ID   PLAS_TETOB              Reviewed;         145 AA.
AC   P26956; Q9SEL9;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Plastocyanin, chloroplastic;
DE   Flags: Precursor;
GN   Name=PETE; Synonyms=PCY1;
OS   Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX   NCBI_TaxID=3088;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=272-3a;
RA   Quinn J.M., Merchant S.;
RT   "Adaptation of Scenedesmus obliquus (Chlorophyceae) to copper-deficiency:
RT   transcriptional regulation of Pcy1 but not Cpx1.";
RL   J. Phycol. 35:1253-1263(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 49-145, FUNCTION, AND SUBCELLULAR LOCATION.
RA   Sykes A.G.;
RT   "Structure and electron-transfer reactivity of the blue copper protein
RT   plastocyanin.";
RL   Chem. Soc. Rev. 14:283-315(1985).
RN   [3]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   McGinnis J., Sinclair-day J.D., Sykes A.G., Powls R., Moore J.,
RA   Wright P.D.;
RT   "Kinetic studies on 1:1 electron-transfer reactions involving blue copper
RT   proteins. 16. Reactivity of plastocyanin from the green alga Scenedesmus
RT   obliquus with inorganic redox partners and related NMR studies.";
RL   Inorg. Chem. 27:2306-2312(1988).
RN   [4]
RP   STRUCTURE BY NMR, AND SUBCELLULAR LOCATION.
RX   PubMed=3353725; DOI=10.1126/science.3353725;
RA   Moore J.M., Case D.A., Chazin W.J., Gippert G.P., Havel T.F., Powls R.,
RA   Wright P.E.;
RT   "Three-dimensional solution structure of plastocyanin from the green alga
RT   Scenedesmus obliquus.";
RL   Science 240:314-317(1988).
RN   [5]
RP   STRUCTURE BY NMR, AND SUBCELLULAR LOCATION.
RX   PubMed=3207712; DOI=10.1021/bi00420a033;
RA   Moore J.M., Chazin W.J., Powls R., Wright P.E.;
RT   "1H NMR studies of plastocyanin from Scenedesmus obliquus: complete
RT   sequence-specific assignment, secondary structure analysis, and global
RT   fold.";
RL   Biochemistry 27:7806-7816(1988).
CC   -!- FUNCTION: Participates in electron transfer between P700 and the
CC       cytochrome b6-f complex in photosystem I. {ECO:0000269|Ref.2}.
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|PubMed:3207712, ECO:0000269|PubMed:3353725,
CC       ECO:0000269|Ref.2}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:3207712, ECO:0000269|PubMed:3353725,
CC       ECO:0000269|Ref.2}; Lumenal side {ECO:0000269|PubMed:3207712,
CC       ECO:0000269|PubMed:3353725, ECO:0000269|Ref.2}. Note=Loosely bound to
CC       the inner thylakoid membrane surface in chloroplasts.
CC   -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR   EMBL; AF114235; AAD03610.1; -; Genomic_DNA.
DR   PIR; JW0013; JW0013.
DR   AlphaFoldDB; P26956; -.
DR   BMRB; P26956; -.
DR   SMR; P26956; -.
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; Transit peptide; Transport.
FT   TRANSIT         1..48
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           49..145
FT                   /note="Plastocyanin, chloroplastic"
FT                   /id="PRO_0000002895"
FT   DOMAIN          49..145
FT                   /note="Plastocyanin-like"
FT   BINDING         85
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
FT   BINDING         130
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
FT   BINDING         133
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
FT   BINDING         138
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
SQ   SEQUENCE   145 AA;  14774 MW;  BF354AE02C6D1761 CRC64;
     MASLMRKAAV APAKATRTTV KASASLQRVA QAAGVAVAGF SLALSANAAN VKLGADSGAL
     VFEPATVTIK AGDSVTWTNN AGFPHNIVFD EDAVPAGVNA DALSHDDYLN APGESYTAKF
     DTAGEYGYFC EPHQGAGMVG KVIVQ