MET1_ARATH
ID MET1_ARATH Reviewed; 335 AA.
AC Q94BS2; Q8L972; Q9ZVU6;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Protein MET1, chloroplastic {ECO:0000303|PubMed:25587003};
DE AltName: Full=PDZ domain, K-box domain, and TPR region containing protein {ECO:0000303|PubMed:15914918};
DE Flags: Precursor;
GN Name=MET1 {ECO:0000303|PubMed:25587003};
GN Synonyms=GAN {ECO:0000303|Ref.2}, ZKT {ECO:0000303|PubMed:15914918};
GN OrderedLocusNames=At1g55480 {ECO:0000312|Araport:AT1G55480};
GN ORFNames=T5A14.12 {ECO:0000312|EMBL:AAD10648.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], REPRESSION BY WOUNDING, PHOSPHORYLATION AFTER
RP WOUNDING, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15914918; DOI=10.1271/bbb.69.972;
RA Ishikawa A., Tanaka H., Kato C., Iwasaki Y., Asahi T.;
RT "Molecular characterization of the ZKT gene encoding a protein with PDZ, K-
RT Box, and TPR motifs in Arabidopsis.";
RL Biosci. Biotechnol. Biochem. 69:972-978(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen H., Huang R., Xiong L.;
RT "GAN, a novel determinant of drought and salt tolerance in Arabidopsis.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION BY LIGHT,
RP SUBUNIT, AND INTERACTION WITH PSBB AND PSBC.
RC STRAIN=cv. Columbia;
RX PubMed=25587003; DOI=10.1105/tpc.114.132787;
RA Bhuiyan N.H., Friso G., Poliakov A., Ponnala L., van Wijk K.J.;
RT "MET1 is a thylakoid-associated TPR protein involved in photosystem II
RT supercomplex formation and repair in Arabidopsis.";
RL Plant Cell 27:262-285(2015).
CC -!- FUNCTION: Involved in photosystem II supercomplex formation and repair,
CC probably acting as a psbB/psbC chaperone on the stromal side of the
CC membrane. {ECO:0000269|PubMed:25587003}.
CC -!- SUBUNIT: Interacts directly with stromal loops of photosystem II (PSII)
CC core components psbB (CP47) and psbC (CP43). Associates with PSII
CC subcomplexes formed during the PSII repair cycle (e.g. PSII dimers,
CC PSII monomers, CP43-less PSII monomerand PSII reaction centers).
CC {ECO:0000269|PubMed:25587003}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:25587003}. Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:25587003}; Peripheral membrane protein
CC {ECO:0000269|PubMed:25587003}; Stromal side
CC {ECO:0000269|PubMed:25587003}. Note=In thylakoids, enriched in stroma
CC lamellae, and also present in grana. {ECO:0000269|PubMed:25587003}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves (at protein level)
CC (PubMed:15914918). Mostly expressed in leaves, stems and siliques, and,
CC to a lower extent, in flowers and senescent leaves, but not present in
CC roots (at protein level) (PubMed:25587003).
CC {ECO:0000269|PubMed:15914918, ECO:0000269|PubMed:25587003}.
CC -!- INDUCTION: Repressed by wounding at the transcript level, but not at
CC the protein level (PubMed:15914918). Strong level decrease during
CC senescence. Low levels observed in etiolated leaves and accumulates
CC rapidly during light-induced greening (PubMed:25587003).
CC {ECO:0000269|PubMed:15914918, ECO:0000269|PubMed:25587003}.
CC -!- PTM: Phosophorylated rapidly (e.g. within 5 minutes) but transiently at
CC threonine and serine residues after wounding.
CC {ECO:0000269|PubMed:15914918}.
CC -!- DISRUPTION PHENOTYPE: Conditional reduced growth in fluctuating white
CC light intensities conditions, with near complete blockage in
CC photosystem II (PSII) supercomplex formation, and concomitant increase
CC of unassembled psbC (CP43), thus leading to reduced PSII efficiency and
CC biomass accumulation. Increased sensitivity to high light conditions,
CC associated with the loss of PSII supercomplexes and accelerated D1
CC degradation. {ECO:0000269|PubMed:25587003}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10648.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB190499; BAD99102.1; -; mRNA.
DR EMBL; AY986818; AAY42135.1; -; mRNA.
DR EMBL; AC005223; AAD10648.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33250.1; -; Genomic_DNA.
DR EMBL; AY039926; AAK64030.1; -; mRNA.
DR EMBL; AY079359; AAL85090.1; -; mRNA.
DR EMBL; AY088606; AAM66135.1; -; mRNA.
DR PIR; A96597; A96597.
DR RefSeq; NP_564691.1; NM_104423.4.
DR AlphaFoldDB; Q94BS2; -.
DR SMR; Q94BS2; -.
DR STRING; 3702.AT1G55480.1; -.
DR iPTMnet; Q94BS2; -.
DR PaxDb; Q94BS2; -.
DR PRIDE; Q94BS2; -.
DR ProteomicsDB; 232285; -.
DR EnsemblPlants; AT1G55480.1; AT1G55480.1; AT1G55480.
DR GeneID; 841995; -.
DR Gramene; AT1G55480.1; AT1G55480.1; AT1G55480.
DR KEGG; ath:AT1G55480; -.
DR Araport; AT1G55480; -.
DR TAIR; locus:2193844; AT1G55480.
DR eggNOG; ENOG502QQQU; Eukaryota.
DR HOGENOM; CLU_053421_2_0_1; -.
DR InParanoid; Q94BS2; -.
DR OMA; FGDEIWP; -.
DR OrthoDB; 1019390at2759; -.
DR PhylomeDB; Q94BS2; -.
DR PRO; PR:Q94BS2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94BS2; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0009575; C:chromoplast stroma; IDA:TAIR.
DR GO; GO:0035448; C:extrinsic component of thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR GO; GO:0015979; P:photosynthesis; IMP:TAIR.
DR GO; GO:0010207; P:photosystem II assembly; IDA:UniProtKB.
DR GO; GO:0010206; P:photosystem II repair; IDA:UniProtKB.
DR GO; GO:0009644; P:response to high light intensity; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Chaperone; Chloroplast; Membrane; Photosynthesis; Photosystem II; Plastid;
KW Reference proteome; Repeat; Thylakoid; TPR repeat; Transit peptide.
FT TRANSIT 1..73
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 74..335
FT /note="Protein MET1, chloroplastic"
FT /id="PRO_0000440118"
FT DOMAIN 97..136
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REPEAT 217..250
FT /note="TPR 1"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REPEAT 254..287
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 289..323
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 161
FT /note="G -> C (in Ref. 6; AAM66135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 37410 MW; E83B3BF8EEB39E51 CRC64;
MSLAPSSYPS LYSSPSLPRT QQTKQNPSLI TQSSFISAKS LFLSSNSASL CNTHVAKRRN
LALKASETES SAKAEAGGDG EEEEKYETYE IEVEQPYGLK FRKGRDGGTY IDAILPGGSA
DKTGKFTVGD RVIATSAVFG TEIWPAAEYG RTMYTIRQRI GPLLMQMEKR NGKAEDTGEL
TEKEIIRAER NAGYISSRLR EIQMQNYLKK KEQKAQREKD LREGLQFSKN GKYEEALERF
ESVLGSKPTP EEASVASYNV ACCYSKLNQV QAGLSALEEA LKSGYEDFKR IRSDPDLETL
RKSKDFDPLL KQFDESFINE SAINAIKSLF GFNKK
