C7101_ARATH
ID C7101_ARATH Reviewed; 495 AA.
AC O64697;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cytochrome P450 710A1 {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=CYP710A1 {ECO:0000303|PubMed:16531502};
GN OrderedLocusNames=At2g34500 {ECO:0000312|Araport:AT2G34500};
GN ORFNames=F13P17.35 {ECO:0000312|EMBL:AAM14944.1};
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,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, 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 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 FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
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 beta-
CC sitosterol and produces stigmasterol. No activity with campesterol.
CC {ECO:0000269|PubMed:16531502, ECO:0000269|PubMed:17909855,
CC ECO:0000269|PubMed:20444228}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for beta-sisterol {ECO:0000269|PubMed:16531502};
CC Note=kcat is 0.53 min(-1) for beta-sisterol.
CC {ECO:0000269|PubMed:16531502};
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 and leaves. Expressed in root tips and sepals. Very low expression in
CC stems and siliques. {ECO:0000269|PubMed:16531502}.
CC -!- INDUCTION: By infection with Pseudomonas syringae.
CC {ECO:0000269|PubMed:20444228}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but upon infection with P.syringae, no accumulation of
CC stigmasterol and increased resistance to the pathogen.
CC {ECO:0000269|PubMed:20444228}.
CC -!- MISCELLANEOUS: Plants overexpressing CYP710A1 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}.
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DR EMBL; AB219423; BAE71351.1; -; Genomic_DNA.
DR EMBL; AC004077; AAC26690.1; -; Genomic_DNA.
DR EMBL; AC004481; AAM14944.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08982.1; -; Genomic_DNA.
DR EMBL; BT002069; AAN72080.1; -; mRNA.
DR EMBL; BT010554; AAQ65177.1; -; mRNA.
DR PIR; T02337; T02337.
DR RefSeq; NP_180997.1; NM_129002.3.
DR AlphaFoldDB; O64697; -.
DR SMR; O64697; -.
DR STRING; 3702.AT2G34500.1; -.
DR PaxDb; O64697; -.
DR PRIDE; O64697; -.
DR ProteomicsDB; 239141; -.
DR EnsemblPlants; AT2G34500.1; AT2G34500.1; AT2G34500.
DR GeneID; 818013; -.
DR Gramene; AT2G34500.1; AT2G34500.1; AT2G34500.
DR KEGG; ath:AT2G34500; -.
DR Araport; AT2G34500; -.
DR TAIR; locus:2040939; AT2G34500.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_023517_1_0_1; -.
DR InParanoid; O64697; -.
DR OMA; MVIPSFY; -.
DR OrthoDB; 574756at2759; -.
DR PhylomeDB; O64697; -.
DR BioCyc; ARA:AT2G34500-MON; -.
DR BioCyc; MetaCyc:AT2G34500-MON; -.
DR BRENDA; 1.14.19.41; 399.
DR UniPathway; UPA00766; -.
DR PRO; PR:O64697; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64697; baseline and differential.
DR Genevisible; O64697; 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..495
FT /note="Cytochrome P450 710A1"
FT /id="PRO_0000411205"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 434
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 495 AA; 55724 MW; 61F428F868D290B1 CRC64;
MVFSVSIFAS LAPYLISAFL LFLLVEQLSY LFKKRNIPGP FFVPPIIGNA VALVRDPTSF
WDKQSSTANI SGLSANYLIG KFIVYIRDTE LSHQIFSNVR PDAFHLIGHP FGKKLFGDHN
LIYMFGEDHK SVRRQLAPNF TPKALSTYSA LQQLVILRHL RQWEGSTSGG SRPVSLRQLV
RELNLETSQT VFVGPYLDKE AKNRFRTDYN LFNLGSMALP IDLPGFAFGE ARRAVKRLGE
TLGICAGKSK ARMAAGEEPA CLIDFWMQAI VAENPQPPHS GDEEIGGLLF DFLFAAQDAS
TSSLLWAVTL LDSEPEVLNR VREEVAKIWS PESNALITVD QLAEMKYTRS VAREVIRYRP
PATMVPHVAA IDFPLTETYT IPKGTIVFPS VFDSSFQGFT EPDRFDPDRF SETRQEDQVF
KRNFLAFGWG PHQCVGQRYA LNHLVLFIAM FSSLLDFKRL RSDGCDEIVY CPTISPKDGC
TVFLSRRVAK YPNFS
