LQY1_ARATH
ID LQY1_ARATH Reviewed; 154 AA.
AC Q8GSJ6; Q9LR08;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein disulfide-isomerase LQY1, chloroplastic {ECO:0000303|PubMed:21586683};
DE EC=5.3.4.1;
DE AltName: Full=Protein LOW QUANTUM YIELD OF PHOTOSYSTEM II 1 {ECO:0000303|PubMed:21586683};
DE Flags: Precursor;
GN Name=LQY1 {ECO:0000303|PubMed:21586683};
GN OrderedLocusNames=At1g75690 {ECO:0000312|Araport:AT1G75690};
GN ORFNames=F10A5.12, F10A5.4 {ECO:0000312|EMBL:AAF87111.1};
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 [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 [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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DISRUPTION PHENOTYPE, INDUCTION BY
RP LIGHT, AND INTERACTION WITH PHOTOSYSTEM II.
RC STRAIN=cv. Columbia;
RX PubMed=21586683; DOI=10.1105/tpc.111.085456;
RA Lu Y., Hall D.A., Last R.L.;
RT "A small zinc finger thylakoid protein plays a role in maintenance of
RT photosystem II in Arabidopsis thaliana.";
RL Plant Cell 23:1861-1875(2011).
RN [6]
RP INTERACTION WITH HHL1, AND FUNCTION.
RX PubMed=24632535; DOI=10.1105/tpc.113.122424;
RA Jin H., Liu B., Luo L., Feng D., Wang P., Liu J., Da Q., He Y., Qi K.,
RA Wang J., Wang H.B.;
RT "HYPERSENSITIVE TO HIGH LIGHT1 interacts with LOW QUANTUM YIELD OF
RT PHOTOSYSTEM II1 and functions in protection of photosystem II from
RT photodamage in Arabidopsis.";
RL Plant Cell 26:1213-1229(2014).
CC -!- FUNCTION: Protein disulfide-isomerase probably involved upon formation
CC of a complex with HHL1 in maintaining photosystem II (PSII) activity
CC under high light by regulating repair and reassembly of PSII complexes.
CC {ECO:0000269|PubMed:21586683, ECO:0000269|PubMed:24632535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000269|PubMed:21586683};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21586683};
CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000269|PubMed:21586683};
CC -!- SUBUNIT: Interacts with the photosystem II core subunits
CC (PubMed:21586683). Interacts with HHL1 (PubMed:24632535).
CC {ECO:0000269|PubMed:21586683, ECO:0000269|PubMed:24632535}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-
CC pass membrane protein. Note=More abundant in stroma-exposed thylakoids.
CC -!- INDUCTION: Not induced by high-light treatment.
CC {ECO:0000269|PubMed:21586683}.
CC -!- DOMAIN: Its sequence is related to the DnaJ family but lacks the J
CC domain. The CR-type-like region is similar to CR-type zinc-fingers and
CC was shown to bind zinc (PubMed:21586683).
CC {ECO:0000305|PubMed:21586683}.
CC -!- DISRUPTION PHENOTYPE: Lower maximum photochemical efficiency of
CC photosystem II after high-light treatment.
CC {ECO:0000269|PubMed:21586683}.
CC -!- SIMILARITY: Belongs to the BSD2 chaperone family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87111.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006434; AAF87111.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35746.1; -; Genomic_DNA.
DR EMBL; BT002378; AAO00738.1; -; mRNA.
DR EMBL; BT006547; AAP21355.1; -; mRNA.
DR EMBL; AK117868; BAC42509.1; -; mRNA.
DR RefSeq; NP_177698.1; NM_106220.4.
DR AlphaFoldDB; Q8GSJ6; -.
DR BioGRID; 29122; 2.
DR IntAct; Q8GSJ6; 1.
DR STRING; 3702.AT1G75690.1; -.
DR PaxDb; Q8GSJ6; -.
DR PRIDE; Q8GSJ6; -.
DR ProteomicsDB; 238799; -.
DR EnsemblPlants; AT1G75690.1; AT1G75690.1; AT1G75690.
DR GeneID; 843903; -.
DR Gramene; AT1G75690.1; AT1G75690.1; AT1G75690.
DR KEGG; ath:AT1G75690; -.
DR Araport; AT1G75690; -.
DR TAIR; locus:2005585; AT1G75690.
DR eggNOG; ENOG502RY5W; Eukaryota.
DR HOGENOM; CLU_118793_0_0_1; -.
DR InParanoid; Q8GSJ6; -.
DR OMA; RENSQPC; -.
DR OrthoDB; 1437451at2759; -.
DR PhylomeDB; Q8GSJ6; -.
DR PRO; PR:Q8GSJ6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GSJ6; baseline and differential.
DR Genevisible; Q8GSJ6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:TAIR.
DR GO; GO:0010206; P:photosystem II repair; IMP:TAIR.
DR InterPro; IPR035272; DUF5351.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR Pfam; PF17302; DUF5351; 1.
DR SUPFAM; SSF57938; SSF57938; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Isomerase; Membrane; Metal-binding; Plastid;
KW Reference proteome; Repeat; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..154
FT /note="Protein disulfide-isomerase LQY1, chloroplastic"
FT /id="PRO_0000415338"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 77..147
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9SN73"
SQ SEQUENCE 154 AA; 16334 MW; 100EE0F0B7324E63 CRC64;
MPVSAPSPPR LHSPFIHCPI NFTPSSFSAR NLRSPSTSYP RIKAELDPNT VVAISVGVAS
VALGIGIPVF YETQIDNAAK RENTQPCFPC NGTGAQKCRL CVGSGNVTVE LGGGEKEVSN
CINCDGAGSL TCTTCQGSGV QPRYLDRREF KDDD
