C7091_ARATH
ID C7091_ARATH Reviewed; 519 AA.
AC Q9ASR3; O80728;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cytochrome P450 709B1 {ECO:0000305};
DE EC=1.14.-.- {ECO:0000305};
GN Name=CYP709B1 {ECO:0000303|PubMed:15280363};
GN OrderedLocusNames=At2g46960 {ECO:0000312|Araport:AT2G46960};
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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, 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9ASR3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in siliques.
CC {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}.
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DR EMBL; AC004411; AAC34227.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10778.1; -; Genomic_DNA.
DR EMBL; AF367329; AAK32916.1; -; mRNA.
DR EMBL; AY091688; AAM10287.1; -; mRNA.
DR PIR; T02191; T02191.
DR RefSeq; NP_566092.1; NM_130264.2. [Q9ASR3-1]
DR AlphaFoldDB; Q9ASR3; -.
DR SMR; Q9ASR3; -.
DR STRING; 3702.AT2G46960.2; -.
DR PaxDb; Q9ASR3; -.
DR PRIDE; Q9ASR3; -.
DR ProteomicsDB; 240265; -. [Q9ASR3-1]
DR EnsemblPlants; AT2G46960.2; AT2G46960.2; AT2G46960. [Q9ASR3-1]
DR GeneID; 819310; -.
DR Gramene; AT2G46960.2; AT2G46960.2; AT2G46960. [Q9ASR3-1]
DR KEGG; ath:AT2G46960; -.
DR Araport; AT2G46960; -.
DR TAIR; locus:2041389; AT2G46960.
DR eggNOG; KOG0157; Eukaryota.
DR InParanoid; Q9ASR3; -.
DR OMA; GMYMFFK; -.
DR PhylomeDB; Q9ASR3; -.
DR BioCyc; ARA:AT2G46960-MON; -.
DR PRO; PR:Q9ASR3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ASR3; 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 Alternative splicing; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..519
FT /note="Cytochrome P450 709B1"
FT /id="PRO_0000435386"
FT TRANSMEM 1..21
FT /note="Helical"
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|UniProtKB:P04798"
SQ SEQUENCE 519 AA; 59604 MW; 3B053C83F917457A CRC64;
MGLVIFLALI VLILIIGLRI FKAFMILVWH PFVLTRRLKN QGISGPNYRI FYGNLSEIKK
MKRESHLSIL DPSSNDIFPR ILPHYQKWMS QYGETFLYWN GTEPRICISD PELAKTMLSN
KLGFFVKSKA RPEAVKLVGS KGLVFIEGAD WVRHRRILNP AFSIDRLKIM TTVMVDCTLK
MLEEWRKEST KEETEHPKIK KEMNEEFQRL TADIIATSAF GSSYVEGIEV FRSQMELKRC
YTTSLNQVSI PGTQYLPTPS NIRVWKLERK MDNSIKRIIS SRLQSKSDYG DDLLGILLKA
YNTEGKERKM SIEEIIHECR TFFFGGHETT SNLLAWTTML LSLHQDWQEK LREEIFKECG
KEKTPDSETF SKLKLMNMVI MESLRLYGPV SALAREASVN IKLGDLEIPK GTTVVIPLLK
MHSDKTLWGS DADKFNPMRF ANGVSRAANH PNALLAFSVG PRACIGQNFV MIEAKTVLTM
ILQRFRFISL CDEYKHTPVD NVTIQPQYGL PVMLQPLED
