PNSL5_ARATH
ID PNSL5_ARATH Reviewed; 259 AA.
AC Q9ASS6; F4K2G0; Q53YK9; Q8L9L5; Q9FY98;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Photosynthetic NDH subunit of lumenal location 5, chloroplastic {ECO:0000303|PubMed:21785130};
DE AltName: Full=Cyclophilin of 20 kDa 2 {ECO:0000303|PubMed:15047905, ECO:0000303|PubMed:15051864, ECO:0000303|PubMed:15084723};
DE Short=AtCYP20-2 {ECO:0000303|PubMed:15047905, ECO:0000303|PubMed:15051864, ECO:0000303|PubMed:15084723};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase CYP20-2 {ECO:0000303|PubMed:16765949};
DE Short=PPIase CYP20-2 {ECO:0000303|PubMed:16765949, ECO:0000303|PubMed:23897924};
DE EC=5.2.1.8 {ECO:0000269|PubMed:16765949, ECO:0000269|PubMed:23897924};
DE AltName: Full=Rotamase CYP20-2 {ECO:0000303|PubMed:23897924};
DE AltName: Full=Thylakoid lumen PPIase of 20 kDa {ECO:0000303|PubMed:19995722};
DE Short=TLP20 {ECO:0000303|PubMed:19995722};
DE Short=TLP21 {ECO:0000303|PubMed:19995722};
DE Flags: Precursor;
GN Name=PNSL5 {ECO:0000303|PubMed:21785130};
GN Synonyms=CYP20-2 {ECO:0000303|PubMed:15047905, ECO:0000303|PubMed:15051864,
GN ECO:0000303|PubMed:15084723, ECO:0000303|PubMed:23897924};
GN OrderedLocusNames=At5g13120 {ECO:0000312|Araport:AT5G13120};
GN ORFNames=T19L5_80 {ECO:0000312|EMBL:CAC05440.1};
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], TISSUE SPECIFICITY, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=15051864; DOI=10.1104/pp.103.022160;
RA Romano P.G.N., Horton P., Gray J.E.;
RT "The Arabidopsis cyclophilin gene family.";
RL Plant Physiol. 134:1268-1282(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
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].
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 PROTEIN SEQUENCE OF 77-88, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [7]
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 [8]
RP GENE FAMILY, NOMENCLATURE, AND INDUCTION.
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=15084723; DOI=10.1104/pp.104.041186;
RA Romano P.G.N., Edvardsson A., Ruban A.V., Andersson B., Vener A.V.,
RA Gray J.E., Horton P.;
RT "Arabidopsis AtCYP20-2 is a light-regulated cyclophilin-type peptidyl-
RT prolyl cis-trans isomerase associated with the photosynthetic membranes.";
RL Plant Physiol. 134:1244-1247(2004).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16765949; DOI=10.1016/j.febslet.2006.05.054;
RA Shapiguzov A., Edvardsson A., Vener A.V.;
RT "Profound redox sensitivity of peptidyl-prolyl isomerase activity in
RT Arabidopsis thylakoid lumen.";
RL FEBS Lett. 580:3671-3676(2006).
RN [11]
RP INTERACTION WITH AHK2.
RX PubMed=18642946; DOI=10.1021/pr0703831;
RA Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT "Toward an interaction map of the two-component signaling pathway of
RT Arabidopsis thaliana.";
RL J. Proteome Res. 7:3649-3660(2008).
RN [12]
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 [13]
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 [14]
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).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH BZR1.
RX PubMed=23897924; DOI=10.1105/tpc.113.110296;
RA Zhang Y., Li B., Xu Y., Li H., Li S., Zhang D., Mao Z., Guo S., Yang C.,
RA Weng Y., Chong K.;
RT "The cyclophilin CYP20-2 modulates the conformation of BRASSINAZOLE-
RT RESISTANT1, which binds the promoter of FLOWERING LOCUS D to regulate
RT flowering in Arabidopsis.";
RL Plant Cell 25:2504-2521(2013).
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.
CC Responsible, with FKBP13, for all PPIase activity observed in thylakoid
CC lumen. Modulates the conformation of BZR1, which regulates flowering
CC (PubMed:16765949, PubMed:23897924). {ECO:0000269|PubMed:16765949,
CC ECO:0000269|PubMed:23897924, 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; Evidence={ECO:0000269|PubMed:16765949,
CC ECO:0000269|PubMed:23897924};
CC -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC {ECO:0000250|UniProtKB:P62937}.
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 (PubMed:21785130). Interacts with AHK2 and BZR1 (PubMed:18642946,
CC PubMed:23897924). {ECO:0000269|PubMed:18642946,
CC ECO:0000269|PubMed:21785130, ECO:0000269|PubMed:23897924}.
CC -!- INTERACTION:
CC Q9ASS6; Q9C5U2: AHK2; NbExp=2; IntAct=EBI-1807485, EBI-1100634;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:11826309, ECO:0000269|PubMed:15084723}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11719511,
CC ECO:0000269|PubMed:15084723}; Lumenal side
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:15084723}.
CC Note=Peripherally associated with PSII complexes (PubMed:15084723).
CC {ECO:0000269|PubMed:15084723}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ASS6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ASS6-2; Sequence=VSP_055387;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15051864}.
CC -!- INDUCTION: Down-regulated by pathogen. Up-regulated by light.
CC {ECO:0000269|PubMed:15047905}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05440.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY568517; AAS75300.1; -; mRNA.
DR EMBL; AL391711; CAC05440.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91852.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91853.1; -; Genomic_DNA.
DR EMBL; AF367307; AAK32894.1; -; mRNA.
DR EMBL; AY059152; AAL15377.1; -; mRNA.
DR EMBL; AY088365; AAM65904.1; -; mRNA.
DR RefSeq; NP_001190299.1; NM_001203370.1. [Q9ASS6-2]
DR RefSeq; NP_196816.1; NM_121315.3. [Q9ASS6-1]
DR PDB; 7WFF; EM; 3.59 A; j=1-259.
DR PDB; 7WG5; EM; 3.89 A; j=1-259.
DR PDBsum; 7WFF; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q9ASS6; -.
DR SMR; Q9ASS6; -.
DR BioGRID; 16429; 4.
DR IntAct; Q9ASS6; 2.
DR STRING; 3702.AT5G13120.1; -.
DR TCDB; 3.D.1.8.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; Q9ASS6; -.
DR PRIDE; Q9ASS6; -.
DR ProteomicsDB; 234791; -. [Q9ASS6-1]
DR EnsemblPlants; AT5G13120.1; AT5G13120.1; AT5G13120. [Q9ASS6-1]
DR EnsemblPlants; AT5G13120.2; AT5G13120.2; AT5G13120. [Q9ASS6-2]
DR GeneID; 831151; -.
DR Gramene; AT5G13120.1; AT5G13120.1; AT5G13120. [Q9ASS6-1]
DR Gramene; AT5G13120.2; AT5G13120.2; AT5G13120. [Q9ASS6-2]
DR KEGG; ath:AT5G13120; -.
DR Araport; AT5G13120; -.
DR TAIR; locus:2179822; AT5G13120.
DR eggNOG; KOG0880; Eukaryota.
DR InParanoid; Q9ASS6; -.
DR OMA; HPGDRPK; -.
DR PhylomeDB; Q9ASS6; -.
DR PRO; PR:Q9ASS6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ASS6; baseline and differential.
DR Genevisible; Q9ASS6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009533; C:chloroplast stromal thylakoid; IDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IMP:TAIR.
DR GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR GO; GO:0010275; P:NAD(P)H dehydrogenase complex assembly; IMP:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chaperone; Chloroplast;
KW Direct protein sequencing; Disulfide bond; Isomerase; Membrane; Plastid;
KW Reference proteome; Rotamase; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..76
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 77..259
FT /note="Photosynthetic NDH subunit of lumenal location 5,
FT chloroplastic"
FT /id="PRO_0000025503"
FT DOMAIN 96..253
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 204..251
FT /evidence="ECO:0000250|UniProtKB:P34791"
FT VAR_SEQ 9..12
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055387"
FT CONFLICT 29
FT /note="F -> L (in Ref. 5; AAM65904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 28306 MW; 7EDD221E80708BE2 CRC64;
MATLSMTLSN PKSLSAPPRR LSPINTSAFT STSFRLRTKS SFDSISFSSS TPFSASSLLL
HTSYTKRNHR CFSVQSNAEV VTEPQSKITH KVYFDISVGN PVGKLAGRIV IGLYGDDVPQ
TVENFRALCT GEKGFGYKGS TFHRVIRDFM IQGGDFEKGN GTGGKSVYGR TFKDENFKLS
HVGPGVLSMA NAGPNTNGSQ FFICTIKTSW LDGRHVVFGQ VIEGMEVVKL IEEQETDRGD
RPRKKVVIAD CGQLPMSEA
