CLT2_ARATH
ID CLT2_ARATH Reviewed; 431 AA.
AC A1L4X0; Q84TI1; Q9STU9;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Protein CLT2, chloroplastic {ECO:0000303|PubMed:20080670};
DE AltName: Full=CRT-like transporter 2 {ECO:0000303|PubMed:20080670};
DE AltName: Full=Chloroquine-resistance transporter-like transporter 2 {ECO:0000303|PubMed:20080670};
DE Flags: Precursor;
GN Name=CLT2 {ECO:0000303|PubMed:20080670};
GN OrderedLocusNames=At4g24460 {ECO:0000312|Araport:AT4G24460};
GN ORFNames=T22A6.290 {ECO:0000312|EMBL:CAB45081.1};
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:ABM06027.1};
RN [1]
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 [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] (ISOFORM 2).
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] (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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) 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). {ECO:0000269|PubMed:20080670}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:20080670}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A1L4X0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A1L4X0-2; Sequence=VSP_057694, VSP_057695;
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=CAB45081.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79356.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL078637; CAB45081.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161561; CAB79356.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84907.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84908.1; -; Genomic_DNA.
DR EMBL; BT005771; AAO64175.1; -; mRNA.
DR EMBL; AK228633; BAF00542.1; -; mRNA.
DR EMBL; BT029757; ABM06027.1; -; mRNA.
DR PIR; T09909; T09909.
DR RefSeq; NP_001190820.1; NM_001203891.1. [A1L4X0-1]
DR RefSeq; NP_194177.2; NM_118579.4. [A1L4X0-1]
DR AlphaFoldDB; A1L4X0; -.
DR SMR; A1L4X0; -.
DR IntAct; A1L4X0; 10.
DR STRING; 3702.AT4G24460.1; -.
DR PaxDb; A1L4X0; -.
DR PRIDE; A1L4X0; -.
DR ProteomicsDB; 240985; -. [A1L4X0-1]
DR EnsemblPlants; AT4G24460.1; AT4G24460.1; AT4G24460. [A1L4X0-1]
DR EnsemblPlants; AT4G24460.2; AT4G24460.2; AT4G24460. [A1L4X0-1]
DR GeneID; 828548; -.
DR Gramene; AT4G24460.1; AT4G24460.1; AT4G24460. [A1L4X0-1]
DR Gramene; AT4G24460.2; AT4G24460.2; AT4G24460. [A1L4X0-1]
DR KEGG; ath:AT4G24460; -.
DR Araport; AT4G24460; -.
DR TAIR; locus:2136032; AT4G24460.
DR eggNOG; ENOG502QR5M; Eukaryota.
DR HOGENOM; CLU_038989_1_0_1; -.
DR InParanoid; A1L4X0; -.
DR OMA; IWPALMI; -.
DR OrthoDB; 630915at2759; -.
DR PhylomeDB; A1L4X0; -.
DR PRO; PR:A1L4X0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; A1L4X0; baseline and differential.
DR Genevisible; A1L4X0; AT.
DR GO; GO:0009507; C:chloroplast; HDA: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: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 Alternative splicing; Chloroplast; Membrane; Plastid; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 80..431
FT /note="Protein CLT2, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433247"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 233..266
FT /note="SGSGADTTLSGIGFLWPAVLVASAAFQAGASIIK -> RYYAIWNRFLMACC
FT IGSIRCFSSWCIYHKGICFQ (in isoform 2)"
FT /id="VSP_057694"
FT VAR_SEQ 267..431
FT /note="Missing (in isoform 2)"
FT /id="VSP_057695"
SQ SEQUENCE 431 AA; 46685 MW; 8C7B4CDA744AB4DC CRC64;
MDTVLMATTP PIRCLHASIP TVFRSPAIYQ VSCRSSQLFS YRSTTMMSMC FLRRSDLRSR
FLSTPKTTSP MRRPRFSVGA STEESSIPSN RNLIVANSVV IVALAVANRV LYKLALVPMK
QYPFFMAQLT TFGYVLIYFT ILYTRRRLGI VTNEMMDVPK WRFAIIGFLE ALGVATGMAA
AAMLPGPVIP ILNQTYLVWQ LLFALLILGR RFLLNQIAGC LLVAVGVVVA VSSGSGADTT
LSGIGFLWPA VLVASAAFQA GASIIKEFVF NDAAKRLEGK SLDIFVVNSF GSGFQALFVF
LLLPFLSNLK GIPFASLPSY LKDGAGCFFN TGAKISGCDG APILPLLYIS TNLAFNISLL
HLVKISSAIV SSLTMMLSVP LAVYIMSKPL PYLPGGSSLS SNFTMGCIVL VLGLLLYNIP
TTPTKQHTKT S
