PNSL1_ARATH
ID PNSL1_ARATH Reviewed; 238 AA.
AC O80634; A8MQY7; Q2V417; Q94BP9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Photosynthetic NDH subunit of lumenal location 1, chloroplastic {ECO:0000303|PubMed:21785130};
DE AltName: Full=PsbP-like protein 2;
DE Flags: Precursor;
GN Name=PNSL1 {ECO:0000303|PubMed:21785130}; Synonyms=PPL2;
GN OrderedLocusNames=At2g39470 {ECO:0000312|Araport:AT2G39470};
GN ORFNames=F12L6.13 {ECO:0000312|EMBL:AAC27838.2};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 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 [4]
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 [5]
RP FUNCTION, GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=17827269; DOI=10.1104/pp.107.105866;
RA Ishihara S., Takabayashi A., Ido K., Endo T., Ifuku K., Sato F.;
RT "Distinct functions for the two PsbP-like proteins PPL1 and PPL2 in the
RT chloroplast thylakoid lumen of Arabidopsis.";
RL Plant Physiol. 145:668-679(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP 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 [7]
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 [8]
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 [9]
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 accumulation of the chloroplast NAD(P)H dehydrogenase
CC (NDH) complex (PubMed:17827269). {ECO:0000269|PubMed:17827269,
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:21785130}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:18431481}; Peripheral membrane protein
CC {ECO:0000305}; Lumenal side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O80634-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O80634-2; Sequence=VSP_034346;
CC Name=3;
CC IsoId=O80634-3; Sequence=VSP_034346, VSP_034347, VSP_034348;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17827269}.
CC -!- SIMILARITY: Belongs to the psbP family. {ECO:0000305}.
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DR EMBL; AC004218; AAC27838.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09682.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09683.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09684.1; -; Genomic_DNA.
DR EMBL; AY039968; AAK64145.1; -; mRNA.
DR EMBL; AY133798; AAM91732.1; -; mRNA.
DR EMBL; AY085632; AAM62853.1; -; mRNA.
DR PIR; T00557; T00557.
DR RefSeq; NP_001031514.2; NM_001036437.3. [O80634-2]
DR RefSeq; NP_001078022.1; NM_001084553.1. [O80634-3]
DR RefSeq; NP_565906.1; NM_129505.4. [O80634-1]
DR PDB; 7WFF; EM; 3.59 A; f=1-238.
DR PDB; 7WG5; EM; 3.89 A; f=1-238.
DR PDBsum; 7WFF; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; O80634; -.
DR SMR; O80634; -.
DR BioGRID; 3870; 3.
DR STRING; 3702.AT2G39470.1; -.
DR TCDB; 3.D.1.8.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; O80634; -.
DR PRIDE; O80634; -.
DR ProteomicsDB; 226191; -. [O80634-1]
DR EnsemblPlants; AT2G39470.1; AT2G39470.1; AT2G39470. [O80634-1]
DR EnsemblPlants; AT2G39470.2; AT2G39470.2; AT2G39470. [O80634-2]
DR EnsemblPlants; AT2G39470.3; AT2G39470.3; AT2G39470. [O80634-3]
DR GeneID; 818532; -.
DR Gramene; AT2G39470.1; AT2G39470.1; AT2G39470. [O80634-1]
DR Gramene; AT2G39470.2; AT2G39470.2; AT2G39470. [O80634-2]
DR Gramene; AT2G39470.3; AT2G39470.3; AT2G39470. [O80634-3]
DR KEGG; ath:AT2G39470; -.
DR Araport; AT2G39470; -.
DR TAIR; locus:2039727; AT2G39470.
DR eggNOG; ENOG502QQHK; Eukaryota.
DR HOGENOM; CLU_039569_1_0_1; -.
DR InParanoid; O80634; -.
DR OMA; HNIITCS; -.
DR OrthoDB; 1480904at2759; -.
DR PhylomeDB; O80634; -.
DR PRO; PR:O80634; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80634; baseline and differential.
DR Genevisible; O80634; AT.
DR GO; GO:0009507; C:chloroplast; HDA: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:0009654; C:photosystem II oxygen evolving complex; IEA:InterPro.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:InterPro.
DR InterPro; IPR016123; Mog1/PsbP_a/b/a-sand.
DR InterPro; IPR002683; PsbP_C.
DR Pfam; PF01789; PsbP; 1.
DR SUPFAM; SSF55724; SSF55724; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Membrane; Plastid;
KW Reference proteome; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..80
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN 81..238
FT /note="Photosynthetic NDH subunit of lumenal location 1,
FT chloroplastic"
FT /id="PRO_0000341584"
FT VAR_SEQ 40..48
FT /note="GKADSSEST -> A (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034346"
FT VAR_SEQ 173..182
FT /note="RVEDGKNYYT -> GGRWKELLHV (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034347"
FT VAR_SEQ 183..238
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034348"
SQ SEQUENCE 238 AA; 26963 MW; AD7EE5672ECB568D CRC64;
MAVSSLSIRC GGFSPTISHK TEILCPNPSL KACCLLSSGG KADSSESTYQ KGSGNNWKRR
QALVGVGTLV ATSIPATLLL AEEIPKSYSP FVDREDGYSY YYPSDWREFD FRAHDSAFKD
RYLQLQNVRV RFIPTEKNDI HEVGPMEEVV YDLVKHKFAA PNQVATIYDM KERVEDGKNY
YTFEYGLRTP IYATTSFATV AVGNNRYYTL IVGANERRWR KVKKQLQVVA DSLKILQI
