PLAS1_POPNI
ID PLAS1_POPNI Reviewed; 168 AA.
AC P00299;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Plastocyanin A, chloroplastic;
DE Short=PCa;
DE Flags: Precursor;
GN Name=PETE;
OS Populus nigra (Lombardy poplar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3691;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Italica; TISSUE=Leaf;
RA Reichert J., Jenzelewski V., Haehnel W.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 70-168, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Italica;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 70-168, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=6698995; DOI=10.2210/pdb2pcy/pdb;
RA Garrett T.P.J., Clingeleffer D.J., Guss J.M., Rogers S.J., Freeman H.C.;
RT "The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The
RT geometry of the copper-binding site is created by the polypeptide.";
RL J. Biol. Chem. 259:2822-2825(1984).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBCELLULAR LOCATION.
RX PubMed=6620385; DOI=10.1016/s0022-2836(83)80064-3;
RA Guss J.M., Freeman H.C.;
RT "Structure of oxidized poplar plastocyanin at 1.6-A resolution.";
RL J. Mol. Biol. 169:521-563(1983).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND SUBCELLULAR LOCATION.
RA Colman P.M., Freeman H.C., Guss J.M., Murata M., Norris V.A.,
RA Ramshaw J.A.M., Venkatappa M.P.;
RT "X-ray crystal structure analysis of plastocyanin at 2.7-A resolution.";
RL Nature 272:319-324(1978).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 70-168 IN COMPLEX WITH COPPER,
RP COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=1492962; DOI=10.1107/s0108768192004270;
RA Guss J.M., Bartunik H.D., Freeman H.C.;
RT "Accuracy and precision in protein structure analysis: restrained least-
RT squares refinement of the structure of poplar plastocyanin at 1.33 A
RT resolution.";
RL Acta Crystallogr. B 48:790-811(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) OF 70-168 IN COMPLEX WITH COPPER,
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Italica;
RX PubMed=22883960; DOI=10.1016/j.jinorgbio.2012.07.015;
RA Kachalova G.S., Shosheva A.C., Bourenkov G.P., Donchev A.A., Dimitrov M.I.,
RA Bartunik H.D.;
RT "Structural comparison of the poplar plastocyanin isoforms PCa and PCb
RT sheds new light on the role of the copper site geometry in interactions
RT with redox partners in oxygenic photosynthesis.";
RL J. Inorg. Biochem. 115:174-181(2012).
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I. {ECO:0000269|PubMed:22883960,
CC ECO:0000269|PubMed:6698995}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:1492962, ECO:0000269|PubMed:22883960};
CC Note=The crystal structure with reduced Cu(1+) has also been determined
CC (PubMed:22883960).;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:1492962, ECO:0000269|PubMed:22883960,
CC ECO:0000269|PubMed:6620385, ECO:0000269|PubMed:6698995,
CC ECO:0000269|Ref.5}; Peripheral membrane protein
CC {ECO:0000269|PubMed:1492962, ECO:0000269|PubMed:22883960,
CC ECO:0000269|PubMed:6620385, ECO:0000269|PubMed:6698995,
CC ECO:0000269|Ref.5}; Lumenal side {ECO:0000269|PubMed:1492962,
CC ECO:0000269|PubMed:22883960, ECO:0000269|PubMed:6620385,
CC ECO:0000269|PubMed:6698995, ECO:0000269|Ref.5}. Note=Loosely bound to
CC the inner thylakoid membrane surface in chloroplasts (PubMed:6698995,
CC PubMed:6620385, Ref.5, PubMed:1492962, PubMed:22883960).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR EMBL; Z50185; CAA90564.1; -; mRNA.
DR PIR; S58209; CUPX.
DR PDB; 1JXG; X-ray; 1.60 A; A/B=70-168.
DR PDB; 1PLC; X-ray; 1.33 A; A=70-168.
DR PDB; 1PNC; X-ray; 1.60 A; A=70-168.
DR PDB; 1PND; X-ray; 1.60 A; A=70-168.
DR PDB; 1TKW; NMR; -; A=70-168.
DR PDB; 2PCY; X-ray; 1.80 A; A=70-168.
DR PDB; 3PCY; X-ray; 1.90 A; A=70-168.
DR PDB; 4DP7; X-ray; 1.08 A; X=70-168.
DR PDB; 4DP8; X-ray; 1.07 A; X=70-168.
DR PDB; 4DP9; X-ray; 1.00 A; X=70-168.
DR PDB; 4DPA; X-ray; 1.05 A; X=70-168.
DR PDB; 4DPB; X-ray; 1.00 A; X=70-168.
DR PDB; 4DPC; X-ray; 1.06 A; X=70-168.
DR PDB; 4PCY; X-ray; 2.15 A; A=70-168.
DR PDB; 5PCY; X-ray; 1.80 A; A=70-168.
DR PDB; 6PCY; X-ray; 1.90 A; A=70-168.
DR PDBsum; 1JXG; -.
DR PDBsum; 1PLC; -.
DR PDBsum; 1PNC; -.
DR PDBsum; 1PND; -.
DR PDBsum; 1TKW; -.
DR PDBsum; 2PCY; -.
DR PDBsum; 3PCY; -.
DR PDBsum; 4DP7; -.
DR PDBsum; 4DP8; -.
DR PDBsum; 4DP9; -.
DR PDBsum; 4DPA; -.
DR PDBsum; 4DPB; -.
DR PDBsum; 4DPC; -.
DR PDBsum; 4PCY; -.
DR PDBsum; 5PCY; -.
DR PDBsum; 6PCY; -.
DR AlphaFoldDB; P00299; -.
DR BMRB; P00299; -.
DR SMR; P00299; -.
DR EvolutionaryTrace; P00299; -.
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;
KW Transit peptide; Transport.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 70..168
FT /note="Plastocyanin A, chloroplastic"
FT /id="PRO_0000002893"
FT DOMAIN 70..168
FT /note="Plastocyanin-like"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1492962,
FT ECO:0000269|PubMed:22883960"
FT BINDING 153
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1492962,
FT ECO:0000269|PubMed:22883960"
FT BINDING 156
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1492962,
FT ECO:0000269|PubMed:22883960"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:1492962,
FT ECO:0000269|PubMed:22883960"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4DP9"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:4DP9"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:4DP9"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1JXG"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4DP9"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:4DP9"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4DP9"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4DP9"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:4DP9"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:4DP9"
SQ SEQUENCE 168 AA; 17020 MW; 901B21A7573DBF82 CRC64;
MATVTSAAVS IPSFTGLKAG SASNAKVSAS AKVSASPLPR LSIKASMKDV GAAVVATAAS
AMIASNAMAI DVLLGADDGS LAFVPSEFSI SPGEKIVFKN NAGFPHNIVF DEDSIPSGVD
ASKISMSEED LLNAKGETFE VALSNKGEYS FYCSPHQGAG MVGKVTVN
