EBP_ARATH
ID EBP_ARATH Reviewed; 223 AA.
AC O48962; Q9SAQ8;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase;
DE EC=5.3.3.5;
DE AltName: Full=Cholestenol Delta-isomerase;
DE AltName: Full=Delta(8)-Delta(7) sterol isomerase;
DE Short=D8-D7 sterol isomerase;
GN OrderedLocusNames=At1g20050; ORFNames=T20H2.18;
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 [MRNA].
RX PubMed=9862498; DOI=10.1023/a:1006028623875;
RA Grebenok R.J., Ohnmeiss T.E., Yamamoto A., Huntley E.D., Galbraith D.W.,
RA Della Penna D.;
RT "Isolation and characterization of an Arabidopsis thaliana C-8,7 sterol
RT isomerase: functional and structural similarities to mammalian C-8,7 sterol
RT isomerase/emopamil-binding protein.";
RL Plant Mol. Biol. 38:807-815(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Benveniste P.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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).
CC -!- FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their
CC corresponding Delta(7)-isomers. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lathosterol = 5alpha-cholest-8-en-3beta-ol;
CC Xref=Rhea:RHEA:15281, ChEBI:CHEBI:16608, ChEBI:CHEBI:17168;
CC EC=5.3.3.5;
CC -!- PATHWAY: Steroid biosynthesis; sterol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EBP family. {ECO:0000305}.
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DR EMBL; AF030357; AAD03489.1; -; mRNA.
DR EMBL; U81498; AAD04752.1; -; mRNA.
DR EMBL; AC022472; AAF79909.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29928.1; -; Genomic_DNA.
DR EMBL; AF334733; AAG50111.1; -; mRNA.
DR PIR; T51727; T51727.
DR RefSeq; NP_173433.1; NM_101859.4.
DR AlphaFoldDB; O48962; -.
DR SMR; O48962; -.
DR BioGRID; 23832; 3.
DR STRING; 3702.AT1G20050.1; -.
DR iPTMnet; O48962; -.
DR PaxDb; O48962; -.
DR PRIDE; O48962; -.
DR ProteomicsDB; 222045; -.
DR EnsemblPlants; AT1G20050.1; AT1G20050.1; AT1G20050.
DR GeneID; 838593; -.
DR Gramene; AT1G20050.1; AT1G20050.1; AT1G20050.
DR KEGG; ath:AT1G20050; -.
DR Araport; AT1G20050; -.
DR TAIR; locus:2198626; AT1G20050.
DR eggNOG; KOG4826; Eukaryota.
DR HOGENOM; CLU_072128_2_0_1; -.
DR InParanoid; O48962; -.
DR OMA; FEGYFAY; -.
DR OrthoDB; 1130914at2759; -.
DR PhylomeDB; O48962; -.
DR BioCyc; ARA:AT1G20050-MON; -.
DR BioCyc; MetaCyc:AT1G20050-MON; -.
DR UniPathway; UPA00766; -.
DR PRO; PR:O48962; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O48962; baseline and differential.
DR Genevisible; O48962; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000247; F:C-8 sterol isomerase activity; IMP:TAIR.
DR GO; GO:0047750; F:cholestenol delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004769; F:steroid delta-isomerase activity; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR007905; EBP.
DR InterPro; IPR033118; EXPERA.
DR PANTHER; PTHR14207; PTHR14207; 1.
DR PROSITE; PS51751; EXPERA; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Isomerase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..223
FT /note="Probable 3-beta-hydroxysteroid-Delta(8),Delta(7)-
FT isomerase"
FT /id="PRO_0000174345"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 54..196
FT /note="EXPERA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01087"
FT CONFLICT 157
FT /note="L -> V (in Ref. 2; AAD04752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 25146 MW; 8060845768EEBACC CRC64;
MEELAHPYVP RDLNLPGYVP ISMSMSSIVS IYLGSSLLVV SLVWLLFGRK KAKLDKLLMC
WWTFTGLTHV ILEGYFVFSP EFFKDNTSAY LAEVWKEYSK GDSRYVGRDS AVVSVEGITA
VIVGPASLLA IYAIAKEKSY SYVLQLAISV CQLYGCLVYF ITAILEGDNF ATNSFYYYSY
YIGANCWWVL IPSLISFRCW KKICAAAAIA NNNVETKTKK KTR
