RPT2_ARATH
ID RPT2_ARATH Reviewed; 593 AA.
AC Q682S0; O04343; O04344; Q0WKX4; Q93VA6; Q9M6N8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Root phototropism protein 2;
DE AltName: Full=BTB/POZ domain-containing protein RPT2;
GN Name=RPT2; OrderedLocusNames=At2g30520/At2g30510;
GN ORFNames=T6B20.13/T6B20.14;
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], FUNCTION, AND INDUCTION.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 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].
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH PHOT1 AND RPT3.
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 [7]
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 [8]
RP INDUCTION, AND FUNCTION.
RX PubMed=20202166; DOI=10.1111/j.1365-313x.2010.04180.x;
RA Tsuchida-Mayama T., Sakai T., Hanada A., Uehara Y., Asami T., Yamaguchi S.;
RT "Role of the phytochrome and cryptochrome signaling pathways in hypocotyl
RT phototropism.";
RL Plant J. 62:653-662(2010).
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. Necessary for root phototropism. Involved
CC in hypocotyl phototropism under high rate but not under low rate light.
CC Regulates stomata opening. Seems to be not involved in chloroplast
CC accumulation and translocation. {ECO:0000250,
CC ECO:0000269|PubMed:10662859, ECO:0000269|PubMed:15031408,
CC ECO:0000269|PubMed:20202166}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RPT3 and PHOT1. {ECO:0000269|PubMed:15031408}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q682S0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in hypocotyls, guard cells and mesophyll
CC cells. {ECO:0000269|PubMed:15031408}.
CC -!- INDUCTION: Light fluence rate-dependent induction, independent of light
CC quality. Up-regulated by blue light treatment.
CC {ECO:0000269|PubMed:10662859, ECO:0000269|PubMed:20202166}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- SIMILARITY: Belongs to the NPH3 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00982}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63085.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g30510 and At2g30520.; Evidence={ECO:0000305};
CC Sequence=AAB63086.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g30510 and At2g30520.; Evidence={ECO:0000305};
CC Sequence=BAD43060.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF181683; AAF33112.1; -; mRNA.
DR EMBL; U93215; AAB63085.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U93215; AAB63086.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08401.1; -; Genomic_DNA.
DR EMBL; AY035063; AAK59568.1; -; mRNA.
DR EMBL; AY056359; AAL07245.1; -; mRNA.
DR EMBL; BT000675; AAN31821.1; -; mRNA.
DR EMBL; AK175297; BAD43060.1; ALT_SEQ; mRNA.
DR EMBL; AK221310; BAD94074.1; -; mRNA.
DR EMBL; AK221993; BAD94572.1; -; mRNA.
DR EMBL; AK222218; BAD95385.1; -; mRNA.
DR EMBL; AK229759; BAF01595.1; -; mRNA.
DR EMBL; AK229844; BAF01673.1; -; mRNA.
DR EMBL; AK230435; BAF02233.1; -; mRNA.
DR PIR; C84709; C84709.
DR PIR; D84709; D84709.
DR RefSeq; NP_001031446.1; NM_001036369.2.
DR RefSeq; NP_001077982.1; NM_001084513.2.
DR RefSeq; NP_850147.1; NM_179816.3. [Q682S0-1]
DR AlphaFoldDB; Q682S0; -.
DR SMR; Q682S0; -.
DR BioGRID; 2950; 6.
DR IntAct; Q682S0; 3.
DR MINT; Q682S0; -.
DR STRING; 3702.AT2G30520.1; -.
DR iPTMnet; Q682S0; -.
DR MetOSite; Q682S0; -.
DR PaxDb; Q682S0; -.
DR PRIDE; Q682S0; -.
DR ProteomicsDB; 226743; -. [Q682S0-1]
DR EnsemblPlants; AT2G30520.1; AT2G30520.1; AT2G30520. [Q682S0-1]
DR GeneID; 817601; -.
DR Gramene; AT2G30520.1; AT2G30520.1; AT2G30520. [Q682S0-1]
DR KEGG; ath:AT2G30520; -.
DR Araport; AT2G30520; -.
DR TAIR; locus:2064357; AT2G30520.
DR eggNOG; ENOG502QUJB; Eukaryota.
DR HOGENOM; CLU_005994_6_0_1; -.
DR InParanoid; Q682S0; -.
DR OMA; GPETFEK; -.
DR OrthoDB; 298243at2759; -.
DR PhylomeDB; Q682S0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q682S0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q682S0; baseline and differential.
DR Genevisible; Q682S0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009904; P:chloroplast accumulation movement; IMP:TAIR.
DR GO; GO:0009638; P:phototropism; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR043454; NPH3/RPT2-like.
DR InterPro; IPR027356; NPH3_dom.
DR InterPro; IPR029958; RPT2.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR32370; PTHR32370; 1.
DR PANTHER; PTHR32370:SF157; PTHR32370:SF157; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF03000; NPH3; 1.
DR SMART; SM00225; BTB; 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; Phosphoprotein; Reference proteome; Transducer;
KW Ubl conjugation pathway.
FT CHAIN 1..593
FT /note="Root phototropism protein 2"
FT /id="PRO_0000097438"
FT DOMAIN 32..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 187..469
FT /note="NPH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00982"
FT MOD_RES 410
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMF5"
FT CONFLICT 244
FT /note="Y -> F (in Ref. 1; AAF33112)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="K -> R (in Ref. 1; AAF33112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 65854 MW; DDB208FD15FF1FB0 CRC64;
MATEGKNPIN MNSMSSSLAR TGQWVFSQDI PTDVVVEVGE ANFSLHKFML VAKSNYIRKL
IMESKDSDVT RINLSDIPGG PEIFEKAAKF CYGVNFEITV QNVAALHCAA EFLQMTDKYC
DNNLAGRTQD FLSQVALSSL SGAIVVLKSC EILLPISRDL GIVRRCVDVV GAKACNEAMF
PCRTPPNWWT EELCILDVDF FSDVVSSMKQ RGVKPSSLAS AIITYTEKSL RDLVRDHSGR
GVKYSDPGDN ESDERSQQRD LVQSIVSLLP SDKGLFPVNF LCSLLRCAVF LDTSLTCKNE
LEKRISVVLE HVSVDDLLIP SFTYDGERLL DLDSVRRIIS AFVEKEKNVG VFNGGDFNRG
VCSVSLQRVA KTVDSYLAEI ATYGDLTISK FNAIANLVPK SARKSDDDLY RAIDIFLKAH
PNLDEIEREK VCSSMDPLKL SYDARLHASQ NKRLPVNIVL HALYYDQLKL RSGVAEQEER
AVVVLPEALK TRSQLQADTT LAKENEALRS ELMKMKMYVS DMQKNKNGAG ASSSNSSSLV
SSKKSKHTFF SSVSKKLGKL NPFKNGSKDT SHIDEDLGGV DITKPRRRRF SIS
