THAH_ARATH
ID THAH_ARATH Reviewed; 477 AA.
AC Q8L7D5; B9DGZ3; Q3E8E7; Q3E8E8; Q9FI38;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cytochrome P450 708A2;
DE EC=1.14.-.-;
DE AltName: Full=Thalianol hydroxylase;
DE Short=AtTHAH;
GN Name=CYP708A2; Synonyms=THAH; OrderedLocusNames=At5g48000;
GN ORFNames=MDN11.7;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18356490; DOI=10.1126/science.1154990;
RA Field B., Osbourn A.E.;
RT "Metabolic diversification -- independent assembly of operon-like gene
RT clusters in different plants.";
RL Science 320:543-547(2008).
CC -!- FUNCTION: Hydroxylates thalianol into thalian-diol.
CC {ECO:0000269|PubMed:18356490}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q8L7D5-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8L7D5-1; Sequence=VSP_038052;
CC -!- TISSUE SPECIFICITY: Expressed primarily in the root epidermis.
CC {ECO:0000269|PubMed:18356490}.
CC -!- DISRUPTION PHENOTYPE: Increased levels of thalianol in roots.
CC {ECO:0000269|PubMed:18356490}.
CC -!- MISCELLANEOUS: Constitutes with three contiguous genes an operon-like
CC gene cluster that is involved in the thalianol pathway.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB017064; BAB11064.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95604.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95605.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95607.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95608.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68581.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68582.1; -; Genomic_DNA.
DR EMBL; AY136329; AAM96995.1; -; mRNA.
DR EMBL; BT000124; AAN15443.1; -; mRNA.
DR EMBL; AK317336; BAH20010.1; -; mRNA.
DR RefSeq; NP_001032030.1; NM_001036953.1. [Q8L7D5-2]
DR RefSeq; NP_001078732.1; NM_001085263.2. [Q8L7D5-2]
DR RefSeq; NP_001318756.1; NM_001344755.1. [Q8L7D5-2]
DR RefSeq; NP_001330320.1; NM_001344756.1. [Q8L7D5-2]
DR RefSeq; NP_199611.2; NM_124174.3. [Q8L7D5-2]
DR RefSeq; NP_851152.1; NM_180821.3.
DR RefSeq; NP_851153.1; NM_180822.2. [Q8L7D5-2]
DR AlphaFoldDB; Q8L7D5; -.
DR SMR; Q8L7D5; -.
DR BioGRID; 20099; 1.
DR STRING; 3702.AT5G48000.1; -.
DR PaxDb; Q8L7D5; -.
DR PRIDE; Q8L7D5; -.
DR ProteomicsDB; 234231; -. [Q8L7D5-2]
DR EnsemblPlants; AT5G48000.2; AT5G48000.2; AT5G48000. [Q8L7D5-2]
DR EnsemblPlants; AT5G48000.3; AT5G48000.3; AT5G48000. [Q8L7D5-2]
DR EnsemblPlants; AT5G48000.4; AT5G48000.4; AT5G48000. [Q8L7D5-2]
DR EnsemblPlants; AT5G48000.5; AT5G48000.5; AT5G48000. [Q8L7D5-2]
DR EnsemblPlants; AT5G48000.6; AT5G48000.6; AT5G48000. [Q8L7D5-2]
DR EnsemblPlants; AT5G48000.7; AT5G48000.7; AT5G48000. [Q8L7D5-2]
DR GeneID; 834851; -.
DR Gramene; AT5G48000.2; AT5G48000.2; AT5G48000. [Q8L7D5-2]
DR Gramene; AT5G48000.3; AT5G48000.3; AT5G48000. [Q8L7D5-2]
DR Gramene; AT5G48000.4; AT5G48000.4; AT5G48000. [Q8L7D5-2]
DR Gramene; AT5G48000.5; AT5G48000.5; AT5G48000. [Q8L7D5-2]
DR Gramene; AT5G48000.6; AT5G48000.6; AT5G48000. [Q8L7D5-2]
DR Gramene; AT5G48000.7; AT5G48000.7; AT5G48000. [Q8L7D5-2]
DR KEGG; ath:AT5G48000; -.
DR Araport; AT5G48000; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q8L7D5; -.
DR OMA; WIRSPFA; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; Q8L7D5; -.
DR BioCyc; MetaCyc:AT5G48000-MON; -.
DR PRO; PR:Q8L7D5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7D5; baseline and differential.
DR Genevisible; Q8L7D5; AT.
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:0016491; F:oxidoreductase 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 GO; GO:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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; Transmembrane; Transmembrane helix.
FT CHAIN 1..477
FT /note="Cytochrome P450 708A2"
FT /id="PRO_0000366941"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 426
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 VAR_SEQ 1
FT /note="M -> MDRRGKYWAGPMWIGLSMCGSGSDTILECRLRLFKLQRQNQ (in
FT isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_038052"
FT CONFLICT 152
FT /note="E -> G (in Ref. 4; BAH20010)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="E -> D (in Ref. 3; AAN15443/AAM96995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 54092 MW; 57927B391D8A767C CRC64;
MSFVWSAAVW VIAVAAVVIS KWLYRWSNPK CNGKLPPGSM GLPIIGETCD FFEPHGLYEI
SPFVKKRMLK YGPLFRTNIF GSNTVVLTEP DIIFEVFRQE NKSFVFSYPE AFVKPFGKEN
VFLKHGNIHK HVKQISLQHL GSEALKKKMI GEIDRVTYEH LRSKANQGSF DAKEAVESVI
MAHLTPKIIS NLKPETQATL VDNIMALGSE WFQSPLKLTT LISIYKVFIA RRYALQVIKD
VFTRRKASRE MCGDFLDTMV EEGEKEDVIF NEESAINLIF AILVVAKEST SSVTSLAIKF
LAENHKALAE LKREHAAILQ NRNGKGAGVS WEEYRHQMTF TNMVINETLR MANMAPIMYR
KAVNDVEIKG YTIPAGWIVA VIPPAVHFND AIYENPLEFN PWRWEGKELR SGSKTFMVFG
GGVRQCVGAE FARLQISIFI HHLVTTYDFS LAQESEFIRA PLPYFPKGLP IKISQSL
