PNSL3_ARATH
ID PNSL3_ARATH Reviewed; 220 AA.
AC Q9SGH4; Q8LEW8;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Photosynthetic NDH subunit of lumenal location 3, chloroplastic {ECO:0000303|PubMed:21785130};
DE AltName: Full=PsbQ-like protein 2;
DE Flags: Precursor;
GN Name=PNSL3 {ECO:0000303|PubMed:21785130}; Synonyms=PQL1, PQL2;
GN OrderedLocusNames=At3g01440 {ECO:0000312|Araport:AT3G01440};
GN ORFNames=T13O15.8 {ECO:0000312|EMBL:AAF24614.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=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].
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 [5]
RP PROTEIN SEQUENCE OF 126-146, 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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 -!- 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; AC010870; AAF24614.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73667.1; -; Genomic_DNA.
DR EMBL; AY070745; AAL50085.1; -; mRNA.
DR EMBL; AY093737; AAM10361.1; -; mRNA.
DR EMBL; AY085184; AAM61735.1; -; mRNA.
DR RefSeq; NP_566137.1; NM_111010.3.
DR PDB; 7WFF; EM; 3.59 A; h=1-220.
DR PDB; 7WG5; EM; 3.89 A; h=1-220.
DR PDBsum; 7WFF; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q9SGH4; -.
DR SMR; Q9SGH4; -.
DR BioGRID; 6476; 5.
DR IntAct; Q9SGH4; 3.
DR STRING; 3702.AT3G01440.1; -.
DR TCDB; 3.D.1.8.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; Q9SGH4; -.
DR PRIDE; Q9SGH4; -.
DR ProteomicsDB; 234790; -.
DR EnsemblPlants; AT3G01440.1; AT3G01440.1; AT3G01440.
DR GeneID; 821143; -.
DR Gramene; AT3G01440.1; AT3G01440.1; AT3G01440.
DR KEGG; ath:AT3G01440; -.
DR Araport; AT3G01440; -.
DR TAIR; locus:2096707; AT3G01440.
DR eggNOG; ENOG502QVCH; Eukaryota.
DR HOGENOM; CLU_104804_0_0_1; -.
DR InParanoid; Q9SGH4; -.
DR OMA; KGMYIAN; -.
DR OrthoDB; 1392734at2759; -.
DR PhylomeDB; Q9SGH4; -.
DR PRO; PR:Q9SGH4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SGH4; baseline and differential.
DR Genevisible; Q9SGH4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; 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; TAS:TAIR.
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:0019684; P:photosynthesis, light reaction; TAS: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; Chloroplast; Direct protein sequencing; Membrane; Plastid;
KW Reference proteome; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 36..77
FT /note="Thylakoid"
FT /evidence="ECO:0000250"
FT CHAIN 78..220
FT /note="Photosynthetic NDH subunit of lumenal location 3,
FT chloroplastic"
FT /id="PRO_0000419236"
FT CONFLICT 181
FT /note="R -> K (in Ref. 4; AAM61735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 220 AA; 24781 MW; 21E96DCEB962CB42 CRC64;
MAHFIDLNSL TNTLPSLPKL PESRKTGKSS GFACRRTEEF QEPDSVQITR RMTLGFAVSI
GLTGILGENN VSLAQDNGFW IDGPLPIPPI YNNIVNEKTG TRTFIKKGVY VADIGTKGRM
YRVKKNAFDL LAMEDLIGPD TLNYVKKYLR LKSTFLFYDF DNLISAAASE DKQPLTDLAN
RLFDNFEKLE DAAKTKNLAE TESCYKDTKF LLQEVMTRMA
