ARPC4_ARATH
ID ARPC4_ARATH Reviewed; 169 AA.
AC F4JUL9; O23274;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Actin-related protein 2/3 complex subunit 4;
DE AltName: Full=Actin-related protein C4;
DE AltName: Full=Arp2/3 complex 20 kDa subunit;
DE Short=p20-ARC;
GN Name=ARPC4; OrderedLocusNames=At4g14147; ORFNames=dl3115c, FCAALL.159;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 TISSUE SPECIFICITY, IDENTIFICATION OF THE ARP2/3 COMPLEX, AND DISRUPTION
RP 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 [5]
RP INTERACTION WITH ARPC2A, 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 [6]
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 [7]
RP DISRUPTION PHENOTYPE, FUNCTION, IDENTIFICATION IN THE ARP2/3 COMPLEX, AND
RP INTERACTION WITH ARP3.
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 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:19801398}.
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 ARPC2A and ARP3.
CC {ECO:0000269|PubMed:15086808, ECO:0000269|PubMed:19801398}.
CC -!- INTERACTION:
CC F4JUL9; Q8LGI3: ARPC2A; NbExp=3; IntAct=EBI-1547718, EBI-1547736;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=F4JUL9-1; Sequence=Displayed;
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 and altered epidermal cell
CC types. {ECO:0000269|PubMed:12913159, ECO:0000269|PubMed:19801398}.
CC -!- SIMILARITY: Belongs to the ARPC4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10194.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 3 genes: At4g14145, At4g14147 and At4g14150.; Evidence={ECO:0000305};
CC Sequence=CAB78457.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 3 genes: At4g14145, At4g14147 and At4g14150.; Evidence={ECO:0000305};
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DR EMBL; Z97335; CAB10194.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161538; CAB78457.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83382.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66065.1; -; Genomic_DNA.
DR RefSeq; NP_001031632.1; NM_001036555.3. [F4JUL9-1]
DR RefSeq; NP_001319932.1; NM_001340903.1. [F4JUL9-1]
DR AlphaFoldDB; F4JUL9; -.
DR SMR; F4JUL9; -.
DR BioGRID; 530765; 7.
DR IntAct; F4JUL9; 5.
DR STRING; 3702.AT4G14147.2; -.
DR PRIDE; F4JUL9; -.
DR ProteomicsDB; 246675; -. [F4JUL9-1]
DR EnsemblPlants; AT4G14147.1; AT4G14147.1; AT4G14147. [F4JUL9-1]
DR EnsemblPlants; AT4G14147.3; AT4G14147.3; AT4G14147. [F4JUL9-1]
DR GeneID; 3770404; -.
DR Gramene; AT4G14147.1; AT4G14147.1; AT4G14147. [F4JUL9-1]
DR Gramene; AT4G14147.3; AT4G14147.3; AT4G14147. [F4JUL9-1]
DR KEGG; ath:AT4G14147; -.
DR Araport; AT4G14147; -.
DR eggNOG; KOG1876; Eukaryota.
DR HOGENOM; CLU_084855_1_0_1; -.
DR OMA; EAYLGEF; -.
DR PhylomeDB; F4JUL9; -.
DR PRO; PR:F4JUL9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JUL9; baseline and differential.
DR GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
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: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 Gene3D; 3.30.1460.20; -; 1.
DR InterPro; IPR034666; ARPC2/4.
DR InterPro; IPR008384; ARPC4.
DR PANTHER; PTHR22629; PTHR22629; 1.
DR Pfam; PF05856; ARPC4; 1.
DR PIRSF; PIRSF039100; ARPC4; 1.
DR SUPFAM; SSF69645; SSF69645; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative initiation; Cell projection; Cytoplasm;
KW Cytoskeleton; Reference proteome.
FT CHAIN 1..169
FT /note="Actin-related protein 2/3 complex subunit 4"
FT /id="PRO_0000422531"
SQ SEQUENCE 169 AA; 19858 MW; 5CB3BFF947D083AF CRC64;
MANSLRLYLA CIKNTLEAAM CLQNFPCQEV ERHNKPEVEL KTSPELLLNP VLICRNEAEK
CLIETSINSL RISLKVKQAD ELENILTKKF LRFLSMRAEA FQVLRRKPVQ GYDISFLITN
YHCEEMQKQK LIDFIIQFME DIEKEIRDLK ESVNTRGRLV ATEFLKQFM
