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UniProtKB/Swiss-Prot entry Q10283


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

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Entry information
Entry name HMDH_SCHPO
Primary accession number Q10283
Secondary accession number O74425
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 65)
Name and origin of the protein
Protein name 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Synonyms HMG-CoA reductase
EC 1.1.1.34
Gene name
Name: hmg1
ORFNames: SPCC162.09c
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].
DOI=10.1002/(SICI)1097-0061(19960915)12:11<1107::AID-YEA992>3.3.CO;2-5; PubMed=8896278 [NCBI, ExPASy, EBI, Israel, Japan]
Lum P.Y., Edwards S., Wright R.;
"Molecular, functional and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces pombe.";
Yeast 12:1107-1124(1996).
[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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1024 AND THR-1028, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
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
L76979; AAB39277.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329672; CAA19589.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S72194; S72194.
RefSeq NP_588235.1; -.
3D structure databases
HSSP P04035; 1DQA. [HSSP ENTRY / PDB]
ModBase Q10283.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-000166-MON; -.
Organism-specific databases
GeneDB_Spombe SPCC162.09c; -.
Gene expression databases
ArrayExpress Q10283; -.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (inferred from direct assay from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR002202; HMG_CoA_Rdtase_cat.
IPR004554; HMG_CoA_Rdtase_I_cat.
IPR000731; SSD_5TM.
Graphical view of domain structure.
Gene3D G3DSA:3.90.770.10; HMG-CoA_red; 1.
PANTHER PTHR10572; HMG-CoA_red; 1.
Pfam PF00368; HMG-CoA_red; 1.
Pfam graphical view of domain structure.
PRINTS PR00071; HMGCOARDTASE.
TIGRFAMs TIGR00533; HMG_CoA_R_NADP; 1.
PROSITE PS00066; HMG_COA_REDUCTASE_1; 1.
PS00318; HMG_COA_REDUCTASE_2; 1.
PS01192; HMG_COA_REDUCTASE_3; FALSE_NEG.
PS50065; HMG_COA_REDUCTASE_4; 1.
PS50156; SSD; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q10283.
Genome annotation databases
GeneID 2538999; -.
KEGG spo:SPCC162.09c; -.
NMPDR fig|4896.1.peg.573; -.
Other
ProtoNet Q10283.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cholesterol biosynthesis; Complete proteome; Endoplasmic reticulum; Glycoprotein; Lipid synthesis; Membrane; NADP; Oxidoreductase; Phosphoprotein; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1053  1053     3-hydroxy-3-methylglutaryl-coenzyme A reductase. PRO_0000114455
TRANSMEM   9     29  21     Potential. 
TRANSMEM   204    224  21     Potential. 
TRANSMEM   233    253  21     Potential. 
TRANSMEM   259    279  21     Potential. 
TRANSMEM   321    341  21     Potential. 
TRANSMEM   342    362  21     Potential. 
TRANSMEM   418    438  21     Potential. 
TRANSMEM   527    547  21     Potential. 
REGION   548    615  68     Linker. 
REGION   616   1053  438     Catalytic. 
ACT_SITE   712    712        Charge relay system (By similarity). 
ACT_SITE   846    846        Charge relay system (By similarity). 
ACT_SITE   922    922        Charge relay system (By similarity). 
ACT_SITE   1018   1018        Proton donor (By similarity). 
MOD_RES   1024   1024        Phosphoserine. 
MOD_RES   1028   1028        Phosphothreonine. 
CARBOHYD   137    137        N-linked (GlcNAc...) (Potential). 
CARBOHYD   399    399        N-linked (GlcNAc...) (Potential). 
CARBOHYD   518    518        N-linked (GlcNAc...) (Potential). 
CARBOHYD   578    578        N-linked (GlcNAc...) (Potential). 
CARBOHYD   776    776        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1022   1022        N-linked (GlcNAc...) (Potential). 
CONFLICT   751    751        N -> D (in Ref. 1; AAB39277). 
Sequence information
Length: 1053 AA [This is the length of the unprocessed precursor] Molecular weight: 114877 Da [This is the MW of the unprocessed precursor] CRC64: 33E5C2365222D238 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIYKLAARYP IQVIAIVGIL VSMAYFSFLE ALTQEDFPVL IRALKRFGIL DGFPNTRLPN 

        70         80         90        100        110        120 
EMILKLSSVQ GEDASVWEQI PAAELGGEGF VDFDITQWYY PANAKVDVAQ LVEPYRNDCI 

       130        140        150        160        170        180 
FHDASGACHF FFKEVGNWTV SSIALPSNLA NPPIDYFLDS SSTVIQRILP AIREHGISWS 

       190        200        210        220        230        240 
WLLQLIARTW MNTLKIASQA SKTELLIVGT AYACMLISIV SLYLKMRRLG SKFWLFFSVL 

       250        260        270        280        290        300 
LSTLFSVQFA MTLVRASGVR ISLVSLIESL PFLINVVALD KAAELTRQVI TRCSVSDSHS 

       310        320        330        340        350        360 
PMHEDIAKAC RNAAPPILRH FSFGIVVLAI FSYCNFGIKQ FFLFAAVMIY DLLLLFSFFV 

       370        380        390        400        410        420 
AILTLKLEMR RYNAKDDVRK VLIEEGLSES TARHVADGND SSATTSAGSR YFKVRYGTKI 

       430        440        450        460        470        480 
ILFIFIAFNL FELCSIPFKH YAATSAAAAR LIPLVRSQYP DFKSQRLLDD GVFDDVLSAI 

       490        500        510        520        530        540 
SSMSNIESPS VRLLPAVFYG AELSSTSFLS TIHSFINNWS HYISASFLSK WIVCALSLSI 

       550        560        570        580        590        600 
AVNVFLLNAA RLNSIKEEPE KKVVEKVVEV VKYIPSSNSS SIDDIQKDEI AQESVVRSLE 

       610        620        630        640        650        660 
ECITLYNNGQ ISTLNDEEVV QLTLAKKIPL YALERVLKDV TRAVVIRRTV VSRSSRTKTL 

       670        680        690        700        710        720 
ESSNCPVYHY DYSRVLNACC ENVIGYMPLP LGVAGPLIID GKPFYIPMAT TEGALVASTM 

       730        740        750        760        770        780 
RGCKAINAGG GAVTVLTRDQ MSRGPCVAFP NLTRAGRAKI WLDSPEGQEV MKKAFNSTSR 

       790        800        810        820        830        840 
FARLQHIKTA LAGTRLFIRF CTSTGDAMGM NMISKGVEHA LVVMSNDAGF DDMQVISVSG 

       850        860        870        880        890        900 
NYCTDKKPAA INWIDGRGKS VIAEAIIPGD AVKSVLKTTV EDLVKLNVDK NLIGSAMAGS 

       910        920        930        940        950        960 
VGGFNAHAAN IVTAVYLATG QDPAQNVESS NCITLMDNVD GNLQLSVSMP SIEVGTIGGG 

       970        980        990       1000       1010       1020 
TVLEPQGAML DLLGVRGAHM TSPGDNSRQL ARVVAAAVMA GELSLCSALA SGHLVKSHIG 

      1030       1040       1050 
LNRSALNTPA MDSSAKKPAT DALKSVNSRV PGR 

Q10283 in FASTA format

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