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C70B2_ARATH
ID   C70B2_ARATH             Reviewed;         572 AA.
AC   F4IK45; O80729;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cytochrome P450 709B2 {ECO:0000305};
DE            EC=1.14.-.- {ECO:0000305};
GN   Name=CYP709B2 {ECO:0000303|PubMed:15280363};
GN   OrderedLocusNames=At2g46950 {ECO:0000312|Araport:AT2G46950};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-572 AND 55-572.
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=15280363; DOI=10.1074/jbc.m406337200;
RA   Takei K., Yamaya T., Sakakibara H.;
RT   "Arabidopsis CYP735A1 and CYP735A2 encode cytokinin hydroxylases that
RT   catalyze the biosynthesis of trans-Zeatin.";
RL   J. Biol. Chem. 279:41866-41872(2004).
RN   [5]
RP   TISSUE SPECIFICITY, INDUCTION BY SALT STRESS, AND DISRUPTION PHENOTYPE.
RX   PubMed=24164720; DOI=10.1186/1471-2229-13-169;
RA   Mao G., Seebeck T., Schrenker D., Yu O.;
RT   "CYP709B3, a cytochrome P450 monooxygenase gene involved in salt tolerance
RT   in Arabidopsis thaliana.";
RL   BMC Plant Biol. 13:169-169(2013).
CC   -!- FUNCTION: Involved in stress response (By similarity). Does not
CC       function as cytokinin hydroxylase in yeast heterologous system
CC       (Probable). {ECO:0000250|UniProtKB:Q9T093,
CC       ECO:0000305|PubMed:15280363}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in siliques and at lower levels in
CC       flowers and rosette leaves. {ECO:0000269|PubMed:24164720}.
CC   -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:24164720}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:24164720}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-56 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC34228.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAS47631.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC004411; AAC34228.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002685; AEC10776.1; -; Genomic_DNA.
DR   EMBL; BT011625; AAS47631.1; ALT_INIT; mRNA.
DR   EMBL; BT014808; AAT41791.1; -; mRNA.
DR   PIR; T02192; T02192.
DR   RefSeq; NP_182218.2; NM_130263.3.
DR   AlphaFoldDB; F4IK45; -.
DR   SMR; F4IK45; -.
DR   STRING; 3702.AT2G46950.1; -.
DR   PaxDb; F4IK45; -.
DR   PRIDE; F4IK45; -.
DR   ProteomicsDB; 239118; -.
DR   EnsemblPlants; AT2G46950.1; AT2G46950.1; AT2G46950.
DR   GeneID; 819309; -.
DR   Gramene; AT2G46950.1; AT2G46950.1; AT2G46950.
DR   KEGG; ath:AT2G46950; -.
DR   Araport; AT2G46950; -.
DR   TAIR; locus:2041399; AT2G46950.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_5_0_1; -.
DR   InParanoid; F4IK45; -.
DR   OMA; CEEPHWL; -.
DR   OrthoDB; 825914at2759; -.
DR   PRO; PR:F4IK45; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; F4IK45; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
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; Stress response; Transmembrane; Transmembrane helix.
FT   CHAIN           1..572
FT                   /note="Cytochrome P450 709B2"
FT                   /id="PRO_0000435385"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         518
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|UniProtKB:P04798"
SQ   SEQUENCE   572 AA;  65229 MW;  7F30AE5E794890A2 CRC64;
     MLFCSVRILF IISSKQLVLI SETEVTTTLT LHTTHKIESP TANPPQSKKN LFVIRMELLS
     TINLLAIALV LLVVPKIYGA CRILVWRPWM LSRRFKKQGI SGPKYRILYG NLREIRKMKN
     EAKLMVLDPN SNDIVPRVLP HLQQWKSQYG ETFLYWQGTD PRLCISDHEL AKQILSNKFV
     FFSKSKTKPE ILKLSGNGLI FVNGLDWVRH RRILNPAFSM DKLKLMTQLM VDCTFRMFLE
     WKKQRNGVET EQFVLISREF KRLTADIIAT AAFGSSYAEG IEVFKSQLEL QKCCAAALTD
     LYFPGIQYLP TPSNLQIWKL DMKVNSSIKR IIDARLTSES KDYGNDLLGI MLTAASSNES
     EKKMSIDEII EECKTFFFAG HETTANLLTW STMLLSLHQD WQEKLREEVF NECGKDKIPD
     AETCSKLKLM NTVFMESLRL YGPVLNLLRL ASEDMKLGNL EIPKGTTIIL PIAKMHRDKA
     VWGSDADKFN PMRFANGLSR AANHPNALLA FSMGPRACIG QNFAIMEAKT VLAMILQRFR
     LNLSADYKHA PADHLTLQPQ YDLPVILEPI DG
 
 
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