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C14B3_MAIZE
ID   C14B3_MAIZE             Reviewed;         527 AA.
AC   B6SSW8; C0PEU9;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Cytochrome P450 714B3;
DE            EC=1.14.-.-;
GN   Name=CYP714B3;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 154-527.
RC   STRAIN=cv. B73;
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=19951895; DOI=10.1186/1479-7364-4-1-59;
RA   Nelson D.R.;
RT   "The cytochrome p450 homepage.";
RL   Hum. Genomics 4:59-65(2009).
CC   -!- FUNCTION: May be involved in gibberellin metabolism. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACN33715.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; EU955833; ACG27951.1; -; mRNA.
DR   EMBL; BT066818; ACN33715.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001169426.1; NM_001175955.1.
DR   AlphaFoldDB; B6SSW8; -.
DR   SMR; B6SSW8; -.
DR   STRING; 4577.GRMZM2G106408_P01; -.
DR   PaxDb; B6SSW8; -.
DR   PRIDE; B6SSW8; -.
DR   GeneID; 100383295; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; B6SSW8; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..527
FT                   /note="Cytochrome P450 714B3"
FT                   /id="PRO_0000422414"
FT   TOPO_DOM        1..14
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..527
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         464
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        417
FT                   /note="N -> S (in Ref. 2; ACN33715)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   527 AA;  58709 MW;  EF3CE4882E2ED271 CRC64;
     MEVAMAMAVK VLLSLCCVGA CGLAVYLYHI LWLVPQKVLA KFEDQKIGGP RPSFPYGNLA
     DMREAAAAAK AARASARRSG SGGGGIVHDY RPAVLPYYEK WRKEYGPIFT YSMGNVVFLH
     VSRPDVVRDI NLCVSLDLGK SSYLKATHEP LFGGGILKSN GEAWLHQRKI IAPEFFLDKV
     KGMVDLMVDS AQPLLMSWEE RVDRNGGITD IKIDDDIRAY SADVISRTCF GSSYIKGKEI
     FMKIRELQQA VSKPNVLAEM TGLRFFPSMR NKQAWELHKQ VRKLILEIVK ESGEDRNLLS
     AILHSASTSR VGIAEAENFI VDNCKSIYFA GHESTAVTAA WCLMLLGLHP EWQNRVREEV
     HEVCRGQPVD SRSLQKMKNL TMVIQETLRL YPAGAFVSRQ ALQELKLGGV HIPKGVNIYI
     PVSTMHLDPE LWGPDVKEFN PERFSDVRPQ LHSYLPFGAG ARTCLGQGFA MAELKILISL
     IVSKFVLKLS PHYQHSPTLK LIVEPELGVD LTLTKVQSVC TKRGTAI
 
 
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