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UniProtKB/Swiss-Prot entry P36209


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

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Entry information
Entry name STS1_SCHPO
Primary accession number P36209
Secondary accession number O13891
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on July 15, 1998 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 55)
Name and origin of the protein
Protein name Delta(24(24(1)))-sterol reductase
Synonyms EC 1.3.1.71
Sterol Delta(24(28))-reductase
C-24(28) sterol reductase
Gene name
Name: sts1
ORFNames: SPAC20G4.07c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1320960 [NCBI, ExPASy, EBI, Israel, Japan]
Shimanuki M., Goebl M., Yanagida M., Toda T.;
"Fission yeast sts1+ gene encodes a protein similar to the chicken lamin B receptor and is implicated in pleiotropic drug-sensitivity, divalent cation-sensitivity, and osmoregulation.";
Mol. Biol. Cell 3:263-273(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
CHARACTERIZATION.
DOI=10.1016/0378-1119(94)90728-5; PubMed=8125337 [NCBI, ExPASy, EBI, Israel, Japan]
Lai M.H., Bard M., Pierson C.A., Alexander J.F., Goebl M., Carter G.T., Kirsch D.R.;
"The identification of a gene family in the Saccharomyces cerevisiae ergosterol biosynthesis pathway.";
Gene 140:41-49(1994).
Comments
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
X63549; CAA45113.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329670; CAB11256.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A43765; A43765.
RefSeq NP_594742.1; -.
3D structure databases
ModBase P36209.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-002820-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC20G4.07c; -.
Gene expression databases
ArrayExpress P36209; -.
Ontologies
GO
GO:0043157; Biological process: response to cation stress (inferred from mutant phenotype from GeneDB_SPombe).
GO:0042493; Biological process: response to drug (inferred from mutant phenotype from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR001171; ERG4_ERG24.
Graphical view of domain structure.
Pfam PF01222; ERG4_ERG24; 1.
Pfam graphical view of domain structure.
PROSITE PS01017; STEROL_REDUCT_1; 1.
PS01018; STEROL_REDUCT_2; 1.
BLOCKS P36209.
Genome annotation databases
GeneID 2541740; -.
KEGG spo:SPAC20G4.07c; -.
NMPDR fig|4896.1.peg.4712; -.
Other
ProtoNet P36209.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Lipid synthesis; Membrane; NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   453  453     Delta(24(24(1)))-sterol reductase. PRO_0000207492
TRANSMEM   13    33  21     Potential. 
TRANSMEM   77    97  21     Potential. 
TRANSMEM   118   138  21     Potential. 
TRANSMEM   153   173  21     Potential. 
TRANSMEM   209   229  21     Potential. 
TRANSMEM   278   298  21     Potential. 
TRANSMEM   311   331  21     Potential. 
TRANSMEM   399   419  21     Potential. 
CONFLICT   412   412        C -> S (in Ref. 1; CAA45113). 
Sequence information
Length: 453 AA [This is the length of the unprocessed precursor] Molecular weight: 52546 Da [This is the MW of the unprocessed precursor] CRC64: 4740B6EE3BBD27CF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKSTVKKSAP REFGGAKGAL AIMTGFPCLM YYLWACSKFN DSQFIKPESF TIAGFQNFFR 

        70         80         90        100        110        120 
TLGHYIYVGA YPTRYAFLVF WSFCIVQAVM YLTLPGVRTQ GLPLKHRNNE RLPYLCNAIW 

       130        140        150        160        170        180 
SFYTTIVILA VLHVTHVFPI TTFIDMFGPL MSVAIITAFV CTFVLYTGTL LFGDRLFDKP 

       190        200        210        220        230        240 
HRLSGNPIYD AFMGACLNPR LGKLLDFKMF FEVRIPWFIL FFISVGAAVR QYETYGTVSP 

       250        260        270        280        290        300 
QVLFVCLGHY LYANACSKGE QLIVPTWDMA YEKFGFMLIF WNMAGVPFTY SHCTLYLFSH 

       310        320        330        340        350        360 
DPSVYNWSTQ YTTGIYVLLL CCYYIFDTCN GQKNHFRNQI YGTEVHRKTF PQLPWLIIKN 

       370        380        390        400        410        420 
PTFIRCANGG TLLTSGWYRY ARKIHYTADF FQSLSWALIT GFQSPLPYFY PCFFFVVLVH 

       430        440        450 
RVSRDIKKCK AKYGADFDEY CRICPYLFIP YIF 

P36209 in FASTA format

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