PSAD1_ARATH
ID PSAD1_ARATH Reviewed; 208 AA.
AC Q9S7H1; Q8L9B6;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Photosystem I reaction center subunit II-1, chloroplastic;
DE AltName: Full=Photosystem I 20 kDa subunit 1;
DE Short=PSI-D1;
DE Flags: Precursor;
GN Name=psaD1; OrderedLocusNames=At4g02770; ORFNames=T5J8.7;
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 Legen J., Misera S., Herrmann R.G., Altschmied L.;
RT "Sequences and map position of 31 Arabidopsis thaliana cDNAs encoding
RT organellar polypeptides.";
RL Submitted (AUG-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 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 46-61, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PHOSPHORYLATION AT THR-48.
RC STRAIN=cv. Wassilewskija; TISSUE=Leaf;
RX PubMed=12883043; DOI=10.1074/mcp.m300050-mcp200;
RA Hansson M., Vener A.V.;
RT "Identification of three previously unknown in vivo protein phosphorylation
RT sites in thylakoid membranes of Arabidopsis thaliana.";
RL Mol. Cell. Proteomics 2:550-559(2003).
RN [7]
RP INTERACTION WITH PGRL1A AND PGRL1B.
RC STRAIN=cv. Columbia;
RX PubMed=18243102; DOI=10.1016/j.cell.2007.12.028;
RA DalCorso G., Pesaresi P., Masiero S., Aseeva E., Schuenemann D.,
RA Finazzi G., Joliot P., Barbato R., Leister D.;
RT "A complex containing PGRL1 and PGR5 is involved in the switch between
RT linear and cyclic electron flow in Arabidopsis.";
RL Cell 132:273-285(2008).
CC -!- FUNCTION: PsaD can form complexes with ferredoxin and ferredoxin-
CC oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode
CC the ferredoxin-docking protein.
CC -!- SUBUNIT: Interacts with PGRL1A and PGRL1B.
CC {ECO:0000269|PubMed:18243102}.
CC -!- INTERACTION:
CC Q9S7H1; Q17TI5: BRX; NbExp=3; IntAct=EBI-1805558, EBI-4426649;
CC Q9S7H1; O23160: MYB73; NbExp=3; IntAct=EBI-1805558, EBI-25506855;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC Peripheral membrane protein; Stromal side.
CC -!- INDUCTION: By light.
CC -!- PTM: Phosphorylated by a threonine specific thylakoid kinase in a light
CC activated and redox-dependent manner. {ECO:0000269|PubMed:12883043}.
CC -!- MISCELLANEOUS: After Mass spectrometry, it is not clear if Ala-45 or
CC Glu-46 is the N-terminus of the mature protein.
CC -!- SIMILARITY: Belongs to the PsaD family. {ECO:0000305}.
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DR EMBL; AJ245906; CAB52676.1; -; mRNA.
DR EMBL; AC004044; AAD15351.1; -; Genomic_DNA.
DR EMBL; AL161495; CAB77762.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82228.1; -; Genomic_DNA.
DR EMBL; AF324675; AAG40026.1; -; mRNA.
DR EMBL; AF326887; AAG41469.1; -; mRNA.
DR EMBL; AF389290; AAK63862.1; -; mRNA.
DR EMBL; AY062512; AAL32590.1; -; mRNA.
DR EMBL; AY081671; AAM10233.1; -; mRNA.
DR EMBL; AY102159; AAM26726.1; -; mRNA.
DR EMBL; AY113939; AAM44987.1; -; mRNA.
DR EMBL; AY088533; AAM66066.1; -; mRNA.
DR PIR; C85035; C85035.
DR RefSeq; NP_192186.1; NM_116511.4.
DR AlphaFoldDB; Q9S7H1; -.
DR SMR; Q9S7H1; -.
DR BioGRID; 13472; 29.
DR IntAct; Q9S7H1; 23.
DR MINT; Q9S7H1; -.
DR STRING; 3702.AT4G02770.1; -.
DR iPTMnet; Q9S7H1; -.
DR PaxDb; Q9S7H1; -.
DR PRIDE; Q9S7H1; -.
DR ProteomicsDB; 226320; -.
DR EnsemblPlants; AT4G02770.1; AT4G02770.1; AT4G02770.
DR GeneID; 828183; -.
DR Gramene; AT4G02770.1; AT4G02770.1; AT4G02770.
DR KEGG; ath:AT4G02770; -.
DR Araport; AT4G02770; -.
DR TAIR; locus:2140255; AT4G02770.
DR eggNOG; ENOG502QQIC; Eukaryota.
DR HOGENOM; CLU_087107_0_0_1; -.
DR InParanoid; Q9S7H1; -.
DR OMA; MAMATQP; -.
DR OrthoDB; 1477247at2759; -.
DR PhylomeDB; Q9S7H1; -.
DR BioCyc; ARA:AT4G02770-MON; -.
DR BioCyc; MetaCyc:MON-1098; -.
DR PRO; PR:Q9S7H1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S7H1; baseline and differential.
DR Genevisible; Q9S7H1; 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:0009538; C:photosystem I reaction center; IEA:InterPro.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0140547; P:acquisition of seed longevity; IMP:TAIR.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR InterPro; IPR003685; PsaD.
DR InterPro; IPR036579; PsaD_sf.
DR PANTHER; PTHR31982; PTHR31982; 1.
DR Pfam; PF02531; PsaD; 1.
DR SUPFAM; SSF64234; SSF64234; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Membrane; Phosphoprotein;
KW Photosynthesis; Photosystem I; Plastid; Reference proteome; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..208
FT /note="Photosystem I reaction center subunit II-1,
FT chloroplastic"
FT /id="PRO_0000029370"
FT REGION 49..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..149
FT /note="Ferredoxin and ferredoxin-oxidoreductase binding"
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12883043"
SQ SEQUENCE 208 AA; 22598 MW; 92F1667DDE0CB713 CRC64;
MATQAAGIFN SAITTAATSG VKKLHFFSTT HRPKSLSFTK TAIRAEKTDS SAAAAAAPAT
KEAPVGFTPP QLDPNTPSPI FAGSTGGLLR KAQVEEFYVI TWNSPKEQIF EMPTGGAAIM
REGPNLLKLA RKEQCLALGT RLRSKYKITY QFYRVFPNGE VQYLHPKDGV YPEKANPGRE
GVGLNMRSIG KNVSPIEVKF TGKQSYDL
