CLT3_ARATH
ID CLT3_ARATH Reviewed; 452 AA.
AC Q8RWL5; Q8LGC9; Q9FMP6; Q9FMP7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein CLT3, chloroplastic {ECO:0000303|PubMed:20080670};
DE AltName: Full=CRT-like transporter 3 {ECO:0000303|PubMed:20080670};
DE AltName: Full=Chloroquine-resistance transporter-like transporter 3 {ECO:0000303|PubMed:20080670};
DE Flags: Precursor;
GN Name=CLT3 {ECO:0000303|PubMed:20080670};
GN OrderedLocusNames=At5g12170 {ECO:0000312|Araport:AT5G12170};
GN ORFNames=MXC9.12 {ECO:0000312|EMBL:BAB10034.1},
GN MXC9.13 {ECO:0000312|EMBL:BAB10035.1};
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 {ECO:0000312|EMBL:AAM13018.1};
RN [1]
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 [2]
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 [3]
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 [4]
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=20080670; DOI=10.1073/pnas.0913689107;
RA Maughan S.C., Pasternak M., Cairns N., Kiddle G., Brach T., Jarvis R.,
RA Haas F., Nieuwland J., Lim B., Muller C., Salcedo-Sora E., Kruse C.,
RA Orsel M., Hell R., Miller A.J., Bray P., Foyer C.H., Murray J.A.,
RA Meyer A.J., Cobbett C.S.;
RT "Plant homologs of the Plasmodium falciparum chloroquine-resistance
RT transporter, PfCRT, are required for glutathione homeostasis and stress
RT responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2331-2336(2010).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=24204368; DOI=10.3389/fpls.2013.00416;
RA Schnaubelt D., Schulz P., Hannah M.A., Yocgo R.E., Foyer C.H.;
RT "A phenomics approach to the analysis of the influence of glutathione on
RT leaf area and abiotic stress tolerance in Arabidopsis thaliana.";
RL Front. Plant Sci. 4:416-416(2013).
CC -!- FUNCTION: Involved in thiol transport from the plastid to the cytosol.
CC Transports probably both glutathione (GSH) and its precursor, gamma-
CC glutamylcysteine (gamma-EC). Exhibits some functional redundancy with
CC CLT1 in maintaining the root GSH pool. {ECO:0000269|PubMed:20080670}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:20080670}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Clt1, clt3 and clt3 triple
CC mutants are more sensitive to Cd(2+), have a decreased level of
CC cytosolic GSH, an altered systemic acquired resistance response and are
CC more sensitive to Phytophthora infection (PubMed:20080670). Clt1, clt3
CC and clt3 triple mutants have decreased lateral root densities
CC (PubMed:24204368). {ECO:0000269|PubMed:20080670,
CC ECO:0000269|PubMed:24204368}.
CC -!- SIMILARITY: Belongs to the CRT-like transporter family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT71935.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305};
CC Sequence=AAU15152.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305};
CC Sequence=BAB10034.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB10035.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB007727; BAB10034.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB007727; BAB10035.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91770.1; -; Genomic_DNA.
DR EMBL; AY093019; AAM13018.1; -; mRNA.
DR EMBL; BT015063; AAT71935.1; ALT_SEQ; mRNA.
DR EMBL; BT015653; AAU15152.1; ALT_SEQ; mRNA.
DR EMBL; AY128939; AAM91339.1; -; mRNA.
DR EMBL; AK176437; BAD44200.1; -; mRNA.
DR EMBL; AY084340; AAM60923.1; -; mRNA.
DR RefSeq; NP_001078575.1; NM_001085106.2.
DR AlphaFoldDB; Q8RWL5; -.
DR SMR; Q8RWL5; -.
DR STRING; 3702.AT5G12170.2; -.
DR PaxDb; Q8RWL5; -.
DR PRIDE; Q8RWL5; -.
DR ProteomicsDB; 240986; -.
DR EnsemblPlants; AT5G12170.2; AT5G12170.2; AT5G12170.
DR GeneID; 831090; -.
DR Gramene; AT5G12170.2; AT5G12170.2; AT5G12170.
DR KEGG; ath:AT5G12170; -.
DR Araport; AT5G12170; -.
DR TAIR; locus:2177008; AT5G12170.
DR eggNOG; ENOG502QR5M; Eukaryota.
DR HOGENOM; CLU_038989_2_0_1; -.
DR InParanoid; Q8RWL5; -.
DR OMA; FTMPLPY; -.
DR OrthoDB; 630915at2759; -.
DR PhylomeDB; Q8RWL5; -.
DR PRO; PR:Q8RWL5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RWL5; baseline and differential.
DR Genevisible; Q8RWL5; AT.
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:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0002229; P:defense response to oomycetes; IGI:TAIR.
DR GO; GO:0034635; P:glutathione transport; IDA:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IMP:TAIR.
DR InterPro; IPR013936; CRT-like.
DR PANTHER; PTHR31326; PTHR31326; 1.
DR Pfam; PF08627; CRT-like; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Membrane; Plastid; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..452
FT /note="Protein CLT3, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433248"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 62
FT /note="G -> E (in Ref. 5; AAM60923)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="G -> S (in Ref. 5; AAM60923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 48469 MW; 7A43D2B73A791DC2 CRC64;
MATTSRRFTT GLFASITSVK SHSANRPQSI SLIRRNHIDH RLPLIVPSSR RWIIQAARSW
DGFDDGAEAE IKKPGAYGYA IGDNEIEGSS SSTVHVIDGE HVKTAEIVIW AAVTAAFGVG
NRVMYKLALV PLKEYPFFLA QLSTFGYVAV YYTILYFRYR AGTVTDAMLS VPKSPFLIVG
ILEALAAAAG MAAAANLSGP STTVLSQTFL VWQIFFSIIF LGRRYSVNQI LGCTLVALGV
IVSVASGSGA AHSLNEAGVL WILLMVLSFL LQGAGTVLKE VIFIDSQRRL KGASLDLFIV
NSYGSAFQAI CIALLLPFLS KLWGIPFNQL GTYLKDGAVC FLNNGTITKG CDGAPFLPLL
FVIMNIGYNI ALLRLLKISS AVVSCLASTV SVPIAVFLFT MPLPYLGVAS SLPKGFMGGT
IILVLGMILY SWTPHGANSS HTDSVIPSPP PT
