ID   PLAS_RUMOB              Reviewed;          99 AA.
AC   P00298;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Plastocyanin;
GN   Name=PETE;
OS   Rumex obtusifolius (Bitter dock).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Polygonaceae; Polygonoideae; Rumiceae; Rumex;
OC   Rumex subgen. Acetosa.
OX   NCBI_TaxID=3619;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RA   Haslett B., Bailey C.J., Ramshaw J.A.M., Scawen M.D., Boulter D.;
RT   "Studies of the amino acid sequence of plastocyanin from Rumex obtusifolius
RT   (broad-leaved dock).";
RL   Biochem. Soc. Trans. 2:1329-1331(1974).
RN   [2]
RP   SEQUENCE REVISION TO 92.
RA   Freeman H.C.;
RT   "Elegance in molecular design: the copper site of photosynthetic electron-
RT   transfer protein.";
RL   J. Proc. Royal Soc. N.S. Wales 112:45-62(1979).
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; A90349; CURXCO.
DR   AlphaFoldDB; P00298; -.
DR   SMR; P00298; -.
DR   PRIDE; P00298; -.
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_0000085572"
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;  10355 MW;  1CCB254EA0B1206A CRC64;
     IEIKLGGDDG ALAFVPGSFT VAAGEKIVFK NNAGFPHNIV FDEDEVPAGV DASKISMSEE
     DLLNAPGETY AVTLSEKGTY SFYCSPHQGA GMVGKVTVQ