ID ERG24_SCHPO Reviewed; 424 AA. AC Q09195; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 64. DE RecName: Full=Delta(14)-sterol reductase; DE EC=1.3.1.70; DE AltName: Full=C-14 sterol reductase; DE AltName: Full=Sterol C14-reductase; GN Name=erg24; ORFNames=SPBC16G5.18; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=SP66; RX MEDLINE=95212923; PubMed=7698661; DOI=10.1016/0378-1119(94)00902-5; RA Smith S.; RT "Cloning and sequence analysis of an ERG24 homolog from RT Schizosaccharomyces pombe."; RL Gene 155:139-140(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Reduces the C14=C15 double bond of 4,4-dimethyl- CC cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24- CC dienol (By similarity). CC -!- CATALYTIC ACTIVITY: 4,4-dimethyl-5-alpha-cholesta-8,24-dien-3- CC beta-ol + NADP(+) = 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3- CC beta-ol + NADPH. CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol CC from lanosterol: step 2/6. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Probable). CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L36039; AAA74121.1; -; mRNA. DR EMBL; CU329671; CAA19037.1; -; Genomic_DNA. DR PIR; JC4057; JC4057. DR RefSeq; NP_596767.1; -. DR GeneID; 2540113; -. DR KEGG; spo:SPBC16G5.18; -. DR NMPDR; fig|4896.1.peg.2633; -. DR GeneDB_Spombe; SPBC16G5.18; -. DR OMA; Q09195; TMFHLLL. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-004750-MON; -. DR BRENDA; 1.3.1.70; 653. DR ArrayExpress; Q09195; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:GeneDB_SPombe. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0050613; F:delta14-sterol reductase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR001171; Ergosterol_biosynth_ERG4_ERG24. 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 2: Evidence at transcript level; KW Complete proteome; Lipid synthesis; Membrane; NADP; Oxidoreductase; KW Steroid biosynthesis; Sterol biosynthesis; Transmembrane. FT CHAIN 1 424 Delta(14)-sterol reductase. FT /FTId=PRO_0000207493. FT TRANSMEM 19 39 Potential. FT TRANSMEM 112 132 Potential. FT TRANSMEM 370 390 Potential. SQ SEQUENCE 424 AA; 48560 MW; 1D3CE704F1E5EF5B CRC64; MAKGAVKKEK FEYEFFGPIG ALGVTVLTTV VSFGSFYICN EEGCPAKFSK ISHIFKKTPL FDQKSLILYL LWFSTLTLLW KCTNGKWAKG TPIDDKGTRL LYKINGFNSA CLILGVVCTS IYLLGASCME FIWDNFLQLM FAAYVFSVVL CTFCYVQSFF GKQQLAKGGT SGNILFDWFI GRSLNPRIGN FDIKCFCELR PGLILWVVFD IAFACHQYLV LGGRITDSMV LVIIFHTWYV LDSLINESAV LTTMDITTDG FGYMLSFGDL VWVPFLYSLQ ARYLAFHPVD LGLVKTLAIL CLQFLGYYIF RGANGQKNRF RSNPNDPKLK HLKFIQTKRG TKLLTSGWWG MARHINYFGD WIMAWAWCLP AGFGSPIPYF YVAYFGVLLV HRNARDDHKC RVKYGEDWEK YCKAVKYRII PYVY //