PB27A_ARATH
ID PB27A_ARATH Reviewed; 174 AA.
AC Q9LR64; Q9FPJ9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Photosystem II repair protein PSB27-H1, chloroplastic;
DE Short=Psb27-H1;
DE AltName: Full=Thylakoid lumenal protein PSB27-H1;
DE Flags: Precursor;
GN Name=PSB27-1; OrderedLocusNames=At1g03600;
GN ORFNames=F21B7.14, F21B7.21, F21B7.22, F21B7_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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 PROTEIN SEQUENCE OF N-TERMINUS, 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 PROTEIN SEQUENCE OF 69-80, AND SUBCELLULAR LOCATION.
RX PubMed=16245054; DOI=10.1023/b:pres.0000006913.86689.f1;
RA Kieselbach T., Schroeder W.P.;
RT "The proteome of the chloroplast lumen of higher plants.";
RL Photosyn. Res. 78:249-264(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16897475; DOI=10.1007/s11103-006-0031-x;
RA Chen H., Zhang D., Guo J., Wu H., Jin M., Lu Q., Lu C., Zhang L.;
RT "A Psb27 homologue in Arabidopsis thaliana is required for efficient repair
RT of photodamaged photosystem II.";
RL Plant Mol. Biol. 61:567-575(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94 AND TYR-132, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Probably involved in repair of photodamaged photosystem II
CC (PSII). {ECO:0000269|PubMed:16897475}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:16245054, ECO:0000269|PubMed:18431481}; Peripheral
CC membrane protein {ECO:0000269|PubMed:16245054}; Lumenal side
CC {ECO:0000269|PubMed:16245054}. Note=Associated with PSII on the lumenal
CC side of the thylakoid membrane.
CC -!- DISRUPTION PHENOTYPE: Plants grow slightly slower and are slightly
CC smaller than wild-type. Somewhat photoinhibited, in strong light the
CC amount of D1 (psbA) protein decreased faster than wild-type and thus
CC levels of PSII are decreased. {ECO:0000269|PubMed:16897475}.
CC -!- SIMILARITY: Belongs to the Psb27 family. {ECO:0000305}.
CC -!- CAUTION: Was also called At1g03610 (in AAM47889). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG40041.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC002560; AAF86516.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27588.1; -; Genomic_DNA.
DR EMBL; AF370539; AAK48966.1; -; mRNA.
DR EMBL; AY044332; AAK73273.1; -; mRNA.
DR EMBL; AY114570; AAM47889.1; -; mRNA.
DR EMBL; AF324690; AAG40041.1; ALT_FRAME; mRNA.
DR EMBL; AY084551; AAM61118.1; -; mRNA.
DR PIR; T00900; T00900.
DR RefSeq; NP_563687.1; NM_100240.3.
DR PDB; 5X56; X-ray; 1.85 A; A/B=69-174.
DR PDBsum; 5X56; -.
DR AlphaFoldDB; Q9LR64; -.
DR SMR; Q9LR64; -.
DR BioGRID; 24684; 4.
DR IntAct; Q9LR64; 3.
DR STRING; 3702.AT1G03600.1; -.
DR iPTMnet; Q9LR64; -.
DR MetOSite; Q9LR64; -.
DR PaxDb; Q9LR64; -.
DR PRIDE; Q9LR64; -.
DR ProteomicsDB; 236438; -.
DR EnsemblPlants; AT1G03600.1; AT1G03600.1; AT1G03600.
DR GeneID; 839449; -.
DR Gramene; AT1G03600.1; AT1G03600.1; AT1G03600.
DR KEGG; ath:AT1G03600; -.
DR Araport; AT1G03600; -.
DR TAIR; locus:2020788; AT1G03600.
DR eggNOG; ENOG502RZI3; Eukaryota.
DR HOGENOM; CLU_112237_1_0_1; -.
DR InParanoid; Q9LR64; -.
DR OMA; HYSSYPN; -.
DR OrthoDB; 1451523at2759; -.
DR PhylomeDB; Q9LR64; -.
DR PRO; PR:Q9LR64; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LR64; baseline and differential.
DR Genevisible; Q9LR64; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0009523; C:photosystem II; IEA:InterPro.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0071484; P:cellular response to light intensity; IMP:TAIR.
DR GO; GO:0010207; P:photosystem II assembly; IBA:GO_Central.
DR GO; GO:0010206; P:photosystem II repair; IMP:TAIR.
DR Gene3D; 1.20.58.810; -; 1.
DR HAMAP; MF_01481; PSII_Psb27; 1.
DR InterPro; IPR025585; PSII_Pbs27.
DR InterPro; IPR038450; PSII_Pbs27_sf.
DR PANTHER; PTHR34041; PTHR34041; 1.
DR Pfam; PF13326; PSII_Pbs27; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Membrane;
KW Phosphoprotein; Plastid; Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..68
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11826309,
FT ECO:0000269|PubMed:16245054"
FT CHAIN 69..174
FT /note="Photosystem II repair protein PSB27-H1,
FT chloroplastic"
FT /id="PRO_0000342099"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:5X56"
FT HELIX 98..116
FT /evidence="ECO:0007829|PDB:5X56"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:5X56"
FT HELIX 126..144
FT /evidence="ECO:0007829|PDB:5X56"
FT HELIX 153..170
FT /evidence="ECO:0007829|PDB:5X56"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5X56"
SQ SEQUENCE 174 AA; 18835 MW; 5C32D46E97269C93 CRC64;
MASASATATL LKPNLPPHKP TIIASSVSPP LPPPRRNHLL RRDFLSLAAT STLLTQSIQF
LAPAPVSAAE DEEYIKDTSA VISKVRSTLS MQKTDPNVAD AVAELREASN SWVAKYRKEK
ALLGKASFRD IYSALNAVSG HYVSFGPTAP IPAKRKARIL EEMETAEKAL TRGR
