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UniProtKB/Swiss-Prot entry P70245


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name EBP_MOUSE
Primary accession number P70245
Secondary accession number Q9CSP4
Integrated into Swiss-Prot on October 18, 2001
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 67)
Name and origin of the protein
Protein name 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
Synonyms EC 5.3.3.5
Cholestenol Delta-isomerase
Delta(8)-Delta(7) sterol isomerase
D8-D7 sterol isomerase
Emopamil-binding protein
Gene name
Name: Ebp
Synonyms: Msi
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.271.37.22434; PubMed=8798407 [NCBI, ExPASy, EBI, Israel, Japan]
Silve S., Dupuy P.H., Labit-Lebouteiller C., Kaghad M., Chalon P., Rahier A., Taton M., Lupker J., Shire D., Loison G.;
"Emopamil-binding protein, a mammalian protein that binds a series of structurally diverse neuroprotective agents, exhibits delta8-delta7 sterol isomerase activity in yeast.";
J. Biol. Chem. 271:22434-22440(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Embryo;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-14; 53-62 AND 210-221, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Liver;
Kanor S., Bienvenut W.V.;
Submitted (OCT-2005) to UniProtKB.
[5]
VARIANT TD ARG-107.
DOI=10.1038/10350; PubMed=10391218 [NCBI, ExPASy, EBI, Israel, Japan]
Derry J.M.J., Gormally E., Means G.D., Zhao W., Meindl A., Kelley R.I., Boyd Y., Herman G.E.;
"Mutations in a delta(8)-delta(7) sterol isomerase in the tattered mouse and X-linked dominant chondrodysplasia punctata.";
Nat. Genet. 22:286-290(1999).
Comments
  • FUNCTION: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers.
  • CATALYTIC ACTIVITY: 5-alpha-cholest-7-en-3-beta-ol = 5-alpha-cholest-8-en-3-beta-ol.
  • PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
  • SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.
  • DISEASE: Defects in Ebp are a cause of 'Tattered' (Td) which is an X-linked, semidominant mouse mutation associated with prenatal male lethality. Heterozygous females are small and at 4 to 5 days of age develop patches of hyperkeratotic skin where no hair grows, resulting in a striping of the coat in adults. Craniofacial anomalies and twisted toes have also been observed in some affected females.
  • MISCELLANEOUS: Binds to the phenylalkylamine calcium-ion antagonist emopamil, an anti-ischemic drug.
  • SIMILARITY: Belongs to the EBP family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X97755; CAA66350.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK012266; BAB28129.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027977; BAC25686.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004703; AAH04703.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004620; AAH04620.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_031924.1; -.
UniGene Mm.27183
3D structure databases
ModBase P70245.
Organism-specific databases
MGI MGI:107822; Ebp.
Gene expression databases
ArrayExpress P70245; -.
GermOnline ENSMUSG00000031168; Mus musculus.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (traceable author statement from MGI).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0000247; Molecular function: C-8 sterol isomerase activity (inferred from direct assay from MGI).
GO:0047750; Molecular function: cholestenol delta-isomerase activity (inferred from electronic annotation from InterPro).
GO:0006695; Biological process: cholesterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0030097; Biological process: hemopoiesis (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR007905; EBP.
Graphical view of domain structure.
PANTHER PTHR14207; EBP; 1.
Pfam PF05241; EBP; 1.
Pfam graphical view of domain structure.
ProtoNet P70245.
Genome annotation databases
Ensembl ENSMUSG00000031168; Mus musculus. [Contig view]
GeneID 13595; -.
KEGG mmu:13595; -.
Phylogenomic databases
HOGENOM P70245; -.
HOVERGEN P70245; -.
Other
NextBio 284216; -.
SOURCE Ebp; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cholesterol biosynthesis; Direct protein sequencing; Disease mutation; Endoplasmic reticulum; Isomerase; Lipid synthesis; Membrane; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   230  229     3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase. PRO_0000174343
TRANSMEM   29    49  21     Potential. 
TRANSMEM   66    86  21     Potential. 
TRANSMEM   121   141  21     Potential. 
TRANSMEM   185   205  21     Potential. 
MOD_RES   2     2        N-acetylthreonine. 
VARIANT   107   107  1     G -> R (in Td). 
Sequence information
Length: 230 AA [This is the length of the unprocessed precursor] Molecular weight: 26215 Da [This is the MW of the unprocessed precursor] CRC64: 26752EEE59F098A7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTTNTVPLHP YWPRHLKLDN FVPNDLPTSH ILVGLFSISG GLIVITWLLS SRASVVPLGA 

        70         80         90        100        110        120 
GRRLALCWFA VCTFIHLVIE GWFSLYNGIL LEDQAFLSQL WKEYSKGDSR YILSDSFVVC 

       130        140        150        160        170        180 
METVTACLWG PLSLWVVIAF LRQQPFRFVL QLVVSMGQIY GDVLYFLTEL HEGLQHGEIG 

       190        200        210        220        230 
HPVYFWFYFV FLNAVWLVIP SILVLDAIKH LTSAQSVLDS KVMKIKSKHN 

P70245 in FASTA format

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