C7103_ARATH
ID C7103_ARATH Reviewed; 493 AA.
AC Q9ZV29;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytochrome P450 710A3 {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=CYP710A3 {ECO:0000303|PubMed:16531502};
GN OrderedLocusNames=At2g28850 {ECO:0000312|Araport:AT2G28850};
GN ORFNames=F8N16.14 {ECO:0000312|EMBL:AAC79589.1};
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 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).
CC -!- FUNCTION: Required to form the C-22 double bond in the sterol side
CC chain. Possesses in vitro C-22 desaturase activity toward beta-
CC sitosterol and produces stigmasterol. {ECO:0000250|UniProtKB:O64697}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in stems. Detected in primary root caps
CC and immature petals. {ECO:0000269|PubMed:16531502}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AC005727; AAC79589.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08181.1; -; Genomic_DNA.
DR PIR; F84689; F84689.
DR RefSeq; NP_180451.1; NM_128444.2.
DR AlphaFoldDB; Q9ZV29; -.
DR SMR; Q9ZV29; -.
DR STRING; 3702.AT2G28850.1; -.
DR PaxDb; Q9ZV29; -.
DR PRIDE; Q9ZV29; -.
DR ProteomicsDB; 240566; -.
DR EnsemblPlants; AT2G28850.1; AT2G28850.1; AT2G28850.
DR GeneID; 817434; -.
DR Gramene; AT2G28850.1; AT2G28850.1; AT2G28850.
DR KEGG; ath:AT2G28850; -.
DR Araport; AT2G28850; -.
DR TAIR; locus:2053220; AT2G28850.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_023517_1_0_1; -.
DR InParanoid; Q9ZV29; -.
DR OMA; CANLPSF; -.
DR OrthoDB; 574756at2759; -.
DR PhylomeDB; Q9ZV29; -.
DR PRO; PR:Q9ZV29; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZV29; baseline.
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; IEA:UniProtKB-KW.
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:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
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 710A3"
FT /id="PRO_0000435505"
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; 55874 MW; 813E492D172B7208 CRC64;
MVSSVSLFAS LTPYLVSALL LFLLLEQLFY RLKKRNLPGP LFVFPIIGNV VALIRDPTSF
WDKQSAMADT SVGLSVNYLI GKFIIYIKDA ELSNKVFSNI RPDAFQLVGH PFGKKLFGDH
SLIFMFGENH KSVRRQVAPN FTRKPLSAYS SLQQIVILRH LRQWEESFSS GSRPVSMRQL
IRELNLETSQ TVFVGPYLDK EVKNTIRDDY NVFNPGTMAL PIDLPGFTFG EARRAVSRLV
NTMSLCVRKS KEKMAAGENP TCLVDFWTHS IVAESPPPPH SKDEEISCVL VDFLFASQDA
STSSLLWAVV LLESEPEVLR RVREDVARFW SPESKESITA DQLAEMKYIR AVAREVLRYR
PPASMVPHVA VSDFRLTESY TIPKGTIVFP SLFDASFQGF TEPDRFDPDR FSETRQEDEV
FKRNFLTFGI GSHQCVGQRY ALNHLVLFIA MFSSMFDFKR VRSDGCDEIV HIPTMSPKDG
CTVFLSSRLV TSP
