PLAS_ULVPR
ID PLAS_ULVPR Reviewed; 98 AA.
AC P07465;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Plastocyanin;
GN Name=PETE;
OS Ulva prolifera (Green seaweed) (Enteromorpha prolifera).
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; OUU clade; Ulvales;
OC Ulvaceae; Ulva.
OX NCBI_TaxID=3117;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RX PubMed=3522227; DOI=10.1111/j.1432-1033.1986.tb09694.x;
RA Simpson R.J., Moritz R.L., Nice E.C., Grego B., Yoshizaki F., Sugimura Y.,
RA Freeman H.C., Murata M.;
RT "Complete amino acid sequence of plastocyanin from a green alga,
RT Enteromorpha prolifera.";
RL Eur. J. Biochem. 157:497-506(1986).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH COPPER, FUNCTION,
RP COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=2308169; DOI=10.1016/0022-2836(90)90269-r;
RA Collyer C.A., Guss J.M., Sugimura Y., Yoshizaki F., Freeman H.C.;
RT "Crystal structure of plastocyanin from a green alga, Enteromorpha
RT prolifera.";
RL J. Mol. Biol. 211:617-632(1990).
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I. {ECO:0000269|PubMed:2308169}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:2308169};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:2308169, ECO:0000269|PubMed:3522227}; Peripheral
CC membrane protein {ECO:0000269|PubMed:2308169}; Lumenal side
CC {ECO:0000269|PubMed:2308169}. Note=Loosely bound to the inner thylakoid
CC membrane surface in chloroplasts (PubMed:2308169).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR PIR; A25055; CUEI.
DR PDB; 7PCY; X-ray; 1.80 A; A=1-98.
DR PDBsum; 7PCY; -.
DR AlphaFoldDB; P07465; -.
DR SMR; P07465; -.
DR EvolutionaryTrace; P07465; -.
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 3D-structure; Chloroplast; Copper; Direct protein sequencing;
KW Electron transport; Membrane; Metal-binding; Plastid; Thylakoid; Transport.
FT CHAIN 1..98
FT /note="Plastocyanin"
FT /id="PRO_0000085566"
FT DOMAIN 1..98
FT /note="Plastocyanin-like"
FT BINDING 38
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:2308169"
FT BINDING 83
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:2308169"
FT BINDING 86
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:2308169"
FT BINDING 91
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:2308169"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:7PCY"
FT STRAND 13..23
FT /evidence="ECO:0007829|PDB:7PCY"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:7PCY"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7PCY"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:7PCY"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:7PCY"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:7PCY"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:7PCY"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:7PCY"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7PCY"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:7PCY"
SQ SEQUENCE 98 AA; 10114 MW; 505FFABF0968C47F CRC64;
AAIVKLGGDD GSLAFVPNNI TVGAGESIEF INNAGFPHNI VFDEDAVPAG VDADAISAED
YLNSKGQTVV RKLTTPGTYG VYCDPHSGAG MKMTITVQ
