ID   PLAS_ULVPE              Reviewed;          98 AA.
AC   P56274;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Plastocyanin;
GN   Name=PETE;
OS   Ulva pertusa (Sea lettuce).
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; OUU clade; Ulvales;
OC   Ulvaceae; Ulva.
OX   NCBI_TaxID=3120;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-20, AND ANTIVIRAL ACTIVITY.
RA   Liu Z., Wu Z., Lin Q., Xie L.;
RL   Submitted (JUN-2003) to UniProtKB.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COPPER, COFACTOR, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=9933621; DOI=10.1074/jbc.274.7.4225;
RA   Shibata N., Inoue T., Nagano C., Nishio N., Kohzuma T., Onodera K.,
RA   Yoshizaki F., Sugimura Y., Kai Y.;
RT   "Novel insight into the copper-ligand geometry in the crystal structure of
RT   Ulva pertusa plastocyanin at 1.6-A resolution. Structural basis for
RT   regulation of the copper site by residue 88.";
RL   J. Biol. Chem. 274:4225-4230(1999).
CC   -!- FUNCTION: Participates in electron transfer between P700 and the
CC       cytochrome b6-f complex in photosystem I (By similarity). Has antiviral
CC       activity against Potato virus Y (strain N) (Ref.1).
CC       {ECO:0000250|UniProtKB:P18068, ECO:0000269|Ref.1}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000269|PubMed:9933621};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:9933621}; 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   PDB; 1IUZ; X-ray; 1.60 A; A=1-98.
DR   PDBsum; 1IUZ; -.
DR   AlphaFoldDB; P56274; -.
DR   SMR; P56274; -.
DR   EvolutionaryTrace; P56274; -.
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   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
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   3D-structure; Antiviral defense; Chloroplast; Copper;
KW   Direct protein sequencing; Electron transport; Membrane; Metal-binding;
KW   Plastid; Thylakoid; Transport.
FT   CHAIN           1..98
FT                   /note="Plastocyanin"
FT                   /id="PRO_0000085579"
FT   DOMAIN          1..98
FT                   /note="Plastocyanin-like"
FT   BINDING         38
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000269|PubMed:9933621,
FT                   ECO:0007744|PDB:1IUZ"
FT   BINDING         83
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000269|PubMed:9933621,
FT                   ECO:0007744|PDB:1IUZ"
FT   BINDING         86
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000269|PubMed:9933621,
FT                   ECO:0007744|PDB:1IUZ"
FT   BINDING         91
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000269|PubMed:9933621,
FT                   ECO:0007744|PDB:1IUZ"
FT   CONFLICT        2
FT                   /note="Q -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:1IUZ"
FT   STRAND          14..23
FT                   /evidence="ECO:0007829|PDB:1IUZ"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:1IUZ"
FT   STRAND          38..42
FT                   /evidence="ECO:0007829|PDB:1IUZ"
FT   HELIX           53..56
FT                   /evidence="ECO:0007829|PDB:1IUZ"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:1IUZ"
FT   STRAND          68..72
FT                   /evidence="ECO:0007829|PDB:1IUZ"
FT   STRAND          77..82
FT                   /evidence="ECO:0007829|PDB:1IUZ"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:1IUZ"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:1IUZ"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:1IUZ"
SQ   SEQUENCE   98 AA;  10189 MW;  FAA821FC739676F2 CRC64;
     AQIVKLGGDD GSLAFVPSKI SVAAGEAIEF VNNAGFPHNI VFDEDAVPAG VDADAISYDD
     YLNSKGETVV RKLSTPGVYG VYCEPHAGAG MKMTITVQ