ORANG_ARATH
ID ORANG_ARATH Reviewed; 307 AA.
AC Q9FKF4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein ORANGE, chloroplastic {ECO:0000305};
DE Short=AtOR {ECO:0000303|PubMed:24267591};
DE AltName: Full=DnaJ-like cysteine-rich domain-containing protein OR {ECO:0000305};
DE Flags: Precursor;
GN Name=OR {ECO:0000303|Ref.1};
GN OrderedLocusNames=At5g61670 {ECO:0000312|Araport:AT5G61670};
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].
RC TISSUE=Leaf;
RA Zhu C., Capell T., Christou P.;
RT "Cloning and functional characterization of Arabidopsis thalian Or gene.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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].
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 FUNCTION.
RX PubMed=24267591; DOI=10.1111/tpj.12384;
RA Bai C., Rivera S.M., Medina V., Alves R., Vilaprinyo E., Sorribas A.,
RA Canela R., Capell T., Sandmann G., Christou P., Zhu C.;
RT "An in vitro system for the rapid functional characterization of genes
RT involved in carotenoid biosynthesis and accumulation.";
RL Plant J. 77:464-475(2014).
RN [7]
RP FUNCTION, INTERACTION WITH PSY1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-90.
RX PubMed=26224804; DOI=10.1104/pp.15.00971;
RA Yuan H., Owsiany K., Sheeja T.E., Zhou X., Rodriguez C., Li Y., Welsch R.,
RA Chayut N., Yang Y., Thannhauser T.W., Parthasarathy M.V., Xu Q., Deng X.,
RA Fei Z., Schaffer A., Katzir N., Burger J., Tadmor Y., Li L.;
RT "A single amino acid substitution in an ORANGE protein promotes carotenoid
RT overaccumulation in Arabidopsis.";
RL Plant Physiol. 169:421-431(2015).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=26634929; DOI=10.1007/s00709-015-0919-x;
RA Sun T.H., Zhou F., Liu C.J., Zhuang Z., Lu S.;
RT "The DnaJ-like zinc finger domain protein ORANGE localizes to the nucleus
RT in etiolated cotyledons of Arabidopsis thaliana.";
RL Protoplasma 253:1599-1604(2016).
RN [9]
RP FUNCTION, INTERACTION WITH PSY1, AND SUBCELLULAR LOCATION.
RX PubMed=25675505; DOI=10.1073/pnas.1420831112;
RA Zhou X., Welsch R., Yang Y., Alvarez D., Riediger M., Yuan H., Fish T.,
RA Liu J., Thannhauser T.W., Li L.;
RT "Arabidopsis OR proteins are the major posttranscriptional regulators of
RT phytoene synthase in controlling carotenoid biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:3558-3563(2015).
RN [10]
RP FUNCTION.
RX PubMed=25857664; DOI=10.1111/pbi.12373;
RA Bai C., Capell T., Berman J., Medina V., Sandmann G., Christou P., Zhu C.;
RT "Bottlenecks in carotenoid biosynthesis and accumulation in rice endosperm
RT are influenced by the precursor-product balance.";
RL Plant Biotechnol. J. 14:195-205(2016).
CC -!- FUNCTION: Involved in chromoplast differentiation. Associated with a
CC cellular process that triggers the differentiation of pro-plastids or
CC other non-colored plastids into chromoplasts for carotenoid
CC accumulation (PubMed:24267591). Is associated with carotenoid
CC accumulation in chromoplasts (PubMed:26224804). Functions as a major
CC regulator of the phytoene synthase PSY1 protein level and activity.
CC Modulates carotenoid biosynthesis by means of post-transcriptional
CC regulation of PSY1 (PubMed:25675505). Modulates carotenoid biosynthesis
CC in part by up-regulating a series of endogenous carotenogenic genes
CC (PubMed:25857664). {ECO:0000269|PubMed:24267591,
CC ECO:0000269|PubMed:25675505, ECO:0000269|PubMed:25857664,
CC ECO:0000269|PubMed:26224804}.
CC -!- SUBUNIT: Interacts with PSY1. {ECO:0000269|PubMed:26224804,
CC ECO:0000269|PubMed:26634929}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:25675505, ECO:0000269|PubMed:26224804,
CC ECO:0000305|PubMed:26634929}. Nucleus {ECO:0000269|PubMed:26634929}.
CC Note=Localizes in the nucleus in etiolated cotyledons.
CC {ECO:0000269|PubMed:26634929}.
CC -!- MISCELLANEOUS: Its sequence is related to the DnaJ family but lacks the
CC J domain. The CR-type-like region is similar to CR-type zinc-fingers.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the orange-like family.
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DR EMBL; JF304772; AEA35046.1; -; mRNA.
DR EMBL; AB012239; BAB09011.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97503.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97504.1; -; Genomic_DNA.
DR EMBL; AY065401; AAL38842.1; -; mRNA.
DR EMBL; AY094431; AAM19804.1; -; mRNA.
DR EMBL; AY117226; AAM51301.1; -; mRNA.
DR EMBL; AY149953; AAN31107.1; -; mRNA.
DR EMBL; AY084568; AAM61134.1; -; mRNA.
DR RefSeq; NP_200975.1; NM_125561.4.
DR RefSeq; NP_974975.1; NM_203246.3.
DR AlphaFoldDB; Q9FKF4; -.
DR STRING; 3702.AT5G61670.2; -.
DR PaxDb; Q9FKF4; -.
DR PRIDE; Q9FKF4; -.
DR ProteomicsDB; 248642; -.
DR EnsemblPlants; AT5G61670.1; AT5G61670.1; AT5G61670.
DR EnsemblPlants; AT5G61670.2; AT5G61670.2; AT5G61670.
DR GeneID; 836289; -.
DR Gramene; AT5G61670.1; AT5G61670.1; AT5G61670.
DR Gramene; AT5G61670.2; AT5G61670.2; AT5G61670.
DR KEGG; ath:AT5G61670; -.
DR Araport; AT5G61670; -.
DR TAIR; locus:2151556; AT5G61670.
DR eggNOG; ENOG502QVC3; Eukaryota.
DR HOGENOM; CLU_060054_0_0_1; -.
DR InParanoid; Q9FKF4; -.
DR OMA; NPAGFCI; -.
DR OrthoDB; 1130087at2759; -.
DR PhylomeDB; Q9FKF4; -.
DR PRO; PR:Q9FKF4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKF4; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:1904143; P:positive regulation of carotenoid biosynthetic process; IMP:TAIR.
DR GO; GO:0050821; P:protein stabilization; IMP:TAIR.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Nucleus; Plastid; Reference proteome; Repeat;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..307
FT /note="Protein ORANGE, chloroplastic"
FT /id="PRO_0000438012"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 230..237
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000305"
FT REPEAT 241..248
FT /note="CXXCXXXG motif"
FT /evidence="ECO:0000305"
FT REPEAT 274..281
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000305"
FT REPEAT 285..292
FT /note="CXXCXXXG motif"
FT /evidence="ECO:0000305"
FT REGION 208..299
FT /note="CR-type-like"
FT /evidence="ECO:0000305"
FT MUTAGEN 90
FT /note="R->F,K: No effect on the accumulation of
FT carotenoids."
FT /evidence="ECO:0000269|PubMed:26224804"
FT MUTAGEN 90
FT /note="R->H,A: Increased accumulation of carotenoids."
FT /evidence="ECO:0000269|PubMed:26224804"
SQ SEQUENCE 307 AA; 33790 MW; CE0C55CDC7CD80BA CRC64;
MSSLGRILSV SYPPDPYTWR FSQYKLSSSL GRNRRLRWRF TALDPESSSL DSESSADKFA
SGFCIIEGPE TVQDFAKMQL QEIQDNIRSR RNKIFLHMEE VRRLRIQQRI KNTELGIINE
EQEHELPNFP SFIPFLPPLT AANLKVYYAT CFSLIAGIIL FGGLLAPTLE LKLGIGGTSY
ADFIQSLHLP MQLSQVDPIV ASFSGGAVGV ISALMVVEVN NVKQQEHKRC KYCLGTGYLA
CARCSSTGAL VLTEPVSAIA GGNHSLSPPK TERCSNCSGA GKVMCPTCLC TGMAMASEHD
PRIDPFD
