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Protein

Photosystem II CP43 reaction center protein

Gene

psbC

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H2O, generating O2 and a proton gradient subsequently used for ATP formation.UniRule annotation

Cofactori

Note: Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi367 – 3671Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2UniRule annotation
Metal bindingi367 – 3671Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Photosynthesis

Keywords - Ligandi

Chlorophyll, Chromophore, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ATCG00280-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem II CP43 reaction center proteinUniRule annotation
Alternative name(s):
PSII 43 kDa proteinUniRule annotation
Protein CP-43UniRule annotation
Gene namesi
Name:psbCUniRule annotation
Synonyms:CP43
Ordered Locus Names:AtCg00280
Encoded oniPlastid; Chloroplast
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chloroplast

Organism-specific databases

TAIRiATCG00280.

Subcellular locationi

  • Plastidchloroplast thylakoid membrane UniRule annotation1 Publication; Multi-pass membrane protein UniRule annotationCurated

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei73 – 8816HelicalUniRule annotationAdd
BLAST
Transmembranei139 – 15315HelicalUniRule annotationAdd
BLAST
Transmembranei180 – 19617HelicalUniRule annotationAdd
BLAST
Transmembranei262 – 27615HelicalUniRule annotationAdd
BLAST
Transmembranei292 – 30716HelicalUniRule annotationAdd
BLAST
Transmembranei452 – 46817HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Photosystem II, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1414UniRule annotationCombined sources1 PublicationPRO_0000029428Add
BLAST
Chaini15 – 473459Photosystem II CP43 reaction center proteinUniRule annotationPRO_0000029429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151N-acetylthreonineUniRule annotationCombined sources1 Publication
Modified residuei15 – 151PhosphothreonineUniRule annotationCombined sources1 Publication
Modified residuei18 – 181Deamidated asparagine1 Publication

Post-translational modificationi

Phosphorylation occurs in normal plant growth light conditions. Rapid dephosphorylation occurs during heat shock.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP56778.
PRIDEiP56778.

PTM databases

iPTMnetiP56778.

Expressioni

Gene expression databases

GenevisibleiP56778. AT.

Interactioni

Subunit structurei

PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes (By similarity). Interacts with PAM68, LPA2 and LPA3. Interacts with HHL1 (PubMed:24632535).UniRule annotation4 Publications

Protein-protein interaction databases

BioGridi29972. 6 interactions.
IntActiP56778. 1 interaction.
MINTiMINT-8360524.
STRINGi3702.ATCG00280.1.

Structurei

3D structure databases

ProteinModelPortaliP56778.
SMRiP56778. Positions 36-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PsbB/PsbC family. PsbC subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEKR. Eukaryota.
ENOG410XQVF. LUCA.
HOGENOMiHOG000111335.
InParanoidiP56778.
KOiK02705.
OMAiFFFLVGH.

Family and domain databases

HAMAPiMF_01496. PSII_PsbC_CP43.
InterProiIPR000932. PS_antenna-like.
IPR005869. PSII_PsbC.
[Graphical view]
PfamiPF00421. PSII. 1 hit.
[Graphical view]
SUPFAMiSSF161077. SSF161077. 1 hit.
TIGRFAMsiTIGR01153. psbC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56778-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLYSLRRF YHVETLFNGT LALAGRDQET TGFAWWAGNA RLINLSGKLL
60 70 80 90 100
GAHVAHAGLI VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG
110 120 130 140 150
PGGEVIDTFP YFVSGVLHLI SSAVLGFGGI YHALLGPETL EESFPFFGYV
160 170 180 190 200
WKDRNKMTTI LGIHLILLGV GAFLLVFKAL YFGGVYDTWA PGGGDVRKIT
210 220 230 240 250
NLTLSPSVIF GYLLKSPFGG EGWIVSVDDL EDIIGGHVWL GSICIFGGIW
260 270 280 290 300
HILTKPFAWA RRALVWSGEA YLSYSLAALS VCGFIACCFV WFNNTAYPSE
310 320 330 340 350
FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI
360 370 380 390 400
FGGETMRFWD LRAPWLEPLR GPNGLDLSRL KKDIQPWQER RSAEYMTHAP
410 420 430 440 450
LGSLNSVGGV ATEINAVNYV SPRSWLSTSH FVLGFFLFVG HLWHAGRARA
460 470
AAAGFEKGID RDFEPVLSMT PLN
Length:473
Mass (Da):51,868
Last modified:January 25, 2012 - v3
Checksum:i1AF08B5C4270126C
GO

Sequence cautioni

The sequence BAA84381.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP000423 Genomic DNA. Translation: BAA84381.2. Sequence problems.
RefSeqiNP_051055.1. NC_000932.1.

Genome annotation databases

EnsemblPlantsiATCG00280.1; ATCG00280.1; ATCG00280.
GeneIDi844773.
GrameneiATCG00280.1; ATCG00280.1; ATCG00280.
KEGGiath:ArthCp018.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP000423 Genomic DNA. Translation: BAA84381.2. Sequence problems.
RefSeqiNP_051055.1. NC_000932.1.

3D structure databases

ProteinModelPortaliP56778.
SMRiP56778. Positions 36-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi29972. 6 interactions.
IntActiP56778. 1 interaction.
MINTiMINT-8360524.
STRINGi3702.ATCG00280.1.

PTM databases

iPTMnetiP56778.

Proteomic databases

PaxDbiP56778.
PRIDEiP56778.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiATCG00280.1; ATCG00280.1; ATCG00280.
GeneIDi844773.
GrameneiATCG00280.1; ATCG00280.1; ATCG00280.
KEGGiath:ArthCp018.

Organism-specific databases

TAIRiATCG00280.

Phylogenomic databases

eggNOGiENOG410IEKR. Eukaryota.
ENOG410XQVF. LUCA.
HOGENOMiHOG000111335.
InParanoidiP56778.
KOiK02705.
OMAiFFFLVGH.

Enzyme and pathway databases

BioCyciMetaCyc:ATCG00280-MONOMER.

Miscellaneous databases

PROiP56778.

Gene expression databases

GenevisibleiP56778. AT.

Family and domain databases

HAMAPiMF_01496. PSII_PsbC_CP43.
InterProiIPR000932. PS_antenna-like.
IPR005869. PSII_PsbC.
[Graphical view]
PfamiPF00421. PSII. 1 hit.
[Graphical view]
SUPFAMiSSF161077. SSF161077. 1 hit.
TIGRFAMsiTIGR01153. psbC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete structure of the chloroplast genome of Arabidopsis thaliana."
    Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.
    DNA Res. 6:283-290(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. Nakamura Y.
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO N-TERMINUS.
  3. "Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana."
    Vener A.V., Harms A., Sussman M.R., Vierstra R.D.
    J. Biol. Chem. 276:6959-6966(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 15-26, SUBCELLULAR LOCATION, DEAMIDATION AT ASN-18, PHOSPHORYLATION AT THR-15, ACETYLATION AT THR-15.
    Strain: cv. Columbia.
  4. "LPA2 is required for efficient assembly of photosystem II in Arabidopsis thaliana."
    Ma J., Peng L., Guo J., Lu Q., Lu C., Zhang L.
    Plant Cell 19:1980-1993(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LPA2, SUBUNIT.
  5. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  6. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "The Arabidopsis thylakoid protein PAM68 is required for efficient D1 biogenesis and photosystem II assembly."
    Armbruster U., Zuhlke J., Rengstl B., Kreller R., Makarenko E., Ruhle T., Schunemann D., Jahns P., Weisshaar B., Nickelsen J., Leister D.
    Plant Cell 22:3439-3460(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAM68, SUBUNIT.
  8. "Cooperation of LPA3 and LPA2 is essential for photosystem II assembly in Arabidopsis."
    Cai W., Ma J., Chi W., Zou M., Guo J., Lu C., Zhang L.
    Plant Physiol. 154:109-120(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LPA3, SUBUNIT.
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-15, CLEAVAGE OF PROPEPTIDE [LARGE SCALE ANALYSIS] AFTER GLU-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "HYPERSENSITIVE TO HIGH LIGHT1 interacts with LOW QUANTUM YIELD OF PHOTOSYSTEM II1 and functions in protection of photosystem II from photodamage in Arabidopsis."
    Jin H., Liu B., Luo L., Feng D., Wang P., Liu J., Da Q., He Y., Qi K., Wang J., Wang H.B.
    Plant Cell 26:1213-1229(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHL1.

Entry informationi

Entry nameiPSBC_ARATH
AccessioniPrimary (citable) accession number: P56778
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 25, 2012
Last modified: May 11, 2016
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The assembly of PsbC into photosystem II complex requires the presence of LPA2 and LPA3.2 Publications

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.