RPT3_ARATH
ID RPT3_ARATH Reviewed; 746 AA.
AC Q9FMF5; F4KDL6; F4KDL7; Q0WSP1; Q9SPB4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Root phototropism protein 3;
DE AltName: Full=BTB/POZ domain-containing protein RPT3;
DE AltName: Full=Non-phototropic hypocotyl protein 3;
GN Name=RPT3; Synonyms=JK218, NPH3; OrderedLocusNames=At5g64330;
GN ORFNames=MSJ1.17;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH PHOT1, PHOSPHORYLATION AT TYR-546, AND MUTAGENESIS OF
RP TYR-546.
RC STRAIN=cv. Columbia;
RX PubMed=10542152; DOI=10.1126/science.286.5441.961;
RA Motchoulski A., Liscum E.;
RT "Arabidopsis NPH3: a NPH1 photoreceptor-interacting protein essential for
RT phototropism.";
RL Science 286:961-964(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION.
RX PubMed=11537679; DOI=10.1073/pnas.89.10.4718;
RA Reymond P., Short T.W., Briggs W.R., Poff K.L.;
RT "Light-induced phosphorylation of a membrane protein plays an early role in
RT signal transduction for phototropism in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4718-4721(1992).
RN [6]
RP FUNCTION.
RX PubMed=10662859; DOI=10.2307/3870924;
RA Sakai T., Wada T., Ishiguro S., Okada K.;
RT "RPT2: a signal transducer of the phototropic response in Arabidopsis.";
RL Plant Cell 12:225-236(2000).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH RPT2.
RX PubMed=15031408; DOI=10.1105/tpc.019901;
RA Inada S., Ohgishi M., Mayama T., Okada K., Sakai T.;
RT "RPT2 is a signal transducer involved in phototropic response and stomatal
RT opening by association with phototropin 1 in Arabidopsis thaliana.";
RL Plant Cell 16:887-896(2004).
RN [8]
RP DOMAIN BTB.
RX PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA Vierstra R.D.;
RT "Cullins 3a and 3b assemble with members of the broad
RT complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL J. Biol. Chem. 280:18810-18821(2005).
RN [9]
RP INDUCTION.
RX PubMed=16908503; DOI=10.1093/jxb/erl086;
RA Molas M.L., Kiss J.Z., Correll M.J.;
RT "Gene profiling of the red light signalling pathways in roots.";
RL J. Exp. Bot. 57:3217-3229(2006).
RN [10]
RP FUNCTION, INTERACTION WITH PKS1 AND PHOT1, AND SUBCELLULAR LOCATION.
RX PubMed=16777956; DOI=10.1073/pnas.0603799103;
RA Lariguet P., Schepens I., Hodgson D., Pedmale U.V., Trevisan M., Kami C.,
RA de Carbonnel M., Alonso J.M., Ecker J.R., Liscum E., Fankhauser C.;
RT "PHYTOCHROME KINASE SUBSTRATE 1 is a phototropin 1 binding protein required
RT for phototropism.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10134-10139(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [13]
RP FUNCTION, INTERACTION WITH PKS1; PKS2; PHOT1 AND PHOT2, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20071603; DOI=10.1104/pp.109.150441;
RA de Carbonnel M., Davis P., Roelfsema M.R., Inoue S., Schepens I.,
RA Lariguet P., Geisler M., Shimazaki K., Hangarter R., Fankhauser C.;
RT "The Arabidopsis PHYTOCHROME KINASE SUBSTRATE2 protein is a phototropin
RT signaling element that regulates leaf flattening and leaf positioning.";
RL Plant Physiol. 152:1391-1405(2010).
RN [14]
RP FUNCTION, AND INTERACTION WITH CAR6 AND PHOT1.
RX PubMed=21367967; DOI=10.1104/pp.110.167411;
RA Knauer T., Duemmer M., Landgraf F., Forreiter C.;
RT "A negative effector of blue light-induced and gravitropic bending in
RT Arabidopsis.";
RL Plant Physiol. 156:439-447(2011).
CC -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). Signal transducer of the phototropic response
CC and photo-induced movements. Involved in the phot1 pathway under low
CC blue light (LBL) fluence rate and in the phot2 pathway under higher
CC fluence rate of blue light (HBL). Necessary for root and hypocotyl
CC phototropisms, but not for the regulation of stomata opening. Not
CC involved in chloroplast accumulation and translocation. {ECO:0000250,
CC ECO:0000269|PubMed:10542152, ECO:0000269|PubMed:10662859,
CC ECO:0000269|PubMed:15031408, ECO:0000269|PubMed:16777956,
CC ECO:0000269|PubMed:20071603}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with PKS1, PKS2, RPT2, PHOT1 and PHOT2
CC (PubMed:10542152, PubMed:15031408, PubMed:16777956, PubMed:20071603).
CC Subunit of a complex made of CAR6, PHOT1 and RPT3/NPH3
CC (PubMed:21367967). {ECO:0000269|PubMed:10542152,
CC ECO:0000269|PubMed:15031408, ECO:0000269|PubMed:16777956,
CC ECO:0000269|PubMed:20071603}.
CC -!- INTERACTION:
CC Q9FMF5; O48963: PHOT1; NbExp=3; IntAct=EBI-1553842, EBI-1553849;
CC Q9FMF5; Q9SWI1: PKS1; NbExp=2; IntAct=EBI-1553842, EBI-626200;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10542152,
CC ECO:0000269|PubMed:16777956}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10542152, ECO:0000269|PubMed:16777956}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FMF5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FMF5-2; Sequence=VSP_041384, VSP_041385;
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls, guard cells and mesophyll
CC cells. {ECO:0000269|PubMed:15031408}.
CC -!- INDUCTION: In the root, up-regulated by red light.
CC {ECO:0000269|PubMed:16908503}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- PTM: Phosphorylated in the dark. {ECO:0000305|PubMed:10542152,
CC ECO:0000305|PubMed:11537679}.
CC -!- DISRUPTION PHENOTYPE: Impaired leaf flattening and slight epinasty when
CC grown under blue light. {ECO:0000269|PubMed:20071603}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NPH3 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00982}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09864.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF180390; AAF05914.1; -; mRNA.
DR EMBL; AB008268; BAB09864.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97870.1; -; Genomic_DNA.
DR EMBL; AK227884; BAE99857.1; -; mRNA.
DR RefSeq; NP_568989.1; NM_125829.4. [Q9FMF5-1]
DR AlphaFoldDB; Q9FMF5; -.
DR BioGRID; 21796; 5.
DR DIP; DIP-61198N; -.
DR IntAct; Q9FMF5; 2.
DR STRING; 3702.AT5G64330.1; -.
DR iPTMnet; Q9FMF5; -.
DR PaxDb; Q9FMF5; -.
DR PRIDE; Q9FMF5; -.
DR ProteomicsDB; 228224; -. [Q9FMF5-1]
DR EnsemblPlants; AT5G64330.1; AT5G64330.1; AT5G64330. [Q9FMF5-1]
DR GeneID; 836554; -.
DR Gramene; AT5G64330.1; AT5G64330.1; AT5G64330. [Q9FMF5-1]
DR KEGG; ath:AT5G64330; -.
DR Araport; AT5G64330; -.
DR TAIR; locus:2173418; AT5G64330.
DR eggNOG; ENOG502QR3H; Eukaryota.
DR HOGENOM; CLU_005994_6_2_1; -.
DR InParanoid; Q9FMF5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FMF5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMF5; baseline and differential.
DR Genevisible; Q9FMF5; AT.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009785; P:blue light signaling pathway; IPI:TAIR.
DR GO; GO:0009638; P:phototropism; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IMP:TAIR.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR029959; NPH3-like.
DR InterPro; IPR043454; NPH3/RPT2-like.
DR InterPro; IPR027356; NPH3_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR32370; PTHR32370; 1.
DR PANTHER; PTHR32370:SF153; PTHR32370:SF153; 1.
DR Pfam; PF03000; NPH3; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS51649; NPH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Transducer; Ubl conjugation pathway.
FT CHAIN 1..746
FT /note="Root phototropism protein 3"
FT /id="PRO_0000097439"
FT DOMAIN 54..122
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 250..605
FT /note="NPH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00982"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 546
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10542152"
FT VAR_SEQ 555..558
FT /note="AHPT -> VYIY (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_041384"
FT VAR_SEQ 559..746
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_041385"
FT MUTAGEN 546
FT /note="Missing: In nph3-2; loss of hypocotyl phototropism."
FT /evidence="ECO:0000269|PubMed:10542152"
FT CONFLICT 519
FT /note="D -> V (in Ref. 4; BAE99857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 746 AA; 81873 MW; 7D91D4224A5F3549 CRC64;
MMWESESDGG VGVGGGGGRE YGDGVLSSNK HGGVKTDGFE LRGQSWFVAT DIPSDLLVKI
GDMNFHLHKY PLLSRSGKMN RLIYESRDPD PTILILDDLP GGPEAFELAS KFCYGVPVDL
TATNISGLRC AAEYLEMTED LEEGNLIFKT EAFLSYVVLS SWRDSILVLK SCEKLSPWAE
NLQIVRRCSE SIAWKACSNP KGIRWAYTGK APSPSTTNFA GSSPRWNESK DSSFYCSPSR
NTNSQPVPPD WWFEDVSILR IDHFVRVITA IKVKGMRFEL LGAVIMHYAG KWLPGLIKEG
GVAIAPAMSS AIGGGLGLGG DEMSISCGSN SSGGSSGPDW KGGLHMVLSA GKTNGHQDSV
ACLAGLGISP KDQRMIVESL ISIIPPQKDS VTCSFLLRLL RAANMLKVAP ALITELEKRV
GMQFEQATLQ DLLIPGYNNK GETMYDVDLV QRLLEHFLVQ EQTEGSSPSR MSPSPSQSMY
ADIPRGNNNN GGGGGGNNQN AKMRVARLVD SYLTEVARDR NLPLTKFQVL AEALPESART
CDDGLYRAID SYLKAHPTLS EHERKRLCRV MDCQKLSMDA CMHAAQNERL PLRVVVQVLF
SEQVKISNAL ANTSLKESTT LGEAMGTYQP MIPNRKTLIE ATPQSFQEGW AAAKKDINTL
KFELETVKTK YVELQNEMEV MQRQFEKTGK VKNTPSSSAW TSGWKKLSKL TKMSGQESHD
ISSGGEQAGV DHPPPRKPRR WRNSIS
