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PLAS_HORVU
ID   PLAS_HORVU              Reviewed;         155 AA.
AC   P08248;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Plastocyanin, chloroplastic;
DE   Flags: Precursor;
GN   Name=PETE;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Bomi;
RA   Nielsen O.S., Gausing K.;
RT   "The precursor of barley plastocyanin: sequence of cDNA clones and gene
RT   expression in different tissues.";
RL   FEBS Lett. 225:159-162(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. NK 1558;
RX   PubMed=8223592; DOI=10.1111/j.1432-1033.1993.tb18223.x;
RA   Nielsen P., Gausing K.;
RT   "In vitro binding of nuclear proteins to the barley plastocyanin gene
RT   promoter region.";
RL   Eur. J. Biochem. 217:97-104(1993).
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; Y00704; CAA68696.1; -; mRNA.
DR   EMBL; Z28347; CAA82201.1; -; Genomic_DNA.
DR   PIR; S38255; S38255.
DR   AlphaFoldDB; P08248; -.
DR   SMR; P08248; -.
DR   ExpressionAtlas; P08248; baseline and differential.
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   2: Evidence at transcript level;
KW   Chloroplast; Copper; Electron transport; Membrane; Metal-binding; Plastid;
KW   Thylakoid; Transit peptide; Transport.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT   CHAIN           59..155
FT                   /note="Plastocyanin, chloroplastic"
FT                   /id="PRO_0000002888"
FT   DOMAIN          59..155
FT                   /note="Plastocyanin-like"
FT   BINDING         95
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
FT   BINDING         140
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
FT   BINDING         143
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
FT   BINDING         148
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P18068"
FT   VARIANT         120
FT                   /note="T -> N (in strain: cv. NK 1558)"
SQ   SEQUENCE   155 AA;  15709 MW;  DAA7EABE5F6F4F91 CRC64;
     MAALSSAAVS VPSFAAATPM RSSRSSRMVV RASLGKKAAS AAVAMAAGAM LLGGSAMAQD
     VLLGANGGVL VFEPNDFSVK AGETITFKNN AGYPHNVVFD EDAVPSGVDV SKISQEEYLT
     APGETFSVTL TVPGTYGFYC EPHAGAGMVG KVTVN
 
 
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