ID   STS1_SCHPO              Reviewed;         453 AA.
AC   P36209; O13891;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   25-NOV-2008, entry version 56.
DE   RecName: Full=Delta(24(24(1)))-sterol reductase;
DE            EC=1.3.1.71;
DE   AltName: Full=Sterol Delta(24(28))-reductase;
DE   AltName: Full=C-24(28) sterol reductase;
GN   Name=sts1; ORFNames=SPAC20G4.07c;
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 [GENOMIC DNA].
RX   MEDLINE=92329994; PubMed=1320960;
RA   Shimanuki M., Goebl M., Yanagida M., Toda T.;
RT   "Fission yeast sts1+ gene encodes a protein similar to the chicken
RT   lamin B receptor and is implicated in pleiotropic drug-sensitivity,
RT   divalent cation-sensitivity, and osmoregulation.";
RL   Mol. Biol. Cell 3:263-273(1992).
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).
RN   [3]
RP   CHARACTERIZATION.
RX   MEDLINE=94171077; PubMed=8125337; DOI=10.1016/0378-1119(94)90728-5;
RA   Lai M.H., Bard M., Pierson C.A., Alexander J.F., Goebl M.,
RA   Carter G.T., Kirsch D.R.;
RT   "The identification of a gene family in the Saccharomyces cerevisiae
RT   ergosterol biosynthesis pathway.";
RL   Gene 140:41-49(1994).
CC   -!- CATALYTIC ACTIVITY: Ergosterol + NADP(+) = ergosta-
CC       5,7,22,24(24(1))-tetraen-3-beta-ol + NADPH.
CC   -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol
CC       from zymosterol: step 5/5.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- SIMILARITY: Belongs to the ERG4/ERG24 family.
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DR   EMBL; X63549; CAA45113.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11256.1; -; Genomic_DNA.
DR   PIR; A43765; A43765.
DR   RefSeq; NP_594742.1; -.
DR   GeneID; 2541740; -.
DR   KEGG; spo:SPAC20G4.07c; -.
DR   NMPDR; fig|4896.1.peg.4712; -.
DR   GeneDB_Spombe; SPAC20G4.07c; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-002820-MON; -.
DR   ArrayExpress; P36209; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000246; F:delta24(24-1) sterol reductase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0043157; P:response to cation stress; IMP:GeneDB_SPombe.
DR   GO; GO:0042493; P:response to drug; IMP:GeneDB_SPombe.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001171; ERG4_ERG24.
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   Complete proteome; Lipid synthesis; Membrane; NADP; Oxidoreductase;
KW   Steroid biosynthesis; Sterol biosynthesis; Transmembrane.
FT   CHAIN         1    453       Delta(24(24(1)))-sterol reductase.
FT                                /FTId=PRO_0000207492.
FT   TRANSMEM     13     33       Potential.
FT   TRANSMEM     77     97       Potential.
FT   TRANSMEM    118    138       Potential.
FT   TRANSMEM    153    173       Potential.
FT   TRANSMEM    209    229       Potential.
FT   TRANSMEM    278    298       Potential.
FT   TRANSMEM    311    331       Potential.
FT   TRANSMEM    399    419       Potential.
FT   CONFLICT    412    412       C -> S (in Ref. 1; CAA45113).
SQ   SEQUENCE   453 AA;  52546 MW;  4740B6EE3BBD27CF CRC64;
     MKSTVKKSAP REFGGAKGAL AIMTGFPCLM YYLWACSKFN DSQFIKPESF TIAGFQNFFR
     TLGHYIYVGA YPTRYAFLVF WSFCIVQAVM YLTLPGVRTQ GLPLKHRNNE RLPYLCNAIW
     SFYTTIVILA VLHVTHVFPI TTFIDMFGPL MSVAIITAFV CTFVLYTGTL LFGDRLFDKP
     HRLSGNPIYD AFMGACLNPR LGKLLDFKMF FEVRIPWFIL FFISVGAAVR QYETYGTVSP
     QVLFVCLGHY LYANACSKGE QLIVPTWDMA YEKFGFMLIF WNMAGVPFTY SHCTLYLFSH
     DPSVYNWSTQ YTTGIYVLLL CCYYIFDTCN GQKNHFRNQI YGTEVHRKTF PQLPWLIIKN
     PTFIRCANGG TLLTSGWYRY ARKIHYTADF FQSLSWALIT GFQSPLPYFY PCFFFVVLVH
     RVSRDIKKCK AKYGADFDEY CRICPYLFIP YIF
//