ARC2A_ARATH
ID ARC2A_ARATH Reviewed; 318 AA.
AC Q8LGI3; Q9SY27;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Actin-related protein 2/3 complex subunit 2A;
DE AltName: Full=Actin-related protein C2A;
DE AltName: Full=Arp2/3 complex 34 kDa subunit;
DE Short=p34-ARC;
DE AltName: Full=Protein DISTORTED TRICHOMES 2;
GN Name=ARPC2A; Synonyms=DIS2; OrderedLocusNames=At1g30825; ORFNames=T17H7.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, AND IDENTIFICATION OF THE ARP2/3 COMPLEX.
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15295064; DOI=10.1093/pcp/pch103;
RA Saedler R., Mathur N., Srinivas B.P., Kernebeck B., Huelskamp M.,
RA Mathur J.;
RT "Actin control over microtubules suggested by DISTORTED2 encoding the
RT Arabidopsis ARPC2 subunit homolog.";
RL Plant Cell Physiol. 45:813-822(2004).
RN [8]
RP FUNCTION, INTERACTION WITH ARPC4, AND 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 [9]
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).
CC -!- FUNCTION: Functions as actin-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 mother actin
CC filament (By similarity). Arp2/3 complex plays a critical role in the
CC control of cell morphogenesis via the modulation of cell polarity
CC development. {ECO:0000250, ECO:0000269|PubMed:15086808,
CC ECO:0000269|PubMed:15295064}.
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 with ARPC4. {ECO:0000269|PubMed:15086808}.
CC -!- INTERACTION:
CC Q8LGI3; F4JUL9: ARPC4; NbExp=3; IntAct=EBI-1547736, EBI-1547718;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in all tissues with a
CC relatively highest expression in inflorescences.
CC {ECO:0000269|PubMed:12913159, ECO:0000269|PubMed:15086808}.
CC -!- DISRUPTION PHENOTYPE: Distorted trichomes.
CC {ECO:0000269|PubMed:15295064}.
CC -!- SIMILARITY: Belongs to the ARPC2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD32938.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004135; AAD32938.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31281.1; -; Genomic_DNA.
DR EMBL; AK118475; BAC43079.1; -; mRNA.
DR EMBL; BT005308; AAO63372.1; -; mRNA.
DR EMBL; AY084256; AAM60850.1; -; mRNA.
DR PIR; B86434; B86434.
DR RefSeq; NP_564364.1; NM_102820.3.
DR AlphaFoldDB; Q8LGI3; -.
DR SMR; Q8LGI3; -.
DR BioGRID; 25200; 2.
DR IntAct; Q8LGI3; 2.
DR STRING; 3702.AT1G30825.1; -.
DR PaxDb; Q8LGI3; -.
DR PRIDE; Q8LGI3; -.
DR ProteomicsDB; 244429; -.
DR EnsemblPlants; AT1G30825.1; AT1G30825.1; AT1G30825.
DR GeneID; 839965; -.
DR Gramene; AT1G30825.1; AT1G30825.1; AT1G30825.
DR KEGG; ath:AT1G30825; -.
DR Araport; AT1G30825; -.
DR TAIR; locus:505006160; AT1G30825.
DR eggNOG; KOG2826; Eukaryota.
DR HOGENOM; CLU_059439_0_0_1; -.
DR InParanoid; Q8LGI3; -.
DR OMA; GPYIVSP; -.
DR OrthoDB; 1345377at2759; -.
DR PhylomeDB; Q8LGI3; -.
DR PRO; PR:Q8LGI3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LGI3; baseline and differential.
DR Genevisible; Q8LGI3; AT.
DR GO; GO:0005885; C:Arp2/3 protein complex; IMP:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; TAS:TAIR.
DR GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0010090; P:trichome morphogenesis; NAS:TAIR.
DR Gene3D; 3.30.1460.20; -; 2.
DR InterPro; IPR007188; ARPC2.
DR InterPro; IPR034666; ARPC2/4.
DR PANTHER; PTHR12058; PTHR12058; 1.
DR Pfam; PF04045; P34-Arc; 1.
DR SUPFAM; SSF69645; SSF69645; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..318
FT /note="Actin-related protein 2/3 complex subunit 2A"
FT /id="PRO_0000422528"
FT REGION 297..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 318 AA; 36041 MW; 303D30BAC3EB3798 CRC64;
MILLQSHSRF LLQTLLTRAQ NLDKAVELDY QWIEFDDVRY HVQVTMKNPN LLLLSVSLPN
PPPEAMSFDG LPLGAIEAIK TTYGTGFQIL DPPRDGFSLT LKLNFSKVRP DEELLTKLAS
IREVVMGAPL KIIFKHLASR TVAPELDRLV AIMHRPNETF FLVPQADKVT VAFPMRFKDS
VDTILATSFL KEFVEARRAA ALNTAPSCSW SPTAPQELEG APKETLSANA GFVTFVIFPR
HVEGKKLDRT VWNLSTFHAY VSYHVKFSEG FMHTRMRRRV ESMIQALDQA KPLEKTRSMN
NKSFKRLGLN EVNHTNSK
