C7102_ARATH
ID C7102_ARATH Reviewed; 499 AA.
AC O64698; Q8LE78;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cytochrome P450 710A2 {ECO:0000303|PubMed:16531502};
DE EC=1.14.19.41 {ECO:0000269|PubMed:16531502};
DE AltName: Full=C-22 sterol desaturase {ECO:0000303|PubMed:16531502};
GN Name=CYP710A2 {ECO:0000303|PubMed:16531502};
GN OrderedLocusNames=At2g34490 {ECO:0000312|Araport:AT2G34490};
GN ORFNames=F13P17.22 {ECO:0000312|EMBL:AAM14945.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND PATHWAY.
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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 in vitro C-22 desaturase activity toward 24-epi-
CC campesterol and beta-sitosterol and produces brassicasterol and
CC stigmasterol, respectively. No activity with campesterol.
CC {ECO:0000269|PubMed:16531502}.
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:0000269|PubMed:16531502};
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:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissues of roots, shoots,
CC stems and leaves. Expressed in root tips, carpes, siliques and seeds.
CC {ECO:0000269|PubMed:16531502}.
CC -!- INDUCTION: Not induced by pathogen infection.
CC {ECO:0000269|PubMed:20444228}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but production of brassicasterol is abolished.
CC {ECO:0000269|PubMed:16531502}.
CC -!- MISCELLANEOUS: Plants overexpressing CYP710A2 show higher levels of
CC brassicasterol/crinosterol and stigmasterol, and lower levels of 24-
CC epi-campesterol/campesterol and beta-sitosterol than the wild-type.
CC {ECO:0000269|PubMed:16531502}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB233425; BAE80316.1; -; Genomic_DNA.
DR EMBL; AC004077; AAC26691.1; -; Genomic_DNA.
DR EMBL; AC004481; AAM14945.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08981.1; -; Genomic_DNA.
DR EMBL; AY074867; AAL75888.1; -; mRNA.
DR EMBL; AY101543; AAM26664.1; -; mRNA.
DR EMBL; AY085577; AAM62799.1; -; mRNA.
DR PIR; T02336; T02336.
DR RefSeq; NP_180996.1; NM_129001.3.
DR AlphaFoldDB; O64698; -.
DR SMR; O64698; -.
DR STRING; 3702.AT2G34490.1; -.
DR PaxDb; O64698; -.
DR PRIDE; O64698; -.
DR ProteomicsDB; 239119; -.
DR EnsemblPlants; AT2G34490.1; AT2G34490.1; AT2G34490.
DR GeneID; 818012; -.
DR Gramene; AT2G34490.1; AT2G34490.1; AT2G34490.
DR KEGG; ath:AT2G34490; -.
DR Araport; AT2G34490; -.
DR TAIR; locus:2040929; AT2G34490.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_023517_1_0_1; -.
DR InParanoid; O64698; -.
DR OMA; ATWLFQT; -.
DR OrthoDB; 574756at2759; -.
DR PhylomeDB; O64698; -.
DR BioCyc; ARA:AT2G34490-MON; -.
DR BioCyc; MetaCyc:AT2G34490-MON; -.
DR BRENDA; 1.14.19.41; 399.
DR UniPathway; UPA00766; -.
DR PRO; PR:O64698; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64698; baseline and differential.
DR Genevisible; O64698; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000249; F:C-22 sterol desaturase activity; IDA:TAIR.
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 1: Evidence at protein 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..499
FT /note="Cytochrome P450 710A2"
FT /id="PRO_0000411206"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 439
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"
FT CONFLICT 18
FT /note="A -> S (in Ref. 4; AAM62799)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 56346 MW; 6CC7D1CBC0474348 CRC64;
MVFSVSIFAS LAPYLVSALL LFFLIEQLSY LVKKRNLPGP LFVPPIIGNA ISLVRDPTSF
WFKQSDTAGT SPGLAANYLI GKFIIYIRDT ELSHQIFSNV RLEAFHPLGH PFGKQLFGDH
SLIYLFGEDH KTVRRHLAPN FTPKALSTYS DLQQIVMLRH LRQWEESFSG GTKPVSMRDL
VRELNLETSQ TVFVGPYLDK EARNTFCTDY NLFNLGSMAL PINLPGFAFN KARRAVMNLE
KTLSVCAGKS KKRMATGEEP TCLIDFWMHA FVTEIESGNP PPLHSEDEAI GGLLFDFLFA
AQDASTSSLL WAVTFLESHP KVLSKVREEV AKIWSPQSGH LITADQLAEM KYTRAVAREV
VRYRPPATMV PHIATNDFPL TESYTIPKGT IVFPSVFDAS FQGFTEPNRF DPDRFSETRQ
EDQVFKRNYL AFGWGAHQCV GQRYALNHLV LFIAMFSSLF DFKRLQSDGC DDIIYCPTIS
PKDGCTVFLS KRIVTYPNL
