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Database: UniProt
Entry: A0A2K1IZ72_PHYPA
LinkDB: A0A2K1IZ72_PHYPA
Original site: A0A2K1IZ72_PHYPA 
ID   A0A2K1IZ72_PHYPA        Unreviewed;       168 AA.
AC   A0A2K1IZ72;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Plastocyanin {ECO:0000256|RuleBase:RU363020};
GN   ORFNames=PHYPA_024401 {ECO:0000313|EMBL:PNR34584.1};
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 {ECO:0000313|EMBL:PNR34584.1};
RN   [1] {ECO:0000313|EMBL:PNR34584.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
RN   [2] {ECO:0000313|EMBL:PNR34584.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=29237241; DOI=10.1111/tpj.13801;
RA   Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA   Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA   Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA   Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA   Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA   Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA   Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA   Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA   Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA   Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA   Schmutz J., Rensing S.A.;
RT   "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT   structure and evolution.";
RL   Plant J. 93:515-533(2018).
CC   -!- FUNCTION: Participates in electron transfer between P700 and the
CC       cytochrome b6-f complex in photosystem I.
CC       {ECO:0000256|RuleBase:RU363020}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602387-1};
CC       Note=The crystal structure with reduced Cu(1+) has also been
CC       determined. {ECO:0000256|PIRSR:PIRSR602387-1};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|ARBA:ARBA00004622, ECO:0000256|RuleBase:RU363020};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004622,
CC       ECO:0000256|RuleBase:RU363020}; Lumenal side
CC       {ECO:0000256|ARBA:ARBA00004622, ECO:0000256|RuleBase:RU363020}.
CC   -!- SIMILARITY: Belongs to the plastocyanin family.
CC       {ECO:0000256|ARBA:ARBA00005338, ECO:0000256|RuleBase:RU363020}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNR34584.1}.
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DR   EMBL; ABEU02000019; PNR34584.1; -; Genomic_DNA.
DR   RefSeq; XP_001779258.1; XM_001779206.1.
DR   AlphaFoldDB; A0A2K1IZ72; -.
DR   SMR; A0A2K1IZ72; -.
DR   STRING; 3218.A0A2K1IZ72; -.
DR   Gramene; Pp3c19_21160V3.1; PAC:32939379.CDS.1; Pp3c19_21160.
DR   Gramene; Pp3c19_21160V3.2; PAC:32939380.CDS.1; Pp3c19_21160.
DR   OMA; YDYYCEP; -.
DR   OrthoDB; 471748at2759; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04219; Plastocyanin; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 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   NCBIfam; TIGR02656; cyanin_plasto; 1.
DR   PANTHER; PTHR34192; PLASTOCYANIN MAJOR ISOFORM, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR34192:SF10; PLASTOCYANIN MAJOR ISOFORM, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00127; Copper-bind; 1.
DR   PRINTS; PR00156; COPPERBLUE.
DR   PRINTS; PR00157; PLASTOCYANIN.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR602387-1};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU363020};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363020};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602387-1};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|RuleBase:RU363020};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363020}.
FT   DOMAIN          73..167
FT                   /note="Blue (type 1) copper"
FT                   /evidence="ECO:0000259|Pfam:PF00127"
FT   BINDING         108
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
FT   BINDING         153
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
FT   BINDING         156
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
FT   BINDING         161
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
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
//
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