PLAS_PHYPA
ID PLAS_PHYPA Reviewed; 168 AA.
AC Q9SXW9; A9TKV7;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Plastocyanin, chloroplastic;
DE Flags: Precursor;
GN Name=PETE; ORFNames=PHYPADRAFT_170637;
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kiyosue T., Wada M.;
RT "Three cDNA sequences for light inducible genes from Physcomitrella
RT patens.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
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; AB026687; BAA77274.1; -; mRNA.
DR EMBL; DS545143; EDQ55946.1; -; Genomic_DNA.
DR RefSeq; XP_001779258.1; XM_001779206.1.
DR AlphaFoldDB; Q9SXW9; -.
DR SMR; Q9SXW9; -.
DR STRING; 3218.PP1S254_25V6.1; -.
DR EnsemblPlants; Pp3c19_21160V3.1; PAC:32939379.CDS.1; Pp3c19_21160.
DR EnsemblPlants; Pp3c19_21160V3.2; PAC:32939380.CDS.1; Pp3c19_21160.
DR Gramene; Pp3c19_21160V3.1; PAC:32939379.CDS.1; Pp3c19_21160.
DR Gramene; Pp3c19_21160V3.2; PAC:32939380.CDS.1; Pp3c19_21160.
DR eggNOG; ENOG502RXIY; Eukaryota.
DR HOGENOM; CLU_084115_0_0_1; -.
DR OMA; YDYYCEP; -.
DR OrthoDB; 1543670at2759; -.
DR Proteomes; UP000006727; Chromosome 19.
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 Reference proteome; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 71..168
FT /note="Plastocyanin, chloroplastic"
FT /id="PRO_0000002892"
FT DOMAIN 71..168
FT /note="Plastocyanin-like"
FT BINDING 108
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 CONFLICT 12
FT /note="P -> S (in Ref. 1; BAA77274)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 17158 MW; A9DE8673D1E446CB CRC64;
MASVAAAAVS VPSFSGLKAE TKAAPARLSS TSVVRMAPVV RASASSDALK TVGKALLAAS
SSLLLVASAN AATVKMGGDD GALGFYPKDI SVAAGESVTF VNNKGFPHNV VFDEDAVPAG
VKTEDINHED YLNGPNESFS ITFKTPGTYE FYCEPHQGAG MKGVVTVS
