as to the actin tails assembled by Listeria
monocytogenes. ARC34 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. They
identified full-length human cDNAs encoding ARC34, ARC21, and ARC16.
Western blot analysis detected ARP3 and ARC34 in all human tissues
tested. ARC34 and ARC21 were localized in the cytoplasm of fibroblasts
lacking lamellipodia, but became enriched in the lamellipodia of
stimulated fibroblasts.
GENE FUNCTION
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.
BIOCHEMICAL FEATURES
- Crystal Structure
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.
MAPPING
Welch et al. (1997) noted that a partial sequence of ARC34 (GenBank
GENBANK U50523) was mapped to the BRCA2 (600185) region on chromosome
13q12-q13 by Couch et al. (1996). However, Gross (2011) mapped the ARPC2
gene to chromosome 2q35 based on an alignment of the ARPC2 sequence
(GenBank GENBANK BC000590) with the genomic sequence (GRCh37).
*FIELD* RF
1. Couch, F. J.; Rommens, J. M.; Neuhausen, S. L.; Belanger, C.; Dumont,
M.; Abel, K.; Bell, R.; Berry, S.; Bogden, R.; Cannon-Albright, L.;
Farid, L.; Frye, C.; and 30 others: Generation of an integrated
transcription map of the BRCA2 region on chromosome 13q12-q13. Genomics 36:
86-99, 1996.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 2/25/2011.
3. 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.
4. 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.
5. 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.
6. 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.
*FIELD* CN
Matthew B. Gross - updated: 02/25/2011
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
mgross: 02/25/2011
alopez: 1/10/2002
alopez: 10/11/2001
mgross: 11/1/1999
psherman: 10/29/1999
mgross: 10/15/1999
psherman: 10/13/1999