PNSL4_ARATH
ID PNSL4_ARATH Reviewed; 217 AA.
AC Q9SCY3; O65658; Q941D9;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Photosynthetic NDH subunit of lumenal location 4, chloroplastic {ECO:0000303|PubMed:21785130};
DE AltName: Full=FK506-binding protein 16-2;
DE Short=AtFKBP16-2;
DE AltName: Full=Immunophilin FKBP16-2;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase FKBP16-2;
DE Short=PPIase FKBP16-2;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=PNSL4 {ECO:0000303|PubMed:21785130};
GN Synonyms=FKBP16-2, FKBP22-2, FKBP23I;
GN OrderedLocusNames=At4g39710 {ECO:0000312|Araport:AT4G39710};
GN ORFNames=T19P19.100 {ECO:0000312|EMBL:CAA18757.1};
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].
RC STRAIN=cv. Columbia;
RA Kolukisaoglu U., Billion K., Eckhoff A., Moeller A., Saal B., Wanke D.,
RA Schulz B.;
RT "Structure and evolution of FKBP-like genes in Arabidopsis.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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 SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11826309; DOI=10.1105/tpc.010304;
RA Peltier J.-B., Emanuelsson O., Kalume D.E., Ytterberg J., Friso G.,
RA Rudella A., Liberles D.A., Soederberg L., Roepstorff P., von Heijne G.,
RA van Wijk K.J.;
RT "Central functions of the lumenal and peripheral thylakoid proteome of
RT Arabidopsis determined by experimentation and genome-wide prediction.";
RL Plant Cell 14:211-236(2002).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15047905; DOI=10.1104/pp.103.031005;
RA He Z., Li L., Luan S.;
RT "Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in
RT Arabidopsis.";
RL Plant Physiol. 134:1248-1267(2004).
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 FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, DISRUPTION PHENOTYPE, AND
RP COMPONENT OF THE CHLOROPLAST NDH SUBCOMPLEX L.
RX PubMed=19903870; DOI=10.1105/tpc.109.068791;
RA Peng L., Fukao Y., Fujiwara M., Takami T., Shikanai T.;
RT "Efficient operation of NAD(P)H dehydrogenase requires supercomplex
RT formation with photosystem I via minor LHCI in Arabidopsis.";
RL Plant Cell 21:3623-3640(2009).
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 PPIases accelerate the folding of proteins. It catalyzes the cis-trans
CC isomerization of proline imidic peptide bonds in oligopeptides (By
CC similarity). Seems to be essential for stabilizing the NDH subcomplex A
CC (PubMed:19903870). {ECO:0000250, ECO:0000269|PubMed:19903870,
CC ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
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 -!- INTERACTION:
CC Q9SCY3; Q9ZR03: petC; NbExp=3; IntAct=EBI-2436954, EBI-2436968;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:11826309}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SCY3-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: RNAi mutant displays impaired NDH activity.
CC {ECO:0000269|PubMed:19903870}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK97696.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA18757.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80634.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ242481; CAB64721.1; -; mRNA.
DR EMBL; AL022605; CAA18757.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161595; CAB80634.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87107.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67449.1; -; Genomic_DNA.
DR EMBL; AY052226; AAK97696.1; ALT_SEQ; mRNA.
DR PIR; T05008; T05008.
DR RefSeq; NP_001329278.1; NM_001342549.1. [Q9SCY3-1]
DR RefSeq; NP_568067.1; NM_120132.4. [Q9SCY3-1]
DR PDB; 7WFF; EM; 3.59 A; i=1-217.
DR PDB; 7WG5; EM; 3.89 A; i=1-217.
DR PDBsum; 7WFF; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q9SCY3; -.
DR SMR; Q9SCY3; -.
DR BioGRID; 15406; 3.
DR IntAct; Q9SCY3; 2.
DR STRING; 3702.AT4G39710.1; -.
DR iPTMnet; Q9SCY3; -.
DR PaxDb; Q9SCY3; -.
DR PRIDE; Q9SCY3; -.
DR ProteomicsDB; 226158; -. [Q9SCY3-1]
DR EnsemblPlants; AT4G39710.1; AT4G39710.1; AT4G39710. [Q9SCY3-1]
DR EnsemblPlants; AT4G39710.3; AT4G39710.3; AT4G39710. [Q9SCY3-1]
DR GeneID; 830126; -.
DR Gramene; AT4G39710.1; AT4G39710.1; AT4G39710. [Q9SCY3-1]
DR Gramene; AT4G39710.3; AT4G39710.3; AT4G39710. [Q9SCY3-1]
DR KEGG; ath:AT4G39710; -.
DR Araport; AT4G39710; -.
DR TAIR; locus:2135287; AT4G39710.
DR eggNOG; KOG0549; Eukaryota.
DR HOGENOM; CLU_013615_10_3_1; -.
DR InParanoid; Q9SCY3; -.
DR OMA; LAVAPCN; -.
DR PhylomeDB; Q9SCY3; -.
DR PRO; PR:Q9SCY3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SCY3; baseline and differential.
DR Genevisible; Q9SCY3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044183; PNSL4-like.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR47833; PTHR47833; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Disulfide bond; Isomerase;
KW Plastid; Reference proteome; Rotamase; Thylakoid; Transit peptide;
KW Transport.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 35..?
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN ?..217
FT /note="Photosynthetic NDH subunit of lumenal location 4,
FT chloroplastic"
FT /id="PRO_0000045903"
FT DOMAIN 112..211
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DISULFID 87..99
FT /evidence="ECO:0000250"
FT DISULFID 188..193
FT /evidence="ECO:0000250"
SQ SEQUENCE 217 AA; 23260 MW; 1122EE1BAFD20E19 CRC64;
MAISTLTLTQ SLYTRSFRPT IFFSSSSSSS FSCLCSSSSD CEPKLSVKKR VFGVGLGFLA
SSILSLTPLD ADATRIDYYA TVGDPLCEYS YAKSGLGFCD LDVGFGDEAP RGVLVNIHYT
ARFADGTLFD SSYKRARPLT MRIGVGKVIR GLDQGILGGE GVPPMRVGGK RKLQIPPKLA
YGPEPAGCFS GDCNIPGNAT LLYDINFVEI YPGSNTR
