C7104_ARATH
ID C7104_ARATH Reviewed; 493 AA.
AC Q9ZV28;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cytochrome P450 710A4 {ECO:0000303|PubMed:16531502};
DE EC=1.14.19.41 {ECO:0000250|UniProtKB:O64697};
DE AltName: Full=C-22 sterol desaturase {ECO:0000303|PubMed:16531502};
GN Name=CYP710A4 {ECO:0000303|PubMed:16531502};
GN OrderedLocusNames=At2g28860 {ECO:0000312|Araport:AT2G28860};
GN ORFNames=F8N16.15 {ECO:0000312|EMBL:AAC79590.1};
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=16531502; DOI=10.1105/tpc.105.036012;
RA Morikawa T., Mizutani M., Aoki N., Watanabe B., Saga H., Saito S.,
RA Oikawa A., Suzuki H., Sakurai N., Shibata D., Wadano A., Sakata K.,
RA Ohta D.;
RT "Cytochrome P450 CYP710A encodes the sterol C-22 desaturase in Arabidopsis
RT and tomato.";
RL Plant Cell 18:1008-1022(2006).
RN [5]
RP FUNCTION.
RX PubMed=17909855; DOI=10.1007/s00425-007-0618-8;
RA Arnqvist L., Persson M., Jonsson L., Dutta P.C., Sitbon F.;
RT "Overexpression of CYP710A1 and CYP710A4 in transgenic Arabidopsis plants
RT increases the level of stigmasterol at the expense of sitosterol.";
RL Planta 227:309-317(2008).
RN [6]
RP INDUCTION.
RX PubMed=20444228; DOI=10.1111/j.1365-313x.2010.04235.x;
RA Griebel T., Zeier J.;
RT "A role for beta-sitosterol to stigmasterol conversion in plant-pathogen
RT interactions.";
RL Plant J. 63:254-268(2010).
CC -!- FUNCTION: Required to form the C-22 double bond in the sterol side
CC chain. Possesses C-22 desaturase activity toward beta-sitosterol and
CC produces stigmasterol. {ECO:0000269|PubMed:17909855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-dehydroepisterol + H(+) + NADPH + O2 = ergosta-
CC 5,7,22,24(28)-tetraen-3beta-ol + 2 H2O + NADP(+);
CC Xref=Rhea:RHEA:33467, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:18249, ChEBI:CHEBI:52972,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.19.41;
CC Evidence={ECO:0000250|UniProtKB:O64697};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Steroid biosynthesis; sterol biosynthesis.
CC {ECO:0000269|PubMed:16531502}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Very weak expression in roots and root hairs. Not
CC detected in the root tips. {ECO:0000269|PubMed:16531502}.
CC -!- INDUCTION: Not induced by pathogen infection.
CC {ECO:0000269|PubMed:20444228}.
CC -!- MISCELLANEOUS: Plants overexpressing CYP710A4 show higher levels of
CC stigmasterol and lower levels of beta-sitosterol than the wild-type.
CC {ECO:0000269|PubMed:16531502}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX820851; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC005727; AAC79590.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08182.1; -; Genomic_DNA.
DR EMBL; BX820851; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; G84689; G84689.
DR RefSeq; NP_180452.1; NM_128445.3.
DR AlphaFoldDB; Q9ZV28; -.
DR SMR; Q9ZV28; -.
DR STRING; 3702.AT2G28860.1; -.
DR PaxDb; Q9ZV28; -.
DR PRIDE; Q9ZV28; -.
DR EnsemblPlants; AT2G28860.1; AT2G28860.1; AT2G28860.
DR GeneID; 817435; -.
DR Gramene; AT2G28860.1; AT2G28860.1; AT2G28860.
DR KEGG; ath:AT2G28860; -.
DR Araport; AT2G28860; -.
DR TAIR; locus:2053235; AT2G28860.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_023517_1_0_1; -.
DR InParanoid; Q9ZV28; -.
DR OMA; WVFLQGK; -.
DR OrthoDB; 574756at2759; -.
DR PhylomeDB; Q9ZV28; -.
DR BRENDA; 1.14.19.41; 399.
DR UniPathway; UPA00766; -.
DR PRO; PR:Q9ZV28; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZV28; baseline and differential.
DR Genevisible; Q9ZV28; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000249; F:C-22 sterol desaturase activity; IDA:UniProtKB.
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; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Monooxygenase; NADP; Oxidoreductase; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..493
FT /note="Cytochrome P450 710A4"
FT /id="PRO_0000411207"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 435
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 493 AA; 55690 MW; 3F68FAD1DDFD2C65 CRC64;
MVSSVSLFAS LTPYLVSALL LFLLLEQLFY RVKKRNLPGP LFVFPIIGNV VALIRDPTSF
WDKQSAMADT SVGLSVNYLI GKFIIYIKDA ELSNKVLSNI RPDAFQLTGH PFGKKLFGDH
SLIFMFGEDH KSVRRQVAPN FTRKPLSAYS SLQQIVILRH LRQWEESFSS GSRPVSMRQL
IRELNLETSQ TVFVGPYLDK EVKKTICDDY SLLTLGTMAI PIDLPGFTFG EARQAVSRLV
NTMSVCVGKS KAKMAAGENP TCLVDFWTHS IIEENPPPPH SKDKEISCVL VDFMFASQDA
STSSLLWAVV MLESEPEVLR RVREDVARFW SSESNELITA DQLAEMKYTR AVAREVLRYR
PPASMIPHVA VSDFRLTESY TIPKGTIVFP SLFDASFQGF TEPDRFDPDR FSETRQEDEV
FKRNFLTFGN GSHQCVGQRY AMNHLVLFIA MFSSMFDFKR VRSDGCDDIV HIPTMSPKDG
CTVFLSSRLV TSP
