Full text data of ARPC4
ARPC4
(ARC20)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Actin-related protein 2/3 complex subunit 4 (Arp2/3 complex 20 kDa subunit; p20-ARC)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Actin-related protein 2/3 complex subunit 4 (Arp2/3 complex 20 kDa subunit; p20-ARC)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P59998
ID ARPC4_HUMAN Reviewed; 168 AA.
AC P59998; C9JWM7; E7ETI0; F6TTL5; O15509; Q6P0W5; Q96QJ3;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Actin-related protein 2/3 complex subunit 4;
DE AltName: Full=Arp2/3 complex 20 kDa subunit;
DE Short=p20-ARC;
GN Name=ARPC4; Synonyms=ARC20;
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=9359840;
RA Machesky L.M., Reeves E., Wientjes F., Mattheyse F.J., Grogan A.,
RA Totty N.F., Burlingame A.L., Hsuan J.J., Segal A.W.;
RT "Mammalian actin-related protein 2/3 complex localizes to regions of
RT lamellipodial protrusion and is composed of evolutionarily conserved
RT proteins.";
RL Biochem. J. 328:105-112(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2-168 (ISOFORM 1).
RC TISSUE=Choriocarcinoma, and Prostate;
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 [6]
RP PROTEIN SEQUENCE OF 2-13, AND ACETYLATION AT THR-2.
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 [7]
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 [8]
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 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P59998-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P59998-2; Sequence=VSP_046151;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P59998-3; Sequence=VSP_046150;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=P59998-4; Sequence=VSP_046753;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- SIMILARITY: Belongs to the ARPC4 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12596.3; Type=Erroneous initiation; Note=Translation N-terminally extended;
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; AF019888; AAB71548.1; -; mRNA.
DR EMBL; AF006087; AAB64192.1; -; mRNA.
DR EMBL; BX419672; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC022382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012596; AAH12596.3; ALT_INIT; mRNA.
DR EMBL; BC025289; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001020130.1; NM_001024959.2.
DR RefSeq; NP_001020131.1; NM_001024960.2.
DR RefSeq; NP_001185709.1; NM_001198780.1.
DR RefSeq; NP_001185722.1; NM_001198793.1.
DR RefSeq; NP_005709.1; NM_005718.4.
DR UniGene; Hs.323342; -.
DR ProteinModelPortal; P59998; -.
DR SMR; P59998; 2-168.
DR DIP; DIP-33188N; -.
DR IntAct; P59998; 9.
DR MINT; MINT-5000208; -.
DR STRING; 9606.ENSP00000380431; -.
DR PhosphoSite; P59998; -.
DR DMDM; 38372625; -.
DR PaxDb; P59998; -.
DR PRIDE; P59998; -.
DR DNASU; 10093; -.
DR Ensembl; ENST00000287613; ENSP00000287613; ENSG00000241553.
DR Ensembl; ENST00000397261; ENSP00000380431; ENSG00000241553.
DR Ensembl; ENST00000433034; ENSP00000388169; ENSG00000241553.
DR Ensembl; ENST00000498623; ENSP00000432235; ENSG00000241553.
DR GeneID; 100526693; -.
DR GeneID; 10093; -.
DR KEGG; hsa:100526693; -.
DR KEGG; hsa:10093; -.
DR UCSC; uc021wsu.1; human.
DR CTD; 100526693; -.
DR CTD; 10093; -.
DR GeneCards; GC03P009834; -.
DR HGNC; HGNC:707; ARPC4.
DR MIM; 604226; gene.
DR neXtProt; NX_P59998; -.
DR PharmGKB; PA25002; -.
DR eggNOG; NOG261545; -.
DR HOGENOM; HOG000202303; -.
DR HOVERGEN; HBG050582; -.
DR KO; K05755; -.
DR OMA; MLKHKIV; -.
DR OrthoDB; EOG7VTDPM; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; ARPC4; human.
DR GeneWiki; ARPC4; -.
DR GenomeRNAi; 10093; -.
DR NextBio; 34054911; -.
DR PRO; PR:P59998; -.
DR ArrayExpress; P59998; -.
DR Bgee; P59998; -.
DR CleanEx; HS_ARPC4; -.
DR Genevestigator; P59998; -.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; NAS:UniProtKB.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:InterPro.
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 InterPro; IPR008384; ARPC4.
DR PANTHER; PTHR22629; PTHR22629; 1.
DR Pfam; PF05856; ARPC4; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell projection;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 168 Actin-related protein 2/3 complex subunit
FT 4.
FT /FTId=PRO_0000124049.
FT MOD_RES 2 2 N-acetylthreonine.
FT VAR_SEQ 1 90 Missing (in isoform 4).
FT /FTId=VSP_046753.
FT VAR_SEQ 1 1 M -> MVREPGPRPGTPGCSASGQW (in isoform 3).
FT /FTId=VSP_046150.
FT VAR_SEQ 110 168 EGYDISFLITNFHTEQMYKHKLVDFVIHFMEEIDKEISEMK
FT LSVNARARIVAEEFLKNF -> EQKKIFTIQGCYPVIRCLL
FT RRRGWVEKKMVHRSGPTLLPPQKDLDSSAMGDSDTTEDEDE
FT DEDEEFQPSQLFDFDDLLKFDDLDGTHALMVGLCLNLRNLP
FT WFDEVDANSFFPRCYCLGAEDDKKAFIGDKQPKKQEKNPVL
FT VSPEFVDEALCACEEYLSNLAHMDIDKDLEAPLYLTPEGWS
FT LFLQRYYQVVHEGAELRHLDTQVQRCEDILQQLQAVVPQID
FT MEGDRNIWIVKPGAKSRGRGIMCMDHLEEMLKLVNGNPVVM
FT KDGKWVVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFY
FT RDSYIRFSTQPFSLKNLDNSVHLCNNSIQKHLENSCHRHPL
FT LPPDNMWSSQRFQAHLQEMGAPNAWSTIIVPGMKDAVIHAL
FT QTSQDTVQCRKASFELYGADFVFGEDFQPWLIEINASPTMA
FT PSTAVTARLCAGVQADTLRVVIDRMLDRNCDTGAFELIYKQ
FT PVTTSPASTPRPSCLLPMYSDTRARSSDDSTASWWALRPCR
FT PQARP (in isoform 2).
FT /FTId=VSP_046151.
FT CONFLICT 94 94 M -> T (in Ref. 5; AAH12596).
SQ SEQUENCE 168 AA; 19667 MW; 273CCB230AC703DF CRC64;
MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP VTISRNEKEK
VLIEGSINSV RVSIAVKQAD EIEKILCHKF MRFMMMRAEN FFILRRKPVE GYDISFLITN
FHTEQMYKHK LVDFVIHFME EIDKEISEMK LSVNARARIV AEEFLKNF
//
ID ARPC4_HUMAN Reviewed; 168 AA.
AC P59998; C9JWM7; E7ETI0; F6TTL5; O15509; Q6P0W5; Q96QJ3;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Actin-related protein 2/3 complex subunit 4;
DE AltName: Full=Arp2/3 complex 20 kDa subunit;
DE Short=p20-ARC;
GN Name=ARPC4; Synonyms=ARC20;
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=9359840;
RA Machesky L.M., Reeves E., Wientjes F., Mattheyse F.J., Grogan A.,
RA Totty N.F., Burlingame A.L., Hsuan J.J., Segal A.W.;
RT "Mammalian actin-related protein 2/3 complex localizes to regions of
RT lamellipodial protrusion and is composed of evolutionarily conserved
RT proteins.";
RL Biochem. J. 328:105-112(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2-168 (ISOFORM 1).
RC TISSUE=Choriocarcinoma, and Prostate;
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 [6]
RP PROTEIN SEQUENCE OF 2-13, AND ACETYLATION AT THR-2.
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 [7]
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 [8]
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 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P59998-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P59998-2; Sequence=VSP_046151;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P59998-3; Sequence=VSP_046150;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=P59998-4; Sequence=VSP_046753;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- SIMILARITY: Belongs to the ARPC4 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12596.3; Type=Erroneous initiation; Note=Translation N-terminally extended;
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; AF019888; AAB71548.1; -; mRNA.
DR EMBL; AF006087; AAB64192.1; -; mRNA.
DR EMBL; BX419672; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC022382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012596; AAH12596.3; ALT_INIT; mRNA.
DR EMBL; BC025289; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001020130.1; NM_001024959.2.
DR RefSeq; NP_001020131.1; NM_001024960.2.
DR RefSeq; NP_001185709.1; NM_001198780.1.
DR RefSeq; NP_001185722.1; NM_001198793.1.
DR RefSeq; NP_005709.1; NM_005718.4.
DR UniGene; Hs.323342; -.
DR ProteinModelPortal; P59998; -.
DR SMR; P59998; 2-168.
DR DIP; DIP-33188N; -.
DR IntAct; P59998; 9.
DR MINT; MINT-5000208; -.
DR STRING; 9606.ENSP00000380431; -.
DR PhosphoSite; P59998; -.
DR DMDM; 38372625; -.
DR PaxDb; P59998; -.
DR PRIDE; P59998; -.
DR DNASU; 10093; -.
DR Ensembl; ENST00000287613; ENSP00000287613; ENSG00000241553.
DR Ensembl; ENST00000397261; ENSP00000380431; ENSG00000241553.
DR Ensembl; ENST00000433034; ENSP00000388169; ENSG00000241553.
DR Ensembl; ENST00000498623; ENSP00000432235; ENSG00000241553.
DR GeneID; 100526693; -.
DR GeneID; 10093; -.
DR KEGG; hsa:100526693; -.
DR KEGG; hsa:10093; -.
DR UCSC; uc021wsu.1; human.
DR CTD; 100526693; -.
DR CTD; 10093; -.
DR GeneCards; GC03P009834; -.
DR HGNC; HGNC:707; ARPC4.
DR MIM; 604226; gene.
DR neXtProt; NX_P59998; -.
DR PharmGKB; PA25002; -.
DR eggNOG; NOG261545; -.
DR HOGENOM; HOG000202303; -.
DR HOVERGEN; HBG050582; -.
DR KO; K05755; -.
DR OMA; MLKHKIV; -.
DR OrthoDB; EOG7VTDPM; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; ARPC4; human.
DR GeneWiki; ARPC4; -.
DR GenomeRNAi; 10093; -.
DR NextBio; 34054911; -.
DR PRO; PR:P59998; -.
DR ArrayExpress; P59998; -.
DR Bgee; P59998; -.
DR CleanEx; HS_ARPC4; -.
DR Genevestigator; P59998; -.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; NAS:UniProtKB.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:InterPro.
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 InterPro; IPR008384; ARPC4.
DR PANTHER; PTHR22629; PTHR22629; 1.
DR Pfam; PF05856; ARPC4; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell projection;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 168 Actin-related protein 2/3 complex subunit
FT 4.
FT /FTId=PRO_0000124049.
FT MOD_RES 2 2 N-acetylthreonine.
FT VAR_SEQ 1 90 Missing (in isoform 4).
FT /FTId=VSP_046753.
FT VAR_SEQ 1 1 M -> MVREPGPRPGTPGCSASGQW (in isoform 3).
FT /FTId=VSP_046150.
FT VAR_SEQ 110 168 EGYDISFLITNFHTEQMYKHKLVDFVIHFMEEIDKEISEMK
FT LSVNARARIVAEEFLKNF -> EQKKIFTIQGCYPVIRCLL
FT RRRGWVEKKMVHRSGPTLLPPQKDLDSSAMGDSDTTEDEDE
FT DEDEEFQPSQLFDFDDLLKFDDLDGTHALMVGLCLNLRNLP
FT WFDEVDANSFFPRCYCLGAEDDKKAFIGDKQPKKQEKNPVL
FT VSPEFVDEALCACEEYLSNLAHMDIDKDLEAPLYLTPEGWS
FT LFLQRYYQVVHEGAELRHLDTQVQRCEDILQQLQAVVPQID
FT MEGDRNIWIVKPGAKSRGRGIMCMDHLEEMLKLVNGNPVVM
FT KDGKWVVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFY
FT RDSYIRFSTQPFSLKNLDNSVHLCNNSIQKHLENSCHRHPL
FT LPPDNMWSSQRFQAHLQEMGAPNAWSTIIVPGMKDAVIHAL
FT QTSQDTVQCRKASFELYGADFVFGEDFQPWLIEINASPTMA
FT PSTAVTARLCAGVQADTLRVVIDRMLDRNCDTGAFELIYKQ
FT PVTTSPASTPRPSCLLPMYSDTRARSSDDSTASWWALRPCR
FT PQARP (in isoform 2).
FT /FTId=VSP_046151.
FT CONFLICT 94 94 M -> T (in Ref. 5; AAH12596).
SQ SEQUENCE 168 AA; 19667 MW; 273CCB230AC703DF CRC64;
MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP VTISRNEKEK
VLIEGSINSV RVSIAVKQAD EIEKILCHKF MRFMMMRAEN FFILRRKPVE GYDISFLITN
FHTEQMYKHK LVDFVIHFME EIDKEISEMK LSVNARARIV AEEFLKNF
//
MIM
604226
*RECORD*
*FIELD* NO
604226
*FIELD* TI
*604226 ACTIN-RELATED PROTEIN 2/3 COMPLEX, SUBUNIT 4; ARPC4
;;ACTIN-RELATED PROTEIN 2/3 COMPLEX, 20-KD SUBUNIT; ARC20;;
read morep20-ARC
*FIELD* TX
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; 604224), ARC21 (ARPC3; 604225),
ARC20 (ARPC4), 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 ARC20 cDNA encodes a deduced
168-amino acid protein that is 68% and 67% identical to its homologs in
S. pombe and S. cerevisiae, respectively.
Machesky et al. (1997) purified the ARP2/3 complex from human
neutrophils and sequenced peptides from each of the subunits.
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.
*FIELD* RF
1. 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.
2. 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.
3. 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.
4. 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
Ada Hamosh - updated: 01/10/2002
Ada Hamosh - updated: 10/11/2001
Patti M. Sherman - updated: 10/29/1999
*FIELD* CD
Patti M. Sherman: 10/8/1999
*FIELD* ED
alopez: 01/10/2002
alopez: 10/11/2001
mgross: 11/1/1999
psherman: 10/29/1999
mgross: 10/15/1999
psherman: 10/13/1999
*RECORD*
*FIELD* NO
604226
*FIELD* TI
*604226 ACTIN-RELATED PROTEIN 2/3 COMPLEX, SUBUNIT 4; ARPC4
;;ACTIN-RELATED PROTEIN 2/3 COMPLEX, 20-KD SUBUNIT; ARC20;;
read morep20-ARC
*FIELD* TX
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; 604224), ARC21 (ARPC3; 604225),
ARC20 (ARPC4), 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 ARC20 cDNA encodes a deduced
168-amino acid protein that is 68% and 67% identical to its homologs in
S. pombe and S. cerevisiae, respectively.
Machesky et al. (1997) purified the ARP2/3 complex from human
neutrophils and sequenced peptides from each of the subunits.
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.
*FIELD* RF
1. 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.
2. 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.
3. 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.
4. 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
Ada Hamosh - updated: 01/10/2002
Ada Hamosh - updated: 10/11/2001
Patti M. Sherman - updated: 10/29/1999
*FIELD* CD
Patti M. Sherman: 10/8/1999
*FIELD* ED
alopez: 01/10/2002
alopez: 10/11/2001
mgross: 11/1/1999
psherman: 10/29/1999
mgross: 10/15/1999
psherman: 10/13/1999