PNSL2_ARATH
ID PNSL2_ARATH Reviewed; 190 AA.
AC Q9XI73; Q0WN14; Q3EDD0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Photosynthetic NDH subunit of lumenal location 2, chloroplastic {ECO:0000303|PubMed:21785130};
DE AltName: Full=PsbQ-like protein 1;
DE Flags: Precursor;
GN Name=PNSL2 {ECO:0000303|PubMed:21785130}; Synonyms=PQL1, PQL2;
GN OrderedLocusNames=At1g14150 {ECO:0000312|Araport:AT1G14150};
GN ORFNames=F7A19.23 {ECO:0000312|EMBL:AAD39297.1};
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] (ISOFORM 1).
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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] (ISOFORM 1).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-190 (ISOFORM 1).
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 [7]
RP PROTEIN SEQUENCE OF 79-92, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [8]
RP REVIEW.
RX PubMed=19995722; DOI=10.1093/mp/ssp052;
RA Suorsa M., Sirpioe S., Aro E.M.;
RT "Towards characterization of the chloroplast NAD(P)H dehydrogenase
RT complex.";
RL Mol. Plant 2:1127-1140(2009).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, NOMENCLATURE, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=20430763; DOI=10.1093/pcp/pcq060;
RA Yabuta S., Ifuku K., Takabayashi A., Ishihara S., Ido K., Ishikawa N.,
RA Endo T., Sato F.;
RT "Three PsbQ-like proteins are required for the function of the chloroplast
RT NAD(P)H dehydrogenase complex in Arabidopsis.";
RL Plant Cell Physiol. 51:866-876(2010).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=20460499; DOI=10.1093/pcp/pcq070;
RA Suorsa M., Sirpioe S., Paakkarinen V., Kumari N., Holmstroem M., Aro E.-M.;
RT "Two proteins homologous to PsbQ are novel subunits of the chloroplast
RT NAD(P)H dehydrogenase.";
RL Plant Cell Physiol. 51:877-883(2010).
RN [11]
RP REVIEW.
RX PubMed=21029720; DOI=10.1016/j.bbabio.2010.10.015;
RA Peng L., Yamamoto H., Shikanai T.;
RT "Structure and biogenesis of the chloroplast NAD(P)H dehydrogenase
RT complex.";
RL Biochim. Biophys. Acta 1807:945-953(2011).
RN [12]
RP NOMENCLATURE, AND COMPONENT OF THE NDH COMPLEX.
RX PubMed=21785130; DOI=10.1093/pcp/pcr098;
RA Ifuku K., Endo T., Shikanai T., Aro E.M.;
RT "Structure of the chloroplast NADH dehydrogenase-like complex: nomenclature
RT for nuclear-encoded subunits.";
RL Plant Cell Physiol. 52:1560-1568(2011).
CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN
CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain
CC and possibly in a chloroplast respiratory chain. The immediate electron
CC acceptor for the enzyme in this species is believed to be
CC plastoquinone. Couples the redox reaction to proton translocation, and
CC thus conserves the redox energy in a proton gradient (Probable).
CC Required for both formation and activity of the chloroplast NAD(P)H
CC dehydrogenase (NDH) complex (PubMed:20430763, PubMed:20460499).
CC {ECO:0000269|PubMed:20430763, ECO:0000269|PubMed:20460499,
CC ECO:0000305}.
CC -!- SUBUNIT: Part of the chloroplast NDH complex, composed of a mixture of
CC chloroplast and nucleus encoded subunits. Component of the NDH lumenal
CC subcomplex, at least composed of PnsL1, PnsL2, PnsL3, PnsL4 and PnsL5.
CC {ECO:0000269|PubMed:20430763, ECO:0000269|PubMed:20460499,
CC ECO:0000269|PubMed:21785130}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20460499}; Peripheral
CC membrane protein {ECO:0000269|PubMed:18431481,
CC ECO:0000269|PubMed:20460499}; Lumenal side
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20460499}.
CC Note=Associated with the chloroplast NAD(P)H dehydrogenase/photosystem
CC I (NDH/PSI) supercomplex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XI73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XI73-2; Sequence=VSP_044136, VSP_044137;
CC -!- DISRUPTION PHENOTYPE: Impaired chloroplastic NAD(P)H dehydrogenase
CC (NDH) activity leading to the loss of post-illumination increases in
CC Chl fluorescence, probably due to a reduced stability of the NDH
CC complex. {ECO:0000269|PubMed:20430763, ECO:0000269|PubMed:20460499}.
CC -!- SIMILARITY: Belongs to the psbQ family. {ECO:0000305}.
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DR EMBL; AF083742; AAN60300.1; -; mRNA.
DR EMBL; AC007576; AAD39297.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29111.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29112.1; -; Genomic_DNA.
DR EMBL; AF370579; AAK49585.1; -; mRNA.
DR EMBL; AY088325; AAM65864.1; -; mRNA.
DR EMBL; AK229642; BAF01486.1; -; mRNA.
DR PIR; A86275; A86275.
DR RefSeq; NP_563937.1; NM_101280.3. [Q9XI73-1]
DR RefSeq; NP_973820.1; NM_202091.2. [Q9XI73-2]
DR PDB; 7WFF; EM; 3.59 A; g=1-190.
DR PDB; 7WG5; EM; 3.89 A; g=1-190.
DR PDBsum; 7WFF; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q9XI73; -.
DR SMR; Q9XI73; -.
DR BioGRID; 23214; 2.
DR STRING; 3702.AT1G14150.1; -.
DR TCDB; 3.D.1.8.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; Q9XI73; -.
DR PRIDE; Q9XI73; -.
DR ProteomicsDB; 234691; -. [Q9XI73-1]
DR EnsemblPlants; AT1G14150.1; AT1G14150.1; AT1G14150. [Q9XI73-1]
DR EnsemblPlants; AT1G14150.2; AT1G14150.2; AT1G14150. [Q9XI73-2]
DR GeneID; 837974; -.
DR Gramene; AT1G14150.1; AT1G14150.1; AT1G14150. [Q9XI73-1]
DR Gramene; AT1G14150.2; AT1G14150.2; AT1G14150. [Q9XI73-2]
DR KEGG; ath:AT1G14150; -.
DR Araport; AT1G14150; -.
DR TAIR; locus:2035775; AT1G14150.
DR eggNOG; ENOG502RXRQ; Eukaryota.
DR HOGENOM; CLU_081110_1_0_1; -.
DR InParanoid; Q9XI73; -.
DR OMA; KYVKTAN; -.
DR PhylomeDB; Q9XI73; -.
DR BioCyc; ARA:AT1G14150-MON; -.
DR PRO; PR:Q9XI73; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XI73; baseline and differential.
DR Genevisible; Q9XI73; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; TAS:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:InterPro.
DR GO; GO:0009344; C:nitrite reductase complex [NAD(P)H]; IMP:TAIR.
DR GO; GO:0009654; C:photosystem II oxygen evolving complex; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IMP:TAIR.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IMP:TAIR.
DR Gene3D; 1.20.120.290; -; 1.
DR InterPro; IPR023222; PsbQ-like_dom_sf.
DR InterPro; IPR008797; PSII_PsbQ.
DR PANTHER; PTHR33399; PTHR33399; 1.
DR Pfam; PF05757; PsbQ; 1.
DR SUPFAM; SSF101112; SSF101112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Coiled coil;
KW Direct protein sequencing; Membrane; Plastid; Reference proteome;
KW Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 32..68
FT /note="Thylakoid"
FT /evidence="ECO:0000250"
FT CHAIN 69..190
FT /note="Photosynthetic NDH subunit of lumenal location 2,
FT chloroplastic"
FT /id="PRO_0000419235"
FT COILED 87..107
FT /evidence="ECO:0000255"
FT COILED 139..159
FT /evidence="ECO:0000255"
FT VAR_SEQ 159..162
FT /note="LDFY -> VYVI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044136"
FT VAR_SEQ 163..190
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044137"
SQ SEQUENCE 190 AA; 22157 MW; 00050C5A816D1B06 CRC64;
MSSFTTTNTP PPYLLRKIYH RRVNQPFSVV CCTGEPQQDI FTRRRTLTSL ITFTVIGGAT
SSALAQEKWG TRSFIKEKYF MPGLSPEDAA ARIKQTAEGL RDMREMLDHM SWRYVIFYIR
LKQAYLSQDL TNAMNILPES RRNDYVQAAN ELVENMSELD FYVRTPKVYE SYLYYEKTLK
SIDNVVEFLA
