PLAS_SPIOL
ID PLAS_SPIOL Reviewed; 168 AA.
AC P00289;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Plastocyanin, chloroplastic;
DE Flags: Precursor;
GN Name=PETE;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2834087; DOI=10.1007/bf00420603;
RA Rother C., Jansen T., Tyagi A., Tittgen J., Herrmann R.G.;
RT "Plastocyanin is encoded by an uninterrupted nuclear gene in spinach.";
RL Curr. Genet. 11:171-176(1986).
RN [2]
RP PROTEIN SEQUENCE OF 70-168, AND SUBCELLULAR LOCATION.
RX PubMed=1180895; DOI=10.1042/bj1470343;
RA Scawen M.D., Ramshaw J.A.M., Boulter D.;
RT "The amino acid sequence of plastocyanin from spinach. (Spinacia oleracea
RT L.).";
RL Biochem. J. 147:343-349(1975).
RN [3]
RP PROTEIN SEQUENCE OF 70-76, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf;
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [4]
RP STRUCTURE BY NMR, AND SUBCELLULAR LOCATION.
RX PubMed=9551554; DOI=10.1016/s0969-2126(98)00035-5;
RA Ubbink M., Ejdebaeck M., Karlsson B.G., Bendall D.S.;
RT "The structure of the complex of plastocyanin and cytochrome f, determined
RT by paramagnetic NMR and restrained rigid-body molecular dynamics.";
RL Structure 6:323-335(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 70-168 IN COMPLEX WITH COPPER,
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=9792096; DOI=10.1002/pro.5560071006;
RA Xue Y., Okvist M., Hansson O., Young S.;
RT "Crystal structure of spinach plastocyanin at 1.7-A resolution.";
RL Protein Sci. 7:2099-2105(1998).
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I. {ECO:0000269|PubMed:9792096}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:9792096};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:1180895,
CC ECO:0000269|PubMed:9551554, ECO:0000269|PubMed:9792096}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11719511,
CC ECO:0000269|PubMed:1180895, ECO:0000269|PubMed:9551554,
CC ECO:0000269|PubMed:9792096}; Lumenal side {ECO:0000269|PubMed:11719511,
CC ECO:0000269|PubMed:1180895, ECO:0000269|PubMed:9551554,
CC ECO:0000269|PubMed:9792096}. Note=Loosely bound to the inner thylakoid
CC membrane surface in chloroplasts (PubMed:9551554, PubMed:9792096).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR EMBL; X04693; CAA28398.1; -; Genomic_DNA.
DR PIR; S00446; CUSP.
DR PDB; 1AG6; X-ray; 1.60 A; A=70-168.
DR PDB; 1OOW; X-ray; 2.00 A; A=70-168.
DR PDB; 1TEF; X-ray; 1.90 A; A/B=70-168.
DR PDB; 1TEG; X-ray; 1.96 A; A/B=70-168.
DR PDB; 1YLB; NMR; -; B=70-168.
DR PDB; 2PCF; NMR; -; A=70-168.
DR PDBsum; 1AG6; -.
DR PDBsum; 1OOW; -.
DR PDBsum; 1TEF; -.
DR PDBsum; 1TEG; -.
DR PDBsum; 1YLB; -.
DR PDBsum; 2PCF; -.
DR AlphaFoldDB; P00289; -.
DR BMRB; P00289; -.
DR SMR; P00289; -.
DR IntAct; P00289; 1.
DR MINT; P00289; -.
DR OrthoDB; 1543670at2759; -.
DR BioCyc; MetaCyc:MON-4821; -.
DR EvolutionaryTrace; P00289; -.
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..?
FT /note="Chloroplast"
FT TRANSIT ?..69
FT /note="Thylakoid"
FT CHAIN 70..168
FT /note="Plastocyanin, chloroplastic"
FT /id="PRO_0000002897"
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:9792096"
FT BINDING 153
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:9792096"
FT BINDING 156
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:9792096"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:9792096"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1AG6"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:1YLB"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1AG6"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1AG6"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1YLB"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2PCF"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1AG6"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:1AG6"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2PCF"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1AG6"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1AG6"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1AG6"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:1AG6"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1AG6"
SQ SEQUENCE 168 AA; 16917 MW; F9AAA77D7EFCDBE0 CRC64;
MATVASSAAV AVPSFTGLKA SGSIKPTTAK IIPTTTAVPR LSVKASLKNV GAAVVATAAA
GLLAGNAMAV EVLLGGGDGS LAFLPGDFSV ASGEEIVFKN NAGFPHNVVF DEDEIPSGVD
AAKISMSEED LLNAPGETYK VTLTEKGTYK FYCSPHQGAG MVGKVTVN
