PLAS_MERPE
ID PLAS_MERPE Reviewed; 99 AA.
AC P00295;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Plastocyanin;
GN Name=PETE;
OS Mercurialis perennis (Dog's mercury).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Mercurialis.
OX NCBI_TaxID=3985;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RA Boulter D., Haslett B.G., Peacock D., Ramshaw J.A.M., Scawen M.D.;
RL (In) Northcote D.H. (eds.);
RL Plant biochemistry II, pp.13:1-40, University Park Press, Baltimore (1977).
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I.
CC {ECO:0000250|UniProtKB:P18068}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:P18068};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|Ref.1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P18068}; Lumenal side
CC {ECO:0000250|UniProtKB:P18068}. Note=Loosely bound to the inner
CC thylakoid membrane surface in chloroplasts (By similarity).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR PIR; A00305; CUDM.
DR AlphaFoldDB; P00295; -.
DR SMR; P00295; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd04219; Plastocyanin; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR001235; Copper_blue_Plastocyanin.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR002387; Plastocyanin.
DR Pfam; PF00127; Copper-bind; 1.
DR PRINTS; PR00156; COPPERBLUE.
DR PRINTS; PR00157; PLASTOCYANIN.
DR SUPFAM; SSF49503; SSF49503; 1.
DR TIGRFAMs; TIGR02656; cyanin_plasto; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Copper; Direct protein sequencing; Electron transport;
KW Membrane; Metal-binding; Plastid; Thylakoid; Transport.
FT CHAIN 1..99
FT /note="Plastocyanin"
FT /id="PRO_0000085569"
FT DOMAIN 1..99
FT /note="Plastocyanin-like"
FT BINDING 37
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT BINDING 84
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
SQ SEQUENCE 99 AA; 10486 MW; 009AB50FDA9B7033 CRC64;
LDVLLGSDDG ELAFVPNNFS VPSGEKITFK NNAGFPHNVV FDEDEIPSGV DASKISMDEA
DLLNAPGETY AVTLTEKGSY SFYCSPHQGA GMVGKVTVN