PSAE1_ARATH
ID PSAE1_ARATH Reviewed; 143 AA.
AC Q9S831;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Photosystem I reaction center subunit IV A, chloroplastic;
DE Short=PSI-E A;
DE Flags: Precursor;
GN Name=PSAE1; OrderedLocusNames=At4g28750; ORFNames=F16A16.140;
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).
CC -!- FUNCTION: Stabilizes the interaction between PsaC and the PSI core,
CC assists the docking of the ferredoxin to PSI and interacts with
CC ferredoxin-NADP oxidoreductase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- PTM: 2 isoforms may exist. With or without the N-terminal alanine (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PsaE family. {ECO:0000305}.
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DR EMBL; AJ245908; CAB52678.1; -; mRNA.
DR EMBL; AL035353; CAA22977.1; -; Genomic_DNA.
DR EMBL; AL161573; CAB81463.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85537.1; -; Genomic_DNA.
DR EMBL; AY042790; AAK68730.1; -; mRNA.
DR EMBL; AY081687; AAM10249.1; -; mRNA.
DR PIR; T04524; T04524.
DR RefSeq; NP_567818.2; NM_119019.4.
DR PDB; 2O01; X-ray; 3.40 A; E=81-142.
DR PDB; 2WSC; X-ray; 3.30 A; E=1-143.
DR PDB; 2WSE; X-ray; 3.49 A; E=1-143.
DR PDB; 2WSF; X-ray; 3.48 A; E=1-143.
DR PDB; 7WFD; EM; 3.25 A; AE=1-143.
DR PDB; 7WFE; EM; 3.25 A; BE=1-143.
DR PDB; 7WG5; EM; 3.89 A; AE/BE=1-143.
DR PDBsum; 2O01; -.
DR PDBsum; 2WSC; -.
DR PDBsum; 2WSE; -.
DR PDBsum; 2WSF; -.
DR PDBsum; 7WFD; -.
DR PDBsum; 7WFE; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q9S831; -.
DR SMR; Q9S831; -.
DR BioGRID; 14283; 6.
DR STRING; 3702.AT4G28750.1; -.
DR iPTMnet; Q9S831; -.
DR PaxDb; Q9S831; -.
DR PRIDE; Q9S831; -.
DR ProteomicsDB; 226306; -.
DR EnsemblPlants; AT4G28750.1; AT4G28750.1; AT4G28750.
DR GeneID; 828996; -.
DR Gramene; AT4G28750.1; AT4G28750.1; AT4G28750.
DR KEGG; ath:AT4G28750; -.
DR Araport; AT4G28750; -.
DR TAIR; locus:2117818; AT4G28750.
DR eggNOG; ENOG502S9HV; Eukaryota.
DR HOGENOM; CLU_136462_0_0_1; -.
DR InParanoid; Q9S831; -.
DR OMA; MATCNIA; -.
DR OrthoDB; 1593036at2759; -.
DR PhylomeDB; Q9S831; -.
DR EvolutionaryTrace; Q9S831; -.
DR PRO; PR:Q9S831; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S831; baseline and differential.
DR Genevisible; Q9S831; 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:0009538; C:photosystem I reaction center; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR InterPro; IPR008990; Elect_transpt_acc-like_dom_sf.
DR InterPro; IPR003375; PSI_PsaE.
DR PANTHER; PTHR34549; PTHR34549; 1.
DR Pfam; PF02427; PSI_PsaE; 1.
DR SUPFAM; SSF50090; SSF50090; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Membrane; Photosynthesis; Photosystem I;
KW Plastid; Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 45..143
FT /note="Photosystem I reaction center subunit IV A,
FT chloroplastic"
FT /id="PRO_0000029378"
FT REGION 43..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2WSC"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:2WSC"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:2WSC"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:2WSF"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2O01"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2WSF"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2WSC"
SQ SEQUENCE 143 AA; 14967 MW; 0E055D8B2F1D03F0 CRC64;
MAMTTASTVF VLPANVTSVA GASSSRSSVS FLPMRNAGSR LVVRAAEDPA PASSSSKDSP
AAAAAPDGAT ATKPKPPPIG PKRGSKVKIL RRESYWFKNV GSVVAVDQDP KTRYPVVVRF
AKVNYANIST NNYALDEVEE VAA
