PLAS_CHLRE
ID PLAS_CHLRE Reviewed; 145 AA.
AC P18068;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Plastocyanin, chloroplastic;
DE AltName: Full=PC6-2;
DE Flags: Precursor;
GN Name=PETE;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=2137;
RX PubMed=2165059; DOI=10.1016/s0021-9258(19)38356-5;
RA Merchant S., Hill K., Kim J.H., Thompson J., Zaitlin D., Bogorad L.;
RT "Isolation and characterization of a complementary DNA clone for an algal
RT pre-apoplastocyanin.";
RL J. Biol. Chem. 265:12372-12379(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8463310; DOI=10.1016/s0021-9258(18)53033-7;
RA Quinn J., Li H.H., Singer J., Morimoto B., Mets L., Kindle K., Merchant S.;
RT "The plastocyanin-deficient phenotype of Chlamydomonas reinhardtii Ac-208
RT results from a frame-shift mutation in the nuclear gene encoding
RT preapoplastocyanin.";
RL J. Biol. Chem. 268:7832-7841(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 48-145 IN COMPLEX WITH COPPER,
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=8399201; DOI=10.1021/bi00091a005;
RA Redinbo M.R., Cascio D., Choukair M.K., Rice D., Merchant S., Yeates T.O.;
RT "The 1.5-A crystal structure of plastocyanin from the green alga
RT Chlamydomonas reinhardtii.";
RL Biochemistry 32:10560-10567(1993).
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I. {ECO:0000269|PubMed:8399201}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:8399201};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:8399201}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8399201}; Lumenal side
CC {ECO:0000269|PubMed:8399201}. Note=Loosely bound to the inner thylakoid
CC membrane surface in chloroplasts (PubMed:8399201).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR EMBL; J05524; AAA33078.1; -; mRNA.
DR EMBL; L07282; AAA33089.1; -; Genomic_DNA.
DR PIR; A36569; A36569.
DR RefSeq; XP_001702952.1; XM_001702900.1.
DR PDB; 2PLT; X-ray; 1.50 A; A=48-145.
DR PDBsum; 2PLT; -.
DR AlphaFoldDB; P18068; -.
DR SMR; P18068; -.
DR BioGRID; 988265; 1.
DR STRING; 3055.EDO96805; -.
DR ProMEX; P18068; -.
DR EnsemblPlants; PNW85356; PNW85356; CHLRE_03g182551v5.
DR GeneID; 5728459; -.
DR Gramene; PNW85356; PNW85356; CHLRE_03g182551v5.
DR KEGG; cre:CHLRE_03g182551v5; -.
DR eggNOG; ENOG502RXIY; Eukaryota.
DR HOGENOM; CLU_084115_0_0_1; -.
DR OMA; LGFFPNK; -.
DR OrthoDB; 1543670at2759; -.
DR EvolutionaryTrace; P18068; -.
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..47
FT /note="Chloroplast"
FT CHAIN 48..145
FT /note="Plastocyanin, chloroplastic"
FT /id="PRO_0000002886"
FT DOMAIN 48..145
FT /note="Plastocyanin-like"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:8399201"
FT BINDING 130
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:8399201"
FT BINDING 133
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:8399201"
FT BINDING 138
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:8399201"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:2PLT"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:2PLT"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2PLT"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2PLT"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2PLT"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:2PLT"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2PLT"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2PLT"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2PLT"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:2PLT"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:2PLT"
SQ SEQUENCE 145 AA; 14875 MW; 7E4454E4B942A779 CRC64;
MKATLRAPAS RASAVRPVAS LKAAAQRVAS VAGVSVASLA LTLAAHADAT VKLGADSGAL
EFVPKTLTIK SGETVNFVNN AGFPHNIVFD EDAIPSGVNA DAISRDDYLN APGETYSVKL
TAAGEYGYYC EPHQGAGMVG KIIVQ
