Full text data of ARPC5
ARPC5
(ARC16)
[Confidence: low (only semi-automatic identification from reviews)]
Actin-related protein 2/3 complex subunit 5 (Arp2/3 complex 16 kDa subunit; p16-ARC)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Actin-related protein 2/3 complex subunit 5 (Arp2/3 complex 16 kDa subunit; p16-ARC)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O15511
ID ARPC5_HUMAN Reviewed; 151 AA.
AC O15511; A6NEC4; Q6PG42;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Actin-related protein 2/3 complex subunit 5;
DE AltName: Full=Arp2/3 complex 16 kDa subunit;
DE Short=p16-ARC;
GN Name=ARPC5; Synonyms=ARC16;
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=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] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP PROTEIN SEQUENCE OF 2-10.
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 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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 component of the Arp2/3 complex which is
CC involved in regulation of actin polymerization and together with
CC an activating nucleation-promoting factor (NPF) mediates the
CC formation of branched actin networks.
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=2;
CC Name=1;
CC IsoId=O15511-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15511-2; Sequence=VSP_024028;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ARPC5 family.
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; AF006088; AAB64193.1; -; mRNA.
DR EMBL; AF017807; AAB70561.1; -; mRNA.
DR EMBL; AL137800; CAC19687.1; -; Genomic_DNA.
DR EMBL; AL137800; CAI19482.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91163.1; -; Genomic_DNA.
DR EMBL; BC057237; AAH57237.1; -; mRNA.
DR RefSeq; NP_001257368.1; NM_001270439.1.
DR RefSeq; NP_005708.1; NM_005717.3.
DR UniGene; Hs.518609; -.
DR ProteinModelPortal; O15511; -.
DR SMR; O15511; 9-150.
DR DIP; DIP-33144N; -.
DR IntAct; O15511; 4.
DR MINT; MINT-2999073; -.
DR STRING; 9606.ENSP00000352918; -.
DR PhosphoSite; O15511; -.
DR OGP; O15511; -.
DR SWISS-2DPAGE; O15511; -.
DR PaxDb; O15511; -.
DR PRIDE; O15511; -.
DR DNASU; 10092; -.
DR Ensembl; ENST00000294742; ENSP00000294742; ENSG00000162704.
DR Ensembl; ENST00000359856; ENSP00000352918; ENSG00000162704.
DR GeneID; 10092; -.
DR KEGG; hsa:10092; -.
DR UCSC; uc001gql.4; human.
DR CTD; 10092; -.
DR GeneCards; GC01M183592; -.
DR HGNC; HGNC:708; ARPC5.
DR HPA; HPA022013; -.
DR MIM; 604227; gene.
DR neXtProt; NX_O15511; -.
DR PharmGKB; PA25003; -.
DR eggNOG; NOG259254; -.
DR HOGENOM; HOG000197215; -.
DR HOVERGEN; HBG050583; -.
DR KO; K05754; -.
DR OMA; STMSARF; -.
DR PhylomeDB; O15511; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; ARPC5; human.
DR GeneWiki; ARPC5; -.
DR GenomeRNAi; 10092; -.
DR NextBio; 38165; -.
DR PRO; PR:O15511; -.
DR ArrayExpress; O15511; -.
DR Bgee; O15511; -.
DR CleanEx; HS_ARPC5; -.
DR Genevestigator; O15511; -.
DR GO; GO:0005885; C:Arp2/3 protein complex; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; 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:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 1.25.40.190; -; 1.
DR InterPro; IPR006789; ARP2/3_p16_Arc.
DR PANTHER; PTHR12644; PTHR12644; 1.
DR Pfam; PF04699; P16-Arc; 1.
DR SUPFAM; SSF69103; SSF69103; 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 2 151 Actin-related protein 2/3 complex subunit
FT 5.
FT /FTId=PRO_0000124054.
FT MOD_RES 2 2 N-acetylserine.
FT VAR_SEQ 48 48 Q -> HSIT (in isoform 2).
FT /FTId=VSP_024028.
SQ SEQUENCE 151 AA; 16320 MW; F050B11774EA6E66 CRC64;
MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK
NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN
SSAMLLQWHE KALAAGGVGS IVRVLTARKT V
//
ID ARPC5_HUMAN Reviewed; 151 AA.
AC O15511; A6NEC4; Q6PG42;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Actin-related protein 2/3 complex subunit 5;
DE AltName: Full=Arp2/3 complex 16 kDa subunit;
DE Short=p16-ARC;
GN Name=ARPC5; Synonyms=ARC16;
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=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] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP PROTEIN SEQUENCE OF 2-10.
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 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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 component of the Arp2/3 complex which is
CC involved in regulation of actin polymerization and together with
CC an activating nucleation-promoting factor (NPF) mediates the
CC formation of branched actin networks.
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=2;
CC Name=1;
CC IsoId=O15511-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15511-2; Sequence=VSP_024028;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ARPC5 family.
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; AF006088; AAB64193.1; -; mRNA.
DR EMBL; AF017807; AAB70561.1; -; mRNA.
DR EMBL; AL137800; CAC19687.1; -; Genomic_DNA.
DR EMBL; AL137800; CAI19482.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91163.1; -; Genomic_DNA.
DR EMBL; BC057237; AAH57237.1; -; mRNA.
DR RefSeq; NP_001257368.1; NM_001270439.1.
DR RefSeq; NP_005708.1; NM_005717.3.
DR UniGene; Hs.518609; -.
DR ProteinModelPortal; O15511; -.
DR SMR; O15511; 9-150.
DR DIP; DIP-33144N; -.
DR IntAct; O15511; 4.
DR MINT; MINT-2999073; -.
DR STRING; 9606.ENSP00000352918; -.
DR PhosphoSite; O15511; -.
DR OGP; O15511; -.
DR SWISS-2DPAGE; O15511; -.
DR PaxDb; O15511; -.
DR PRIDE; O15511; -.
DR DNASU; 10092; -.
DR Ensembl; ENST00000294742; ENSP00000294742; ENSG00000162704.
DR Ensembl; ENST00000359856; ENSP00000352918; ENSG00000162704.
DR GeneID; 10092; -.
DR KEGG; hsa:10092; -.
DR UCSC; uc001gql.4; human.
DR CTD; 10092; -.
DR GeneCards; GC01M183592; -.
DR HGNC; HGNC:708; ARPC5.
DR HPA; HPA022013; -.
DR MIM; 604227; gene.
DR neXtProt; NX_O15511; -.
DR PharmGKB; PA25003; -.
DR eggNOG; NOG259254; -.
DR HOGENOM; HOG000197215; -.
DR HOVERGEN; HBG050583; -.
DR KO; K05754; -.
DR OMA; STMSARF; -.
DR PhylomeDB; O15511; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; ARPC5; human.
DR GeneWiki; ARPC5; -.
DR GenomeRNAi; 10092; -.
DR NextBio; 38165; -.
DR PRO; PR:O15511; -.
DR ArrayExpress; O15511; -.
DR Bgee; O15511; -.
DR CleanEx; HS_ARPC5; -.
DR Genevestigator; O15511; -.
DR GO; GO:0005885; C:Arp2/3 protein complex; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; 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:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 1.25.40.190; -; 1.
DR InterPro; IPR006789; ARP2/3_p16_Arc.
DR PANTHER; PTHR12644; PTHR12644; 1.
DR Pfam; PF04699; P16-Arc; 1.
DR SUPFAM; SSF69103; SSF69103; 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 2 151 Actin-related protein 2/3 complex subunit
FT 5.
FT /FTId=PRO_0000124054.
FT MOD_RES 2 2 N-acetylserine.
FT VAR_SEQ 48 48 Q -> HSIT (in isoform 2).
FT /FTId=VSP_024028.
SQ SEQUENCE 151 AA; 16320 MW; F050B11774EA6E66 CRC64;
MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK
NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN
SSAMLLQWHE KALAAGGVGS IVRVLTARKT V
//
MIM
604227
*RECORD*
*FIELD* NO
604227
*FIELD* TI
*604227 ACTIN-RELATED PROTEIN 2/3 COMPLEX, SUBUNIT 5; ARPC5
;;ACTIN-RELATED PROTEIN 2/3 COMPLEX, 16-KD SUBUNIT; ARC16;;
read morep16-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; 604226), and ARC16 (ARPC5). 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 ARC16 cDNA encodes a deduced
151-amino acid protein that is 26% and 21% 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. They
identified full-length human cDNAs encoding ARC34, ARC21, and ARC16.
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. 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
Patti M. Sherman - updated: 10/29/1999
*FIELD* CD
Patti M. Sherman: 10/8/1999
*FIELD* ED
alopez: 01/10/2002
mgross: 11/1/1999
psherman: 10/29/1999
mgross: 10/15/1999
psherman: 10/13/1999
*RECORD*
*FIELD* NO
604227
*FIELD* TI
*604227 ACTIN-RELATED PROTEIN 2/3 COMPLEX, SUBUNIT 5; ARPC5
;;ACTIN-RELATED PROTEIN 2/3 COMPLEX, 16-KD SUBUNIT; ARC16;;
read morep16-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; 604226), and ARC16 (ARPC5). 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 ARC16 cDNA encodes a deduced
151-amino acid protein that is 26% and 21% 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. They
identified full-length human cDNAs encoding ARC34, ARC21, and ARC16.
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. 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
Patti M. Sherman - updated: 10/29/1999
*FIELD* CD
Patti M. Sherman: 10/8/1999
*FIELD* ED
alopez: 01/10/2002
mgross: 11/1/1999
psherman: 10/29/1999
mgross: 10/15/1999
psherman: 10/13/1999