PSBH_ARATH
ID PSBH_ARATH Reviewed; 73 AA.
AC P56780;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Photosystem II reaction center protein H {ECO:0000255|HAMAP-Rule:MF_00752};
DE Short=PSII-H {ECO:0000255|HAMAP-Rule:MF_00752};
DE AltName: Full=Photosystem II 10 kDa phosphoprotein {ECO:0000255|HAMAP-Rule:MF_00752};
GN Name=psbH {ECO:0000255|HAMAP-Rule:MF_00752}; OrderedLocusNames=AtCg00710;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
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=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
RN [2]
RP PROTEIN SEQUENCE OF 2-11, SUBUNIT, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT THR-3 AND THR-5.
RC STRAIN=cv. Columbia;
RX PubMed=11113141; DOI=10.1074/jbc.m009394200;
RA Vener A.V., Harms A., Sussman M.R., Vierstra R.D.;
RT "Mass spectrometric resolution of reversible protein phosphorylation in
RT photosynthetic membranes of Arabidopsis thaliana.";
RL J. Biol. Chem. 276:6959-6966(2001).
RN [3]
RP PHOSPHORYLATION AT THR-5 BY STN8 AND AT THR-3.
RC STRAIN=cv. Columbia;
RX PubMed=16040609; DOI=10.1074/jbc.m505729200;
RA Vainonen J.P., Hansson M., Vener A.V.;
RT "STN8 protein kinase in Arabidopsis thaliana is specific in phosphorylation
RT of photosystem II core proteins.";
RL J. Biol. Chem. 280:33679-33686(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3 AND THR-5, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5]
RP INTERACTION WITH PAM68, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=20923938; DOI=10.1105/tpc.110.077453;
RA Armbruster U., Zuhlke J., Rengstl B., Kreller R., Makarenko E., Ruhle T.,
RA Schunemann D., Jahns P., Weisshaar B., Nickelsen J., Leister D.;
RT "The Arabidopsis thylakoid protein PAM68 is required for efficient D1
RT biogenesis and photosystem II assembly.";
RL Plant Cell 22:3439-3460(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: One of the components of the core complex of photosystem II
CC (PSII), required for its stability and/or assembly. PSII is a light-
CC driven water:plastoquinone oxidoreductase that uses light energy to
CC abstract electrons from H(2)O, generating O(2) and a proton gradient
CC subsequently used for ATP formation. It consists of a core antenna
CC complex that captures photons, and an electron transfer chain that
CC converts photonic excitation into a charge separation.
CC {ECO:0000255|HAMAP-Rule:MF_00752}.
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, numerous small proteins, at least 3 peripheral
CC proteins of the oxygen-evolving complex and a large number of
CC cofactors. It forms dimeric complexes (PubMed:11113141). Interacts with
CC PAM68 (PubMed:20923938). {ECO:0000255|HAMAP-Rule:MF_00752,
CC ECO:0000269|PubMed:11113141, ECO:0000269|PubMed:20923938}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000269|PubMed:11113141,
CC ECO:0000269|PubMed:20923938}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00752}.
CC -!- PTM: Phosphorylation is a light-dependent reaction catalyzed by a
CC membrane-bound kinase. Hyperphosphorylation at Thr-5 is rapidly
CC reversible upon light/dark transitions (PubMed:11113141).
CC Phosphorylation at Thr-5 but not Thr-3 is performed by STN8
CC (PubMed:16040609). Phosphorylation at Thr-3 is not light-dependent and
CC is probably necessary for subsequent phosphorylation at Thr-5
CC (PubMed:16040609). {ECO:0000269|PubMed:11113141,
CC ECO:0000269|PubMed:16040609}.
CC -!- SIMILARITY: Belongs to the PsbH family. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
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DR EMBL; AP000423; BAA84414.1; -; Genomic_DNA.
DR RefSeq; NP_051087.1; NC_000932.1.
DR PDB; 5MDX; EM; 5.30 A; H/h=2-73.
DR PDB; 7OUI; EM; 2.79 A; H/h=2-73.
DR PDBsum; 5MDX; -.
DR PDBsum; 7OUI; -.
DR AlphaFoldDB; P56780; -.
DR SMR; P56780; -.
DR BioGRID; 29936; 11.
DR IntAct; P56780; 2.
DR MINT; P56780; -.
DR STRING; 3702.ATCG00710.1; -.
DR TCDB; 3.E.2.2.3; the photosynthetic reaction center (prc) family.
DR iPTMnet; P56780; -.
DR PaxDb; P56780; -.
DR PRIDE; P56780; -.
DR ProteomicsDB; 226329; -.
DR EnsemblPlants; ATCG00710.1; ATCG00710.1; ATCG00710.
DR GeneID; 844730; -.
DR Gramene; ATCG00710.1; ATCG00710.1; ATCG00710.
DR KEGG; ath:ArthCp052; -.
DR Araport; ATCG00710; -.
DR TAIR; locus:504954694; ATCG00710.
DR eggNOG; ENOG502S8Y7; Eukaryota.
DR HOGENOM; CLU_190203_1_0_1; -.
DR InParanoid; P56780; -.
DR OMA; PLMAVFM; -.
DR OrthoDB; 1583583at2759; -.
DR BioCyc; MetaCyc:ATCG00710-MON; -.
DR PRO; PR:P56780; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P56780; baseline and differential.
DR Genevisible; P56780; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009654; C:photosystem II oxygen evolving complex; TAS:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0042301; F:phosphate ion binding; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR GO; GO:0050821; P:protein stabilization; IEA:InterPro.
DR Gene3D; 1.20.5.880; -; 1.
DR HAMAP; MF_00752; PSII_PsbH; 1.
DR InterPro; IPR001056; PSII_PsbH.
DR InterPro; IPR036863; PSII_PsbH_sf.
DR PANTHER; PTHR34469; PTHR34469; 1.
DR Pfam; PF00737; PsbH; 1.
DR SUPFAM; SSF161025; SSF161025; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chloroplast; Direct protein sequencing;
KW Membrane; Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11113141,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..73
FT /note="Photosystem II reaction center protein H"
FT /id="PRO_0000070498"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752,
FT ECO:0000269|PubMed:11113141, ECO:0000269|PubMed:16040609,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752,
FT ECO:0000269|PubMed:11113141, ECO:0000269|PubMed:16040609,
FT ECO:0007744|PubMed:19376835"
FT HELIX 18..23
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 40..62
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:7OUI"
SQ SEQUENCE 73 AA; 7702 MW; 6566FCC384606110 CRC64;
MATQTVEDSS RSGPRSTTVG KLLKPLNSEY GKVAPGWGTT PLMGVAMALF AVFLSIILEI
YNSSVLLDGI SVN
