ATPD_ARATH
ID ATPD_ARATH Reviewed; 234 AA.
AC Q9SSS9; Q8RY87;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ATP synthase subunit delta, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE Flags: Precursor;
GN Name=ATPD {ECO:0000255|HAMAP-Rule:MF_01416};
GN OrderedLocusNames=At4g09650 {ECO:0000312|Araport:AT4G09650};
GN ORFNames=T25P22.90 {ECO:0000312|EMBL:CAB82132.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
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 [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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=12970486; DOI=10.1104/pp.103.024190;
RA Maiwald D., Dietzmann A., Jahns P., Pesaresi P., Joliot P., Joliot A.,
RA Levin J.Z., Salamini F., Leister D.;
RT "Knock-out of the genes coding for the Rieske protein and the ATP-synthase
RT delta-subunit of Arabidopsis. Effects on photosynthesis, thylakoid protein
RT composition, and nuclear chloroplast gene expression.";
RL Plant Physiol. 133:191-202(2003).
RN [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17103225; DOI=10.1007/s00425-006-0416-8;
RA Mahler H., Wuennenberg P., Linder M., Przybyla D., Zoerb C., Landgraf F.,
RA Forreiter C.;
RT "Singlet oxygen affects the activity of the thylakoid ATP synthase and has
RT a strong impact on its gamma subunit.";
RL Planta 225:1073-1083(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-48, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER MET-47, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation (Potential).
CC Essential for photosynthesis, probably by facilitating electron
CC transport in both photosystems I and II (PubMed:12970486).
CC {ECO:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:12970486}.
CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CF(1).
CC It either transmits conformational changes from CF(0) to CF(1) or is
CC implicated in proton conduction. {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main
CC subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC form an alternating ring which encloses part of the gamma chain. F(1)
CC is attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta, b and b'
CC chains. {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- INTERACTION:
CC Q9SSS9; O23160: MYB73; NbExp=3; IntAct=EBI-25516560, EBI-25506855;
CC Q9SSS9; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-25516560, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01416, ECO:0000269|PubMed:17103225};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01416,
CC ECO:0000269|PubMed:17103225}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethal. High-chlorophyll (Chl)-
CC fluorescence phenotype associated with an increase in non-photochemical
CC quenching of Chl fluorescence and a higher de-epoxidation state of
CC xanthophyll cycle pigments under low light. Impaired electron flow in
CC photosystems I and II. {ECO:0000269|PubMed:12970486}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL69493.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL161515; CAB78088.1; -; Genomic_DNA.
DR EMBL; AL161831; CAB82132.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82777.1; -; Genomic_DNA.
DR EMBL; AY065158; AAL38334.1; -; mRNA.
DR EMBL; AY074525; AAL69493.1; ALT_INIT; mRNA.
DR EMBL; AY114577; AAM47896.1; -; mRNA.
DR EMBL; AY123002; AAM67535.1; -; mRNA.
DR EMBL; AY087900; AAM65451.1; -; mRNA.
DR PIR; G85098; G85098.
DR RefSeq; NP_192703.1; NM_117033.3.
DR AlphaFoldDB; Q9SSS9; -.
DR SMR; Q9SSS9; -.
DR IntAct; Q9SSS9; 2.
DR STRING; 3702.AT4G09650.1; -.
DR iPTMnet; Q9SSS9; -.
DR MetOSite; Q9SSS9; -.
DR PaxDb; Q9SSS9; -.
DR PRIDE; Q9SSS9; -.
DR ProteomicsDB; 241003; -.
DR EnsemblPlants; AT4G09650.1; AT4G09650.1; AT4G09650.
DR GeneID; 826551; -.
DR Gramene; AT4G09650.1; AT4G09650.1; AT4G09650.
DR KEGG; ath:AT4G09650; -.
DR Araport; AT4G09650; -.
DR TAIR; locus:2136922; AT4G09650.
DR eggNOG; KOG1662; Eukaryota.
DR HOGENOM; CLU_085114_1_0_1; -.
DR InParanoid; Q9SSS9; -.
DR OMA; QVIVAHE; -.
DR OrthoDB; 1432799at2759; -.
DR PhylomeDB; Q9SSS9; -.
DR BioCyc; ARA:AT4G09650-MON; -.
DR PRO; PR:Q9SSS9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SSS9; baseline and differential.
DR Genevisible; Q9SSS9; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IMP:TAIR.
DR GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IMP:TAIR.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IMP:TAIR.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR Gene3D; 1.10.520.20; -; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR020781; ATPase_OSCP/d_CS.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; SSF47928; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR PROSITE; PS00389; ATPASE_DELTA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; CF(1); Chloroplast; Glycoprotein;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Photosynthesis; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transport.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 48..234
FT /note="ATP synthase subunit delta, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432101"
FT MOD_RES 48
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 234 AA; 25669 MW; 78473309D02727DC CRC64;
MASLQQTLFS LQSKLPPSSF QIARSLPLRK TFPIRINNGG NAAGARMSAT AASSYAMALA
DVAKRNDTME LTVTDIEKLE QVFSDPQVLN FFANPTITVE KKRQVIDDIV KSSSLQSHTS
NFLNVLVDAN RINIVTEIVK EFELVYNKLT DTQLAEVRSV VKLEAPQLAQ IAKQVQKLTG
AKNVRVKTVI DASLVAGFTI RYGESGSKLI DMSVKKQLED IASQLELGEI QLAT
