EBPL_MOUSE
ID EBPL_MOUSE Reviewed; 206 AA.
AC Q9D0P0; Q3TQR1; Q9CRQ2; Q9CY81;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Emopamil-binding protein-like;
DE AltName: Full=Emopamil-binding-related protein;
GN Name=Ebpl; Synonyms=Ebrp, Erp;
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].
RC STRAIN=C57BL/6J;
RX PubMed=12760743; DOI=10.1042/bj20030465;
RA Moebius F.F., Fitzky B.U., Wietzorrek G., Haidekker A., Eder A.,
RA Glossmann H.;
RT "Cloning of an emopamil-binding protein (EBP)-like protein that lacks
RT sterol delta8-delta7 isomerase activity.";
RL Biochem. J. 374:229-237(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, and 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 STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
CC -!- FUNCTION: Does not possess sterol isomerase activity and does not bind
CC sigma ligands. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; AF243434; AAK28349.2; -; mRNA.
DR EMBL; AK011237; BAB27485.1; -; mRNA.
DR EMBL; AK019140; BAB31565.1; -; mRNA.
DR EMBL; AK019963; BAB31938.1; -; mRNA.
DR EMBL; AK163371; BAE37321.1; -; mRNA.
DR EMBL; BC027422; AAH27422.1; -; mRNA.
DR CCDS; CCDS27183.1; -.
DR RefSeq; NP_080874.2; NM_026598.3.
DR AlphaFoldDB; Q9D0P0; -.
DR SMR; Q9D0P0; -.
DR BioGRID; 212703; 2.
DR STRING; 10090.ENSMUSP00000022494; -.
DR EPD; Q9D0P0; -.
DR jPOST; Q9D0P0; -.
DR MaxQB; Q9D0P0; -.
DR PaxDb; Q9D0P0; -.
DR PRIDE; Q9D0P0; -.
DR ProteomicsDB; 277795; -.
DR Antibodypedia; 53037; 66 antibodies from 13 providers.
DR DNASU; 68177; -.
DR Ensembl; ENSMUST00000022494; ENSMUSP00000022494; ENSMUSG00000021928.
DR GeneID; 68177; -.
DR KEGG; mmu:68177; -.
DR UCSC; uc007ufv.2; mouse.
DR CTD; 84650; -.
DR MGI; MGI:1915427; Ebpl.
DR VEuPathDB; HostDB:ENSMUSG00000021928; -.
DR eggNOG; KOG4826; Eukaryota.
DR GeneTree; ENSGT00530000063715; -.
DR HOGENOM; CLU_072128_1_1_1; -.
DR InParanoid; Q9D0P0; -.
DR OMA; VYLWLYL; -.
DR OrthoDB; 1323969at2759; -.
DR PhylomeDB; Q9D0P0; -.
DR TreeFam; TF314716; -.
DR BioGRID-ORCS; 68177; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Ebpl; mouse.
DR PRO; PR:Q9D0P0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9D0P0; protein.
DR Bgee; ENSMUSG00000021928; Expressed in retinal neural layer and 63 other tissues.
DR Genevisible; Q9D0P0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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:0047750; F:cholestenol delta-isomerase activity; IEA:InterPro.
DR GO; GO:0016125; P:sterol metabolic process; IEA:InterPro.
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; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..206
FT /note="Emopamil-binding protein-like"
FT /id="PRO_0000174348"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 39..184
FT /note="EXPERA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01087"
FT CONFLICT 9..11
FT /note="PEA -> SEQ (in Ref. 1; AAK28349)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="L -> R (in Ref. 2; BAB31565)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="S -> T (in Ref. 2; BAB31938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 23307 MW; 429079796100C764 CRC64;
MGEHWALGPE AGSSLLLCSA LLAVGCALGL RLGRGRSAVE RWVLAWLCYD SLVHFVLEGA
FVYLSIVGNV ADSQGLIASL WKEYGKADTR WLYSDPTVVS LEILTVVLDG LLALVLIYAI
VKEKYYRHFV QIVLCVCELY GCWMTFFPEW LVGSPSLNTS SWLYLWVYLV FFNGLWVLIP
GLLLWQSWVE LKKRDSQEAN LAKKHK
