EBP_RAT
ID EBP_RAT Reviewed; 230 AA.
AC Q9JJ46; Q548M8;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase {ECO:0000305};
DE EC=5.3.3.5 {ECO:0000305|PubMed:11171067};
DE AltName: Full=Cholestenol Delta-isomerase;
DE AltName: Full=Delta(8)-Delta(7) sterol isomerase;
DE Short=D8-D7 sterol isomerase;
DE AltName: Full=Emopamil-binding protein;
DE AltName: Full=Sterol 8-isomerase;
GN Name=Ebp {ECO:0000312|RGD:620957}; Synonyms=Rsi;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND ACTIVITY REGULATION.
RX PubMed=11171067; DOI=10.1042/0264-6021:3530689;
RA Bae S., Seong J., Paik Y.;
RT "Cholesterol biosynthesis from lanosterol: molecular cloning, chromosomal
RT localization, functional expression and liver-specific gene regulation of
RT rat sterol delta8-isomerase, a cholesterogenic enzyme with multiple
RT functions.";
RL Biochem. J. 353:689-699(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Fischer 344; TISSUE=Liver;
RA Shin H.-J., Paik Y.-K.;
RT "Gene structure and analysis of promoter region of rat sterol 8-isomerase
RT gene.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their
CC corresponding Delta(7)-isomers. {ECO:0000269|PubMed:11171067}.
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; Evidence={ECO:0000250|UniProtKB:Q15125};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15282;
CC Evidence={ECO:0000250|UniProtKB:Q15125};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=zymosterol = 5alpha-cholesta-7,24-dien-3beta-ol;
CC Xref=Rhea:RHEA:33999, ChEBI:CHEBI:16290, ChEBI:CHEBI:18252;
CC Evidence={ECO:0000269|PubMed:11171067};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34000;
CC Evidence={ECO:0000305|PubMed:11171067};
CC -!- ACTIVITY REGULATION: Enzymatic activity is induced by 25-
CC hydroxycholesterol, cholestyramine and lovastatin.
CC {ECO:0000269|PubMed:11171067}.
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC {ECO:0000269|PubMed:11171067}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15125}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q15125}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q15125}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q15125}. Note=During interphase, detected on the
CC endoplasmic reticulum and the nuclear envelope. During mitosis,
CC detected on cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q15125}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:11171067}.
CC -!- DEVELOPMENTAL STAGE: Expression in liver is reduced by 70% in 2 years
CC old rats compare to 3 weeks old. {ECO:0000269|PubMed:11171067}.
CC -!- MISCELLANEOUS: Binds to the phenylalkylamine calcium-ion antagonist
CC emopamil, an anti-ischemic drug.
CC -!- SIMILARITY: Belongs to the EBP family. {ECO:0000305}.
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DR EMBL; AF071501; AAF74807.1; -; mRNA.
DR EMBL; AF318617; AAQ14592.1; -; Genomic_DNA.
DR RefSeq; NP_476478.1; NM_057137.1.
DR RefSeq; XP_006256761.1; XM_006256699.3.
DR AlphaFoldDB; Q9JJ46; -.
DR SMR; Q9JJ46; -.
DR STRING; 10116.ENSRNOP00000007015; -.
DR PaxDb; Q9JJ46; -.
DR PRIDE; Q9JJ46; -.
DR Ensembl; ENSRNOT00000007015; ENSRNOP00000007015; ENSRNOG00000004903.
DR GeneID; 117278; -.
DR KEGG; rno:117278; -.
DR UCSC; RGD:620957; rat.
DR CTD; 10682; -.
DR RGD; 620957; Ebp.
DR eggNOG; KOG4826; Eukaryota.
DR GeneTree; ENSGT00530000063715; -.
DR HOGENOM; CLU_072128_0_0_1; -.
DR InParanoid; Q9JJ46; -.
DR OMA; FEGYFAY; -.
DR OrthoDB; 1130914at2759; -.
DR PhylomeDB; Q9JJ46; -.
DR TreeFam; TF314716; -.
DR BRENDA; 5.3.3.5; 5301.
DR Reactome; R-RNO-6807047; Cholesterol biosynthesis via desmosterol.
DR Reactome; R-RNO-6807062; Cholesterol biosynthesis via lathosterol.
DR SABIO-RK; Q9JJ46; -.
DR UniPathway; UPA00063; -.
DR PRO; PR:Q9JJ46; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000004903; Expressed in liver and 19 other tissues.
DR Genevisible; Q9JJ46; RN.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0000247; F:C-8 sterol isomerase activity; IDA:RGD.
DR GO; GO:0047750; F:cholestenol delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004769; F:steroid delta-isomerase activity; ISS:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IDA:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0043931; P:ossification involved in bone maturation; ISO:RGD.
DR GO; GO:0016126; P:sterol biosynthetic process; ISO:RGD.
DR InterPro; IPR007905; EBP.
DR InterPro; IPR033118; EXPERA.
DR PANTHER; PTHR14207; PTHR14207; 1.
DR PROSITE; PS51751; EXPERA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cholesterol biosynthesis; Cholesterol metabolism;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Isomerase; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Nucleus; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15125"
FT CHAIN 2..230
FT /note="3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase"
FT /id="PRO_0000174344"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 61..204
FT /note="EXPERA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01087"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15125"
SQ SEQUENCE 230 AA; 26738 MW; 7CBBF252A0B9E546 CRC64;
MTTNMLPLHP YWPRHLRLDN FVPNDLPTWH ILVGLFSFSG VLIVITWLLS SRVSVVPLGT
GRRLALCWFA VCTFIHLVIE GWFSFYHEIL LEDQAFLSQL WKEYSKGDSR YILSDGFIVC
MESVTACLWG PLSLWVVIAF LRHQPFRFVL QLVVSVGQIY GDVLYFLTEL RDGFQHGELG
HPLYFWFYFV IMNAIWLVIP GILVFDAIKH LTNAQSMLDN KVMKIKSKHN
