ERG24_MOUSE
ID ERG24_MOUSE Reviewed; 418 AA.
AC Q71KT5; B5LBK0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Delta(14)-sterol reductase TM7SF2;
DE Short=Delta-14-SR;
DE EC=1.3.1.70 {ECO:0000250|UniProtKB:Q8WMV1};
DE AltName: Full=3-beta-hydroxysterol Delta (14)-reductase {ECO:0000250|UniProtKB:O76062};
DE AltName: Full=C-14 sterol reductase;
DE Short=C14SR;
DE AltName: Full=Sterol C14-reductase;
DE AltName: Full=Transmembrane 7 superfamily member 2;
GN Name=Tm7sf2;
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].
RA Roberti R., Bennati A.M.;
RT "cDNA cloning and expression of the gene encoding the mouse C-14 sterol
RT reductase.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=18785926; DOI=10.1111/j.1742-4658.2008.06637.x;
RA Bennati A.M., Schiavoni G., Franken S., Piobbico D., Della Fazia M.A.,
RA Caruso D., De Fabiani E., Benedetti L., Cusella De Angelis M.G.,
RA Gieselmann V., Servillo G., Beccari T., Roberti R.;
RT "Disruption of the gene encoding 3beta-hydroxysterol Delta14-reductase
RT (Tm7sf2) in mice does not impair cholesterol biosynthesis.";
RL FEBS J. 275:5034-5047(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
CC -!- FUNCTION: Catalyzes the reduction of the C14-unsaturated bond of
CC lanosterol, as part of the metabolic pathway leading to cholesterol
CC biosynthesis. {ECO:0000269|PubMed:18785926}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) =
CC 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH;
CC Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813,
CC ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70;
CC Evidence={ECO:0000250|UniProtKB:Q8WMV1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-cholest-8,14-dien-3beta-ol + H(+) + NADPH = 5alpha-
CC cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46456,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16608, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:86131;
CC Evidence={ECO:0000269|PubMed:18785926};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-8,14-cholestadien-3beta-ol + H(+) + NADPH = 4,4-
CC dimethyl-5alpha-cholest-8-en-3beta-ol + NADP(+);
CC Xref=Rhea:RHEA:46812, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78904, ChEBI:CHEBI:87044;
CC Evidence={ECO:0000250|UniProtKB:Q8WMV1};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O76062}; Multi-pass membrane protein
CC {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:18785926}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in liver, weaker in ovary,
CC testis, kidney and brain. {ECO:0000269|PubMed:18785926}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally, appear healthy and are
CC fertile. {ECO:0000269|PubMed:18785926}.
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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DR EMBL; AF480070; AAQ05836.1; -; mRNA.
DR EMBL; EU672836; ACF94776.1; -; Genomic_DNA.
DR EMBL; AK155475; BAE33285.1; -; mRNA.
DR EMBL; CH466612; EDL33202.1; -; Genomic_DNA.
DR CCDS; CCDS29490.2; -.
DR RefSeq; NP_082730.2; NM_028454.2.
DR AlphaFoldDB; Q71KT5; -.
DR SMR; Q71KT5; -.
DR STRING; 10090.ENSMUSP00000025713; -.
DR iPTMnet; Q71KT5; -.
DR PhosphoSitePlus; Q71KT5; -.
DR jPOST; Q71KT5; -.
DR MaxQB; Q71KT5; -.
DR PaxDb; Q71KT5; -.
DR PeptideAtlas; Q71KT5; -.
DR PRIDE; Q71KT5; -.
DR ProteomicsDB; 275769; -.
DR Antibodypedia; 29654; 123 antibodies from 23 providers.
DR DNASU; 73166; -.
DR Ensembl; ENSMUST00000025713; ENSMUSP00000025713; ENSMUSG00000024799.
DR GeneID; 73166; -.
DR KEGG; mmu:73166; -.
DR UCSC; uc008ggw.1; mouse.
DR CTD; 7108; -.
DR MGI; MGI:1920416; Tm7sf2.
DR VEuPathDB; HostDB:ENSMUSG00000024799; -.
DR eggNOG; KOG1435; Eukaryota.
DR GeneTree; ENSGT00390000000417; -.
DR HOGENOM; CLU_015631_0_1_1; -.
DR InParanoid; Q71KT5; -.
DR OMA; GWIILNC; -.
DR OrthoDB; 532774at2759; -.
DR PhylomeDB; Q71KT5; -.
DR TreeFam; TF101179; -.
DR BRENDA; 1.3.1.70; 3474.
DR Reactome; R-MMU-191273; Cholesterol biosynthesis.
DR UniPathway; UPA00063; -.
DR BioGRID-ORCS; 73166; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Tm7sf2; mouse.
DR PRO; PR:Q71KT5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q71KT5; protein.
DR Bgee; ENSMUSG00000024799; Expressed in left lobe of liver and 236 other tissues.
DR ExpressionAtlas; Q71KT5; baseline and differential.
DR Genevisible; Q71KT5; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0031090; C:organelle membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0050613; F:delta14-sterol reductase activity; IMP:UniProtKB.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001171; ERG24_DHCR-like.
DR InterPro; IPR018083; Sterol_reductase_CS.
DR Pfam; PF01222; ERG4_ERG24; 1.
DR PROSITE; PS01017; STEROL_REDUCT_1; 1.
DR PROSITE; PS01018; STEROL_REDUCT_2; 1.
PE 1: Evidence at protein level;
KW Cholesterol biosynthesis; Cholesterol metabolism; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Microsome; NADP;
KW Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..418
FT /note="Delta(14)-sterol reductase TM7SF2"
FT /id="PRO_0000331121"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 311
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 315
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 338
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 343
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 350..351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 390
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 394..398
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 405
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT CONFLICT 298
FT /note="V -> A (in Ref. 1; AAQ05836 and 3; BAE33285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46521 MW; 0DCCA4E4B9423A31 CRC64;
MTSREASQAP LEFGGPLGVA ALLILLPATM FHLLLAARSG PARLLALPAY LPGLEELWSP
WALLLLFIWL GLQVALYLLP ARKVAEGLEL KDKSRLRYPI NGFQALVLTA LLMGLGVSVG
LPLGALPGML LPLAFATTLT SFIFSLLLYA KALVAPASAL APGGNSGNSM YDFFLGRELN
PRLGSFDFKY FCELRPGLIG WVFINLALLM QEAELRGSPS LAMWLVNGFQ LLYVGDALWY
EESVLTTMDI IHDGFGFMLV FGDLAWVPFT YSLQAQFLLY HPQPLGLPMA LLICLLKVIG
YYIFRGANSQ KNTFRKNPSD PSVAGLETIP TATGRQLLVS GWWGMVRHPN YLGDLIMALA
WSLPCGLSHL LPYFYVLYFT ALLVHREARD EQQCLQKYGR AWQEYCKRVP YRIIPYVY
