EBP_MOUSE
ID EBP_MOUSE Reviewed; 230 AA.
AC P70245; Q9CSP4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase {ECO:0000305};
DE EC=5.3.3.5 {ECO:0000269|PubMed:8798407};
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 {ECO:0000312|MGI:MGI:107822}; Synonyms=Msi;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND PATHWAY.
RX PubMed=8798407; DOI=10.1074/jbc.271.37.22434;
RA Silve S., Dupuy P.H., Labit-Lebouteiller C., Kaghad M., Chalon P.,
RA Rahier A., Taton M., Lupker J., Shire D., Loison G.;
RT "Emopamil-binding protein, a mammalian protein that binds a series of
RT structurally diverse neuroprotective agents, exhibits delta8-delta7 sterol
RT isomerase activity in yeast.";
RL J. Biol. Chem. 271:22434-22440(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-14; 53-62 AND 210-221, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Kanor S., Bienvenut W.V.;
RL Submitted (OCT-2005) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP VARIANT TD ARG-107.
RX PubMed=10391218; DOI=10.1038/10350;
RA Derry J.M.J., Gormally E., Means G.D., Zhao W., Meindl A., Kelley R.I.,
RA Boyd Y., Herman G.E.;
RT "Mutations in a delta(8)-delta(7) sterol isomerase in the tattered mouse
RT and X-linked dominant chondrodysplasia punctata.";
RL Nat. Genet. 22:286-290(1999).
CC -!- FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their
CC corresponding Delta(7)-isomers. {ECO:0000269|PubMed:8798407}.
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:0000269|PubMed:8798407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15282;
CC Evidence={ECO:0000305|PubMed:8798407};
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:0000269|PubMed:8798407}.
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 -!- DISEASE: Note=Defects in Ebp are a cause of 'Tattered' (Td) which is an
CC X-linked, semidominant mouse mutation associated with prenatal male
CC lethality. Heterozygous females are small and at 4 to 5 days of age
CC develop patches of hyperkeratotic skin where no hair grows, resulting
CC in a striping of the coat in adults. Craniofacial anomalies and twisted
CC toes have also been observed in some affected females.
CC -!- MISCELLANEOUS: Binds to the phenylalkylamine calcium-ion antagonist
CC emopamil, an anti-ischemic drug.
CC -!- SIMILARITY: Belongs to the EBP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X97755; CAA66350.1; -; mRNA.
DR EMBL; AK012266; BAB28129.1; -; mRNA.
DR EMBL; AK027977; BAC25686.1; -; mRNA.
DR EMBL; BC004703; AAH04703.1; -; mRNA.
DR EMBL; BC004620; AAH04620.1; -; mRNA.
DR CCDS; CCDS29989.1; -.
DR RefSeq; NP_031924.1; NM_007898.3.
DR AlphaFoldDB; P70245; -.
DR SMR; P70245; -.
DR BioGRID; 199362; 3.
DR STRING; 10090.ENSMUSP00000033509; -.
DR ChEMBL; CHEMBL3774293; -.
DR SwissLipids; SLP:000001210; -.
DR iPTMnet; P70245; -.
DR PhosphoSitePlus; P70245; -.
DR EPD; P70245; -.
DR jPOST; P70245; -.
DR MaxQB; P70245; -.
DR PaxDb; P70245; -.
DR PeptideAtlas; P70245; -.
DR PRIDE; P70245; -.
DR ProteomicsDB; 277667; -.
DR DNASU; 13595; -.
DR Ensembl; ENSMUST00000033509; ENSMUSP00000033509; ENSMUSG00000031168.
DR GeneID; 13595; -.
DR KEGG; mmu:13595; -.
DR UCSC; uc009soi.1; mouse.
DR CTD; 10682; -.
DR MGI; MGI:107822; Ebp.
DR VEuPathDB; HostDB:ENSMUSG00000031168; -.
DR eggNOG; KOG4826; Eukaryota.
DR GeneTree; ENSGT00530000063715; -.
DR HOGENOM; CLU_072128_0_0_1; -.
DR InParanoid; P70245; -.
DR OMA; FEGYFAY; -.
DR OrthoDB; 1130914at2759; -.
DR PhylomeDB; P70245; -.
DR TreeFam; TF314716; -.
DR BRENDA; 5.3.3.5; 3474.
DR Reactome; R-MMU-6807047; Cholesterol biosynthesis via desmosterol.
DR Reactome; R-MMU-6807062; Cholesterol biosynthesis via lathosterol.
DR UniPathway; UPA00063; -.
DR BioGRID-ORCS; 13595; 3 hits in 75 CRISPR screens.
DR PRO; PR:P70245; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P70245; protein.
DR Bgee; ENSMUSG00000031168; Expressed in left lobe of liver and 265 other tissues.
DR ExpressionAtlas; P70245; baseline and differential.
DR Genevisible; P70245; MM.
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; ISM:MGI.
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; IDA:MGI.
DR GO; GO:0047750; F:cholestenol delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004769; F:steroid delta-isomerase activity; ISO:MGI.
DR GO; GO:0006695; P:cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0043931; P:ossification involved in bone maturation; ISO:MGI.
DR GO; GO:0016126; P:sterol biosynthetic process; IMP:MGI.
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; Direct protein sequencing; Disease variant;
KW Endoplasmic reticulum; Isomerase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Nucleus; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..230
FT /note="3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase"
FT /id="PRO_0000174343"
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:0000269|Ref.4"
FT VARIANT 107
FT /note="G -> R (in Td)"
FT /evidence="ECO:0000269|PubMed:10391218"
SQ SEQUENCE 230 AA; 26215 MW; 26752EEE59F098A7 CRC64;
MTTNTVPLHP YWPRHLKLDN FVPNDLPTSH ILVGLFSISG GLIVITWLLS SRASVVPLGA
GRRLALCWFA VCTFIHLVIE GWFSLYNGIL LEDQAFLSQL WKEYSKGDSR YILSDSFVVC
METVTACLWG PLSLWVVIAF LRQQPFRFVL QLVVSMGQIY GDVLYFLTEL HEGLQHGEIG
HPVYFWFYFV FLNAVWLVIP SILVLDAIKH LTSAQSVLDS KVMKIKSKHN
