PSBC_ARATH
ID PSBC_ARATH Reviewed; 473 AA.
AC P56778;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Photosystem II CP43 reaction center protein {ECO:0000255|HAMAP-Rule:MF_01496};
DE AltName: Full=PSII 43 kDa protein {ECO:0000255|HAMAP-Rule:MF_01496};
DE AltName: Full=Protein CP-43 {ECO:0000255|HAMAP-Rule:MF_01496};
DE Flags: Precursor;
GN Name=psbC {ECO:0000255|HAMAP-Rule:MF_01496}; Synonyms=CP43;
GN OrderedLocusNames=AtCg00280;
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 SEQUENCE REVISION TO N-TERMINUS.
RA Nakamura Y.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 15-26, SUBCELLULAR LOCATION, DEAMIDATION AT ASN-18,
RP PHOSPHORYLATION AT THR-15, AND ACETYLATION AT THR-15.
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 [4]
RP RETRACTED PAPER.
RX PubMed=17601825; DOI=10.1105/tpc.107.050526;
RA Ma J., Peng L., Guo J., Lu Q., Lu C., Zhang L.;
RT "LPA2 is required for efficient assembly of photosystem II in Arabidopsis
RT thaliana.";
RL Plant Cell 19:1980-1993(2007).
RN [5]
RP RETRACTION NOTICE OF PUBMED:17601825.
RX PubMed=27895223; DOI=10.1105/tpc.16.00881;
RA Ma J., Peng L., Guo J., Lu Q., Lu C., Zhang L.;
RL Plant Cell 28:3061-3061(2016).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15, AND IDENTIFICATION BY
RP 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 [8]
RP INTERACTION WITH PAM68, AND SUBUNIT.
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 [9]
RP RETRACTED PAPER.
RX PubMed=20605914; DOI=10.1104/pp.110.159558;
RA Cai W., Ma J., Chi W., Zou M., Guo J., Lu C., Zhang L.;
RT "Cooperation of LPA3 and LPA2 is essential for photosystem II assembly in
RT Arabidopsis.";
RL Plant Physiol. 154:109-120(2010).
RN [10]
RP RETRACTION NOTICE OF PUBMED:20605914.
RX PubMed=28154118; DOI=10.1104/pp.16.01908;
RA Cai W., Ma J., Chi W., Zou M., Guo J., Lu C., Zhang L.;
RL Plant Physiol. 173:1526-1526(2017).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-15, CLEAVAGE OF PROPEPTIDE [LARGE
RP SCALE ANALYSIS] AFTER GLU-14, 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).
RN [12]
RP INTERACTION WITH HHL1.
RX PubMed=24632535; DOI=10.1105/tpc.113.122424;
RA Jin H., Liu B., Luo L., Feng D., Wang P., Liu J., Da Q., He Y., Qi K.,
RA Wang J., Wang H.B.;
RT "HYPERSENSITIVE TO HIGH LIGHT1 interacts with LOW QUANTUM YIELD OF
RT PHOTOSYSTEM II1 and functions in protection of photosystem II from
RT photodamage in Arabidopsis.";
RL Plant Cell 26:1213-1229(2014).
CC -!- FUNCTION: One of the components of the core complex of photosystem II
CC (PSII). It binds chlorophyll and helps catalyze the primary light-
CC induced photochemical processes of PSII. PSII is a light-driven
CC water:plastoquinone oxidoreductase, using light energy to abstract
CC electrons from H(2)O, generating O(2) and a proton gradient
CC subsequently used for ATP formation. {ECO:0000255|HAMAP-Rule:MF_01496}.
CC -!- COFACTOR:
CC Note=Binds multiple chlorophylls and provides some of the ligands for
CC the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also
CC provide a ligand for a Cl- that is required for oxygen evolution. PSII
CC binds additional chlorophylls, carotenoids and specific lipids.
CC {ECO:0000255|HAMAP-Rule:MF_01496};
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-
CC evolving complex and a large number of cofactors. It forms dimeric
CC complexes (By similarity). Interacts with PAM68 (PubMed:20923938).
CC Interacts with HHL1 (PubMed:24632535). {ECO:0000255|HAMAP-
CC Rule:MF_01496, ECO:0000269|PubMed:20923938,
CC ECO:0000269|PubMed:24632535}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000269|PubMed:11113141}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000305}.
CC -!- PTM: Phosphorylation occurs in normal plant growth light conditions.
CC Rapid dephosphorylation occurs during heat shock.
CC {ECO:0000269|PubMed:11113141}.
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01496}.
CC -!- CAUTION: An article reported an interaction with LPA2; however, this
CC paper was later retracted. An article reported an interaction with
CC LPA3; however, this paper was later retracted.
CC {ECO:0000305|PubMed:17601825, ECO:0000305|PubMed:20605914,
CC ECO:0000305|PubMed:27895223, ECO:0000305|PubMed:28154118}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA84381.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000423; BAA84381.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_051055.1; NC_000932.1.
DR PDB; 5MDX; EM; 5.30 A; C/c=15-473.
DR PDB; 7OUI; EM; 2.79 A; C/c=15-473.
DR PDBsum; 5MDX; -.
DR PDBsum; 7OUI; -.
DR AlphaFoldDB; P56778; -.
DR SMR; P56778; -.
DR BioGRID; 29972; 30.
DR IntAct; P56778; 2.
DR MINT; P56778; -.
DR STRING; 3702.ATCG00280.1; -.
DR TCDB; 3.E.2.2.3; the photosynthetic reaction center (prc) family.
DR iPTMnet; P56778; -.
DR PaxDb; P56778; -.
DR PRIDE; P56778; -.
DR ProteomicsDB; 226226; -.
DR EnsemblPlants; ATCG00280.1; ATCG00280.1; ATCG00280.
DR GeneID; 844773; -.
DR Gramene; ATCG00280.1; ATCG00280.1; ATCG00280.
DR KEGG; ath:ArthCp018; -.
DR Araport; ATCG00280; -.
DR TAIR; locus:504954652; ATCG00280.
DR eggNOG; ENOG502QR3X; Eukaryota.
DR HOGENOM; CLU_028310_1_1_1; -.
DR InParanoid; P56778; -.
DR OMA; WKDKNKM; -.
DR OrthoDB; 620323at2759; -.
DR BioCyc; MetaCyc:ATCG00280-MON; -.
DR PRO; PR:P56778; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P56778; baseline and differential.
DR Genevisible; P56778; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009533; C:chloroplast stromal thylakoid; IDA: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:0009539; C:photosystem II reaction center; TAS:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR Gene3D; 1.10.10.670; -; 1.
DR HAMAP; MF_01496; PSII_PsbC_CP43; 1.
DR InterPro; IPR000932; PS_antenna-like.
DR InterPro; IPR036001; PS_II_antenna-like_sf.
DR InterPro; IPR005869; PSII_PsbC.
DR InterPro; IPR044900; PSII_PsbC_sf.
DR PANTHER; PTHR33180; PTHR33180; 1.
DR Pfam; PF00421; PSII; 1.
DR SUPFAM; SSF161077; SSF161077; 1.
DR TIGRFAMs; TIGR01153; psbC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chlorophyll; Chloroplast; Chromophore;
KW Direct protein sequencing; Manganese; Membrane; Metal-binding;
KW Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
FT PROPEP 1..14
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:11113141, ECO:0007744|PubMed:22223895"
FT /id="PRO_0000029428"
FT CHAIN 15..473
FT /note="Photosystem II CP43 reaction center protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000029429"
FT TRANSMEM 73..88
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 139..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 180..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 262..276
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 292..307
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 452..468
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT BINDING 367
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT MOD_RES 15
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:11113141, ECO:0007744|PubMed:22223895"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:11113141, ECO:0007744|PubMed:19376835"
FT MOD_RES 18
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000269|PubMed:11113141"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 46..73
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 109..134
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 154..180
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 230..253
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 268..292
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 306..324
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 386..396
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 422..453
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:7OUI"
SQ SEQUENCE 473 AA; 51868 MW; 1AF08B5C4270126C CRC64;
MKTLYSLRRF YHVETLFNGT LALAGRDQET TGFAWWAGNA RLINLSGKLL GAHVAHAGLI
VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG PGGEVIDTFP YFVSGVLHLI
SSAVLGFGGI YHALLGPETL EESFPFFGYV WKDRNKMTTI LGIHLILLGV GAFLLVFKAL
YFGGVYDTWA PGGGDVRKIT NLTLSPSVIF GYLLKSPFGG EGWIVSVDDL EDIIGGHVWL
GSICIFGGIW HILTKPFAWA RRALVWSGEA YLSYSLAALS VCGFIACCFV WFNNTAYPSE
FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI FGGETMRFWD
LRAPWLEPLR GPNGLDLSRL KKDIQPWQER RSAEYMTHAP LGSLNSVGGV ATEINAVNYV
SPRSWLSTSH FVLGFFLFVG HLWHAGRARA AAAGFEKGID RDFEPVLSMT PLN
