ID   PLAS_FRIAG              Reviewed;         166 AA.
AC   O22646;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Plastocyanin, chloroplastic;
DE   Flags: Precursor;
GN   Name=PETE; Synonyms=PLOC;
OS   Fritillaria agrestis (Stinkbells).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Fritillaria.
OX   NCBI_TaxID=64177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Panico E., Baysdorfer C.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P18068}; 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   EMBL; AF031545; AAB86855.1; -; mRNA.
DR   AlphaFoldDB; O22646; -.
DR   SMR; O22646; -.
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; 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.
PE   2: Evidence at transcript level;
KW   Chloroplast; Copper; Electron transport; Membrane; Metal-binding; Plastid;
KW   Thylakoid; Transit peptide; Transport.
FT   TRANSIT         1..67
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           68..166
FT                   /note="Plastocyanin, chloroplastic"
FT                   /id="PRO_0000002887"
FT   DOMAIN          68..166
FT                   /note="Plastocyanin-like"
FT   BINDING         104
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
FT   BINDING         151
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
FT   BINDING         154
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
FT   BINDING         159
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
SQ   SEQUENCE   166 AA;  16788 MW;  E9C1263422D23078 CRC64;
     MASLTSAAVT IPSFTGLKAG RAPTTPSTSI KPPTPMSFSV KASFKEAIGT ALVATAAGAV
     LASNALAVEV LLGGSDGSLA FVPSNIEVAA GETVVFKNNA GFPHNVLFDE DEVPKGVDAG
     AISMKEEDLL NAPGETFSVT LKEKGTYSIY CSPHQGAGMA GKITVN