PLAS_PEA
ID PLAS_PEA Reviewed; 168 AA.
AC P16002;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Plastocyanin, chloroplastic;
DE Flags: Precursor;
GN Name=PETE;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Feltham First; TISSUE=Shoot;
RA Last D.I., Gray J.C.;
RT "Plastocyanin is encoded by a single-copy gene in the pea haploid genome.";
RL Plant Mol. Biol. 12:655-666(1989).
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I.
CC {ECO:0000250|UniProtKB:P18068}.
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:0000250|UniProtKB:P18068}; 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 EMBL; X16082; CAA34212.1; -; Genomic_DNA.
DR PIR; S04861; S04861.
DR PDB; 6YEZ; EM; 2.70 A; P=70-168.
DR PDB; 6ZOO; EM; 2.74 A; P=70-168.
DR PDBsum; 6YEZ; -.
DR PDBsum; 6ZOO; -.
DR AlphaFoldDB; P16002; -.
DR SMR; P16002; -.
DR DIP; DIP-631N; -.
DR IntAct; P16002; 1.
DR MINT; P16002; -.
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; Electron transport; Membrane;
KW Metal-binding; Plastid; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT CHAIN 70..168
FT /note="Plastocyanin, chloroplastic"
FT /id="PRO_0000002891"
FT DOMAIN 70..168
FT /note="Plastocyanin-like"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT BINDING 153
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT BINDING 156
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P18068"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6YEZ"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6YEZ"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:6YEZ"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6YEZ"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6ZOO"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:6YEZ"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6YEZ"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6YEZ"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:6YEZ"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:6YEZ"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6YEZ"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:6YEZ"
SQ SEQUENCE 168 AA; 17154 MW; E2B2F6B7094FDF43 CRC64;
MATVTSTTVA IPSFSGLKTN AATKVSAMAK IPTSTSQSPR LCVRASLKDF GVALVATAAS
AVLASNALAV EVLLGASDGG LAFVPSSLEV SAGETIVFKN NAGFPHNVVF DEDEIPAGVD
ASKISMPEED LLNAPGETYS VKLDAKGTYK FYCSPHQGAG MVGQVTVN