ARP2_ARATH
ID ARP2_ARATH Reviewed; 389 AA.
AC Q9LSD6; Q9ZSS8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Actin-related protein 2;
DE AltName: Full=Protein WURM;
GN Name=ARP2; Synonyms=WRM; OrderedLocusNames=At3g27000; ORFNames=MOJ10.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY LIGHT, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10561069; DOI=10.1023/a:1006247600932;
RA Klahre U., Chua N.-H.;
RT "The Arabidopsis ACTIN-RELATED PROTEIN 2 (AtARP2) promoter directs
RT expression in xylem precursor cells and pollen.";
RL Plant Mol. Biol. 41:65-73(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, TISSUE SPECIFICITY, AND GENE
RP FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=11891255; DOI=10.1104/pp.010906;
RA McKinney E.C., Kandasamy M.K., Meagher R.B.;
RT "Arabidopsis contains ancient classes of differentially expressed actin-
RT related protein genes.";
RL Plant Physiol. 128:997-1007(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP FUNCTION.
RX PubMed=10572033; DOI=10.1242/dev.126.24.5559;
RA Mathur J., Spielhofer P., Kost B., Chua N.-H.;
RT "The actin cytoskeleton is required to elaborate and maintain spatial
RT patterning during trichome cell morphogenesis in Arabidopsis thaliana.";
RL Development 126:5559-5568(1999).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12906796; DOI=10.1016/s0960-9822(03)00493-7;
RA Le J., El-Din El-Assal S., Basu D., Saad M.E., Szymanski D.B.;
RT "Requirements for Arabidopsis ATARP2 and ATARP3 during epidermal
RT development.";
RL Curr. Biol. 13:1341-1347(2003).
RN [7]
RP FUNCTION.
RX PubMed=12690443; DOI=10.1007/s00438-003-0843-1;
RA Schwab B., Mathur J., Saedler R., Schwarz H., Frey B., Scheidegger C.,
RA Huelskamp M.;
RT "Regulation of cell expansion by the DISTORTED genes in Arabidopsis
RT thaliana: actin controls the spatial organization of microtubules.";
RL Mol. Genet. Genomics 269:350-360(2003).
RN [8]
RP FUNCTION, MUTAGENESIS OF GLY-151, AND DISRUPTION PHENOTYPE.
RX PubMed=12837952; DOI=10.1105/tpc.011676;
RA Mathur J., Mathur N., Kernebeck B., Huelskamp M.;
RT "Mutations in actin-related proteins 2 and 3 affect cell shape development
RT in Arabidopsis.";
RL Plant Cell 15:1632-1645(2003).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION OF THE ARP2/3 COMPLEX, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12913159; DOI=10.1104/pp.103.028563;
RA Li S., Blanchoin L., Yang Z., Lord E.M.;
RT "The putative Arabidopsis arp2/3 complex controls leaf cell
RT morphogenesis.";
RL Plant Physiol. 132:2034-2044(2003).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=15086808; DOI=10.1111/j.1365-313x.2004.02065.x;
RA El-Din El-Assal S., Le J., Basu D., Mallery E.L., Szymanski D.B.;
RT "DISTORTED2 encodes an ARPC2 subunit of the putative Arabidopsis ARP2/3
RT complex.";
RL Plant J. 38:526-538(2004).
RN [11]
RP REVIEW, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15063870; DOI=10.1016/j.tplants.2004.02.004;
RA Kandasamy M.K., Deal R.B., McKinney E.C., Meagher R.B.;
RT "Plant actin-related proteins.";
RL Trends Plant Sci. 9:196-202(2004).
RN [12]
RP REVIEW.
RX PubMed=15653407; DOI=10.1016/j.pbi.2004.11.004;
RA Szymanski D.B.;
RT "Breaking the WAVE complex: the point of Arabidopsis trichomes.";
RL Curr. Opin. Plant Biol. 8:103-112(2005).
RN [13]
RP INTERACTION WITH ARP3 AND ABI1.
RX PubMed=17267444; DOI=10.1242/dev.02792;
RA Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M.,
RA Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.;
RT "The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell
RT morphogenesis.";
RL Development 134:967-977(2007).
CC -!- FUNCTION: Functions as ATP-binding component of the Arp2/3 complex
CC which is involved in regulation of actin polymerization and together
CC with an activating nucleation-promoting factor (NPF) mediates the
CC formation of branched actin networks. Seems to contact the pointed end
CC of the daughter actin filament (By similarity). Arp2/3 complex plays a
CC critical role in the control of cell morphogenesis via the modulation
CC of cell polarity development. Involved in the control of cell
CC morphogenesis in leaf epidermal pavement cells, root hairs, hypocotyls
CC epidermal cells and trichomes, especially during rapid cell expansion.
CC Regulates the directionality of cell expansion by regulating the actin
CC organization, and thus the microtubules distribution and the fusion of
CC small vacuoles. {ECO:0000250, ECO:0000269|PubMed:10572033,
CC ECO:0000269|PubMed:12690443, ECO:0000269|PubMed:12837952,
CC ECO:0000269|PubMed:12906796, ECO:0000269|PubMed:12913159}.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of ARP2, ARP3,
CC ARPC1/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and
CC ARPC5/p16-ARC. Interacts directly with ARP3/DIS1 and ABI1.
CC {ECO:0000269|PubMed:17267444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, seedlings, stems,
CC leaves, flowers, pollen, siliques and at a higher level in
CC inflorescences. Specifically localized in cells adjacent to mature
CC xylem and in developing xylem vessels. {ECO:0000269|PubMed:10561069,
CC ECO:0000269|PubMed:11891255, ECO:0000269|PubMed:12913159,
CC ECO:0000269|PubMed:15086808}.
CC -!- INDUCTION: Repressed by light. {ECO:0000269|PubMed:10561069}.
CC -!- DISRUPTION PHENOTYPE: Distorted trichomes and altered epidermal cell
CC types. {ECO:0000269|PubMed:12837952, ECO:0000269|PubMed:12906796,
CC ECO:0000269|PubMed:12913159}.
CC -!- MISCELLANEOUS: 'Wurm' means 'worm' in German. Plants impaired in WURM
CC display worm-shaped trichomes.
CC -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {ECO:0000305}.
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DR EMBL; AF095912; AAC69601.1; -; Genomic_DNA.
DR EMBL; AF507910; AAM53242.1; -; mRNA.
DR EMBL; AB026649; BAB01081.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77253.1; -; Genomic_DNA.
DR EMBL; BK000428; DAA00034.1; -; Genomic_DNA.
DR RefSeq; NP_189336.1; NM_113614.3.
DR AlphaFoldDB; Q9LSD6; -.
DR SMR; Q9LSD6; -.
DR BioGRID; 7647; 2.
DR IntAct; Q9LSD6; 2.
DR STRING; 3702.AT3G27000.1; -.
DR PaxDb; Q9LSD6; -.
DR PRIDE; Q9LSD6; -.
DR ProteomicsDB; 246889; -.
DR EnsemblPlants; AT3G27000.1; AT3G27000.1; AT3G27000.
DR GeneID; 822317; -.
DR Gramene; AT3G27000.1; AT3G27000.1; AT3G27000.
DR KEGG; ath:AT3G27000; -.
DR Araport; AT3G27000; -.
DR TAIR; locus:2092005; AT3G27000.
DR eggNOG; KOG0677; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR OMA; WEDMQHL; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; Q9LSD6; -.
DR PRO; PR:Q9LSD6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSD6; baseline and differential.
DR Genevisible; Q9LSD6; AT.
DR GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:TAIR.
DR GO; GO:0007015; P:actin filament organization; IMP:TAIR.
DR GO; GO:0030029; P:actin filament-based process; TAS:TAIR.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0010090; P:trichome morphogenesis; IMP:TAIR.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Developmental protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..389
FT /note="Actin-related protein 2"
FT /id="PRO_0000320522"
FT BINDING 157..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 211..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 302..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 151
FT /note="G->D: In wrm1-1; distorted trichomes and epidermal
FT cells."
FT /evidence="ECO:0000269|PubMed:12837952"
FT CONFLICT 149
FT /note="L -> Q (in Ref. 1; AAC69601)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="D -> G (in Ref. 1; AAC69601)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="P -> R (in Ref. 1; AAC69601)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="K -> I (in Ref. 1; AAC69601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 44356 MW; DE10C27051F8E11B CRC64;
MDNKNVVVCD NGTGYVKCGF AGENFPTSVF PCVVGRPLLR YEESLMEQQV KDIVVGETCS
ELRHQLDINY PVHNGIVQNW DDMEHVWDHA FYNELKINPS DCKILLTDPP LNPSKNREKM
IETMFEKYNF AGVFIQIQAV LTLYAQGLLT GLVIDSGDGV THVVPVVDGY SFPHLTKRMN
VAGRHITAYL VDLLSRRGYA MNKTADFETV REIKEKLCYI SYDYKRESQL GLETTILVKN
YTLPDGRVIK VGTERFQAPE ALFTPELIDV EGDGMADMVF RCIQEMDIDN RMMLYQHIVL
SGGSTMYPGL PSRLEKEIQD RYLDTVLKGN KDGLKKLRLR IEDPPRRKHM VYLGGAVLAG
IMKDAPEFWI NREDYMEEGI NCLNKMSQA
