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PST2_PETHY
ID   PST2_PETHY              Reviewed;         106 AA.
AC   B3EWI4;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Photosystem II 5 kDa protein, chloroplastic {ECO:0000303|PubMed:22700981};
DE   Flags: Precursor;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root {ECO:0000269|PubMed:21143680};
RX   PubMed=21143680; DOI=10.1111/j.1365-313x.2010.04385.x;
RA   Breuillin F., Schramm J., Hajirezaei M., Ahkami A., Favre P., Druege U.,
RA   Hause B., Bucher M., Kretzschmar T., Bossolini E., Kuhlemeier C.,
RA   Martinoia E., Franken P., Scholz U., Reinhardt D.;
RT   "Phosphate systemically inhibits development of arbuscular mycorrhiza in
RT   Petunia hybrida and represses genes involved in mycorrhizal functioning.";
RL   Plant J. 64:1002-1017(2010).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 77-106, TISSUE SPECIFICITY, DISULFIDE BOND, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Leaf {ECO:0000269|PubMed:22700981};
RX   PubMed=22700981; DOI=10.1074/jbc.m112.370841;
RA   Poth A.G., Mylne J.S., Grassl J., Lyons R.E., Millar A.H., Colgrave M.L.,
RA   Craik D.J.;
RT   "Cyclotides associate with leaf vasculature and are the products of a novel
RT   precursor in Petunia (Solanaceae).";
RL   J. Biol. Chem. 287:27033-27046(2012).
CC   -!- FUNCTION: May be a component of the oxygen-evolving complex.
CC       {ECO:0000250|UniProtKB:P31336}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250|UniProtKB:P31336}. Note=Associated with the photosystem II
CC       complex. {ECO:0000250|UniProtKB:P31336}.
CC   -!- TISSUE SPECIFICITY: Expressed in midvein, lamina and periphery of
CC       leaves (at protein level). {ECO:0000269|PubMed:22700981}.
CC   -!- PTM: Disulfide bond. {ECO:0000269|PubMed:22700981}.
CC   -!- MASS SPECTROMETRY: Mass=3424.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22700981};
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DR   EMBL; FN008610; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3EWI4; -.
DR   SMR; B3EWI4; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   InterPro; IPR040296; PSBT.
DR   PANTHER; PTHR34940; PTHR34940; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Disulfide bond; Membrane;
KW   Photosynthesis; Photosystem II; Plastid; Thylakoid; Transit peptide.
FT   TRANSIT         1..76
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:22700981"
FT   CHAIN           77..106
FT                   /note="Photosystem II 5 kDa protein, chloroplastic"
FT                   /evidence="ECO:0000269|PubMed:22700981"
FT                   /id="PRO_0000419345"
FT   DISULFID        95..104
FT                   /evidence="ECO:0000269|PubMed:22700981"
SQ   SEQUENCE   106 AA;  11317 MW;  7E1A8588BFB0001B CRC64;
     MASITMMSSF LGGSTVAPAK VPSANRRGVV MVKAMHEGEN NVVISKNEES KNSGRRELFF
     AMAAAAACSV AKTAMADEEP KRGTPEAKKK YSSVCVTNPT ARICRY
 
 
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