ID   ARP3_ARATH              Reviewed;         427 AA.
AC   Q9SAF1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Actin-related protein 3;
DE   AltName: Full=Protein DISTORTED TRICHOMES 1;
GN   Name=ARP3; Synonyms=DIS1; OrderedLocusNames=At1g13180; ORFNames=F3F19.20;
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 [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   [2]
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   [3]
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   [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   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   [6]
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   [7]
RP   FUNCTION, 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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
RP   INTERACTION WITH ARP2; ABI1; ABI2; ABI4; BRICK1 AND SCAR3.
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).
RN   [13]
RP   INTERACTION WITH ARPC4.
RX   PubMed=19801398; DOI=10.1104/pp.109.143859;
RA   Kotchoni S.O., Zakharova T., Mallery E.L., Le J., El-Din El-Assal S.,
RA   Szymanski D.B.;
RT   "The association of the Arabidopsis actin-related protein2/3 complex with
RT   cell membranes is linked to its assembly status but not its activation.";
RL   Plant Physiol. 151:2095-2109(2009).
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:12690443,
CC       ECO:0000269|PubMed:12837952, ECO:0000269|PubMed:12906796,
CC       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 ARP2/WRM, ABI1, ABI2, ABI4,
CC       BRICK1 and SCAR3. Interacts with ARPC4. {ECO:0000269|PubMed:17267444,
CC       ECO:0000269|PubMed:19801398}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in roots, seedlings,
CC       leaves, stems, flowers, pollen, siliques and at a higher level in
CC       inflorescences. {ECO:0000269|PubMed:11891255,
CC       ECO:0000269|PubMed:12913159, ECO:0000269|PubMed:15086808}.
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   -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. {ECO:0000305}.
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DR   EMBL; AF507911; AAM53243.1; -; Genomic_DNA.
DR   EMBL; AC007357; AAD31071.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28980.1; -; Genomic_DNA.
DR   EMBL; AY093149; AAM13148.1; -; mRNA.
DR   EMBL; BT006584; AAP31928.1; -; mRNA.
DR   EMBL; BK000427; DAA00033.1; -; Genomic_DNA.
DR   PIR; B86266; B86266.
DR   RefSeq; NP_172777.1; NM_101188.3.
DR   AlphaFoldDB; Q9SAF1; -.
DR   SMR; Q9SAF1; -.
DR   BioGRID; 23116; 7.
DR   IntAct; Q9SAF1; 6.
DR   STRING; 3702.AT1G13180.1; -.
DR   PaxDb; Q9SAF1; -.
DR   PRIDE; Q9SAF1; -.
DR   ProteomicsDB; 246844; -.
DR   EnsemblPlants; AT1G13180.1; AT1G13180.1; AT1G13180.
DR   GeneID; 837876; -.
DR   Gramene; AT1G13180.1; AT1G13180.1; AT1G13180.
DR   KEGG; ath:AT1G13180; -.
DR   Araport; AT1G13180; -.
DR   TAIR; locus:2031815; AT1G13180.
DR   eggNOG; KOG0678; Eukaryota.
DR   HOGENOM; CLU_027965_3_0_1; -.
DR   InParanoid; Q9SAF1; -.
DR   OMA; TAEFKSY; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; Q9SAF1; -.
DR   PRO; PR:Q9SAF1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SAF1; baseline and differential.
DR   Genevisible; Q9SAF1; 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:0007015; P:actin filament organization; IMP: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   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..427
FT                   /note="Actin-related protein 3"
FT                   /id="PRO_0000320525"
SQ   SEQUENCE   427 AA;  47660 MW;  55F03ED31CB52E80 CRC64;
     MDPTSRPAIV IDNGTGYTKM GFAGNVEPCF ILPTVVAVNE SFLNQSKSSS KATWQTQHNA
     GVAADLDFYI GDEALAKSRS SSTHNLHYPI EHGQVEDWDA MERYWQQCIF NYLRCDPEDH
     YFLLTESPLT PPESREYTGE ILFETFNVPG LYIAVNSVLA LAAGYTTSKC EMTGVVVDVG
     DGATHVVPVA EGYVIGSCIK SIPIAGKDVT LFIQQLMRER GENIPPEDSF DVARKVKEMY
     CYTCSDIVKE FNKHDKEPAK YIKQWKGVKP KTGAPYTCDV GYERFLGPEV FFNPEIYSND
     FTTTLPAVID KCIQSAPIDT RRALYKNIVL SGGSTMFKDF GRRLQRDLKK IVDARVLANN
     ARTGGEITSQ PVEVNVVSHP VQRFAVWFGG SVLSSTPEFF ASCRTKEEYE EYGASICRTN
     PVFKGMY