PSBH_MAIZE
ID PSBH_MAIZE Reviewed; 73 AA.
AC P24993;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 112.
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};
OS Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2835175; DOI=10.1007/bf00420729;
RA Rock C.D., Barkan A., Taylor W.C.;
RT "The maize plastid psbB-psbF-petB-petD gene cluster: spliced and unspliced
RT petB and petD RNAs encode alternative products.";
RL Curr. Genet. 12:69-77(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [3]
RP PROTEIN SEQUENCE OF 2-15, SUBUNIT, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT THR-3 AND THR-5.
RC STRAIN=cv. Olenka; TISSUE=Bundle sheath cell, and Mesophyll cell;
RX PubMed=22833285; DOI=10.1002/pmic.201200196;
RA Fristedt R., Wasilewska W., Romanowska E., Vener A.V.;
RT "Differential phosphorylation of thylakoid proteins in mesophyll and bundle
RT sheath chloroplasts from maize plants grown under low or high light.";
RL Proteomics 12:2852-2861(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. {ECO:0000255|HAMAP-
CC Rule:MF_00752, ECO:0000269|PubMed:22833285}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000269|PubMed:22833285}; Single-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00752,
CC ECO:0000305|PubMed:22833285}. Note=PSII is more abundant in mesophyll
CC cells than bundle sheath cells. {ECO:0000269|PubMed:22833285}.
CC -!- PTM: Phosphorylated in both bundle sheath and mesophyll cells,
CC phosphorylation increases when cells are grown under high rather than
CC low light regimes (70 vs 900 umol photons/m-2/s). Double
CC phosphorylation in bundle sheath cells is only seen when cells are
CC grown under high light regimes. {ECO:0000269|PubMed:22833285}.
CC -!- PTM: Phosphorylation is a light-dependent reaction catalyzed by a
CC membrane-bound kinase; phosphorylation occurs on Thr residue(s) in the
CC N-terminus of the protein. {ECO:0000255|HAMAP-Rule:MF_00752}.
CC -!- SIMILARITY: Belongs to the PsbH family. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
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DR EMBL; X05422; CAA28998.1; -; Genomic_DNA.
DR EMBL; X86563; CAA60314.1; -; Genomic_DNA.
DR PIR; S08591; F2ZMBH.
DR RefSeq; NP_043052.1; NC_001666.2.
DR AlphaFoldDB; P24993; -.
DR SMR; P24993; -.
DR STRING; 4577.GRMZM5G831399_P01; -.
DR iPTMnet; P24993; -.
DR PaxDb; P24993; -.
DR GeneID; 845205; -.
DR KEGG; zma:845205; -.
DR MaizeGDB; 69555; -.
DR eggNOG; ENOG502S8Y7; Eukaryota.
DR HOGENOM; CLU_190203_1_0_1; -.
DR OMA; MSWLSST; -.
DR OrthoDB; 1583583at2759; -.
DR Proteomes; UP000007305; Chloroplast.
DR Genevisible; P24993; ZM.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
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 Chloroplast; Direct protein sequencing; Membrane; Phosphoprotein;
KW Photosynthesis; Photosystem II; Plastid; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:22833285"
FT CHAIN 2..73
FT /note="Photosystem II reaction center protein H"
FT /id="PRO_0000070515"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752,
FT ECO:0000269|PubMed:22833285"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752,
FT ECO:0000269|PubMed:22833285"
SQ SEQUENCE 73 AA; 7787 MW; 9901A2599B3A6341 CRC64;
MATQTVEDSS RPKPKRTGAG SLLKPLNSEY GKVAPGWGTT PFMGVAMALF AIFLSIILEI
YNSSVLLDGI LTN
