EBP_CAVPO
ID EBP_CAVPO Reviewed; 229 AA.
AC Q60490; Q9QV23;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=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;
DE AltName: Full=Emopamil-binding protein;
GN Name=EBP;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Pirbright white; TISSUE=Liver;
RX PubMed=7706302; DOI=10.1074/jbc.270.13.7551;
RA Hanner M., Moebius F.F., Weber F., Grabner M., Striessnig J., Glossmann H.;
RT "Phenylalkylamine Ca2+ antagonist binding protein. Molecular cloning,
RT tissue distribution, and heterologous expression.";
RL J. Biol. Chem. 270:7551-7557(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-34, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=7961902; DOI=10.1016/s0021-9258(19)62046-6;
RA Moebius F.F., Hanner M., Knaus H.G., Weber F., Striessnig J., Glossmann H.;
RT "Purification and amino-terminal sequencing of the high affinity
RT phenylalkylamine Ca2+ antagonist binding protein from guinea pig liver
RT endoplasmic reticulum.";
RL J. Biol. Chem. 269:29314-29320(1994).
CC -!- FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their
CC corresponding Delta(7)-isomers. {ECO:0000250|UniProtKB:Q15125}.
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:0000250|UniProtKB:Q15125};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34000;
CC Evidence={ECO:0000250|UniProtKB:Q15125};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC {ECO:0000250|UniProtKB:Q15125}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:7961902}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:7961902}. 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: Highly expressed in liver, bowel, adrenal gland,
CC testis, ovary, and uterus and less expressed in brain, cerebellum,
CC skeletal muscle, and heart.
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; Z37985; CAA86067.1; -; mRNA.
DR PIR; A56122; A56122.
DR RefSeq; NP_001166416.1; NM_001172945.1.
DR AlphaFoldDB; Q60490; -.
DR SMR; Q60490; -.
DR STRING; 10141.ENSCPOP00000012749; -.
DR BindingDB; Q60490; -.
DR ChEMBL; CHEMBL5525; -.
DR DrugCentral; Q60490; -.
DR Ensembl; ENSCPOT00000014293; ENSCPOP00000012749; ENSCPOG00000014151.
DR GeneID; 100135518; -.
DR KEGG; cpoc:100135518; -.
DR CTD; 10682; -.
DR eggNOG; KOG4826; Eukaryota.
DR GeneTree; ENSGT00530000063715; -.
DR HOGENOM; CLU_072128_0_0_1; -.
DR InParanoid; Q60490; -.
DR OMA; FEGYFAY; -.
DR OrthoDB; 1130914at2759; -.
DR TreeFam; TF314716; -.
DR BRENDA; 5.3.3.5; 1225.
DR UniPathway; UPA00063; -.
DR PRO; PR:Q60490; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000014151; Expressed in adrenal gland and 13 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0000247; F:C-8 sterol isomerase activity; ISS:UniProtKB.
DR GO; GO:0047750; F:cholestenol delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004769; F:steroid delta-isomerase activity; ISS:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
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 Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Nucleus;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7961902"
FT CHAIN 2..229
FT /note="3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase"
FT /id="PRO_0000174341"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 62..205
FT /note="EXPERA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01087"
FT CONFLICT 27
FT /note="L -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="Y -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 26679 MW; 2D95E07F3248B2E6 CRC64;
MATTSTGPLH PYWPRHLRLD HFVPNDLSAW YIVTVLFTVF GALVVTMWLL SSRASVVPLG
TWRRLSVCWF AVCAFVHLVI EGWFVLYQKA ILGDQAFLSQ LWKEYAKGDS RYIIEDNFII
CMESITVVLW GPLSLWAVIA FLRQHPSRYV LQFVISLGQI YGDLLYFLTE YRDGFQHGEM
GHPIYFWFYF FFMNVLWLVI PGVLFFDSVK QFYGAQNALD TKVMKSKGK
