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UniProtKB/Swiss-Prot entry P14773


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

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Entry information
Entry name HMDH_DROME
Primary accession number P14773
Secondary accession numbers A4V3A8 Q9VCI8
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on May 24, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 86)
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: Hmgcr
Synonyms: HmG-CoAR
ORFNames: CG10367
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ENZYME REGULATION.
PubMed=3136321 [NCBI, ExPASy, EBI, Israel, Japan]
Gertler F.B., Chiu C.-Y., Richter-Mann L., Chin D.J.;
"Developmental and metabolic regulation of the Drosophila melanogaster 3-hydroxy-3-methylglutaryl coenzyme A reductase.";
Mol. Cell. Biol. 8:2713-2721(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1038/24871; PubMed=9853754 [NCBI, ExPASy, EBI, Israel, Japan]
Van Doren M., Broihier H.T., Moore L.A., Lehmann R.;
"HMG-CoA reductase guides migrating primordial germ cells.";
Nature 396:466-469(1998).
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
M21329; AAA28608.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAF56175.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAS65198.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S32572; S32572.
RefSeq NP_732900.1; -.
NP_996271.1; -.
UniGene Dm.21259
3D structure databases
HSSP P04035; 1HW8. [HSSP ENTRY / PDB]
ModBase P14773.
Organism-specific databases
FlyBase FBgn0001205; Hmgcr.
Gene expression databases
ArrayExpress P14773; -.
GermOnline CG10367; Drosophila melanogaster.
Ontologies
GO
GO:0005622; Cellular component: intracellular (traceable author statement from FlyBase).
GO:0035050; Biological process: embryonic heart tube development (inferred from mutant phenotype from FlyBase).
GO:0035232; Biological process: germ cell attraction (traceable author statement from FlyBase).
GO:0008406; Biological process: gonad development (traceable author statement from FlyBase).
GO:0008299; Biological process: isoprenoid biosynthetic process (traceable author statement from FlyBase).
GO:0007280; Biological process: pole cell migration (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002202; HMG_CoA_Rdtase_cat.
IPR004554; HMG_CoA_Rdtase_I_cat.
IPR004816; HMG_CoA_Rdtase_I_metazoan.
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 TIGR00920; 2A060605; 1.
TIGR00533; HMG_CoA_R_NADP; 1.
PROSITE PS00066; HMG_COA_REDUCTASE_1; 1.
PS00318; HMG_COA_REDUCTASE_2; 1.
PS01192; HMG_COA_REDUCTASE_3; 1.
PS50065; HMG_COA_REDUCTASE_4; 1.
PS50156; SSD; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P14773.
Genome annotation databases
Ensembl CG10367; Drosophila melanogaster. [Contig view]
GeneID 42803; -.
KEGG dme:Dmel_CG10367; -.
Phylogenomic databases
HOGENOM P14773; -.
Other
ProtoNet P14773.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; Glycoprotein; Isoprene biosynthesis; Membrane; NADP; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   920  920     3-hydroxy-3-methylglutaryl-coenzyme A reductase. PRO_0000114431
TRANSMEM   12    32  21     Potential. 
TRANSMEM   107   129  23     Potential. 
TRANSMEM   136   156  21     Potential. 
TRANSMEM   170   190  21     Potential. 
TRANSMEM   208   228  21     Potential. 
TRANSMEM   237   257  21     Potential. 
TRANSMEM   364   384  21     Potential. 
DOMAIN   106   263  158     SSD. 
REGION   385   498  114     Linker. 
REGION   499   829  331     Catalytic. 
ACT_SITE   586   586        Charge relay system (By similarity). 
ACT_SITE   717   717        Charge relay system (By similarity). 
ACT_SITE   793   793        Charge relay system (By similarity). 
ACT_SITE   892   892        Proton donor (By similarity). 
CARBOHYD   37    37        N-linked (GlcNAc...) (Potential). 
CARBOHYD   342   342        N-linked (GlcNAc...) (Potential). 
CARBOHYD   346   346        N-linked (GlcNAc...) (Potential). 
CARBOHYD   443   443        N-linked (GlcNAc...) (Potential). 
CARBOHYD   475   475        N-linked (GlcNAc...) (Potential). 
CARBOHYD   797   797        N-linked (GlcNAc...) (Potential). 
CARBOHYD   802   802        N-linked (GlcNAc...) (Potential). 
CARBOHYD   896   896        N-linked (GlcNAc...) (Potential). 
CARBOHYD   910   910        N-linked (GlcNAc...) (Potential). 
CONFLICT   4     4        R -> P (in Ref. 1; AAA28608). 
CONFLICT   9    11        HGE -> TQ (in Ref. 1; AAA28608). 
CONFLICT   33    49        TVDKNNTLDASSGLGTA -> NGGQEQYPGCEQRIGHS (in Ref. 1; AAA28608). 
CONFLICT   58    58        Missing (in Ref. 1; AAA28608). 
CONFLICT   186   191        AQLALS -> RSGAM (in Ref. 1; AAA28608). 
CONFLICT   220   220        E -> V (in Ref. 1; AAA28608). 
CONFLICT   286   286        L -> P (in Ref. 1; AAA28608). 
CONFLICT   321   330        VAFSGSDYDA -> EVSPAATTM (in Ref. 1; AAA28608). 
CONFLICT   403   403        A -> E (in Ref. 1; AAA28608). 
CONFLICT   680   680        A -> R (in Ref. 1; AAA28608). 
CONFLICT   689   700        GAEMALRRIQLQ -> ALRWPFAEFTLH (in Ref. 1; AAA28608). 
Sequence information
Length: 920 AA [This is the length of the unprocessed precursor] Molecular weight: 98317 Da [This is the MW of the unprocessed precursor] CRC64: C2E3959EAF339841 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIGRLFRAHG EFCASHPWEV IVALLTITAC MLTVDKNNTL DASSGLGTAT ASAAAAGGSG 

        70         80         90        100        110        120 
SGAGSGASGT IPPSSMGGSA TSSRHRPCHG WSQSCDGLEA EYNAADVILM TIVRCTAVLY 

       130        140        150        160        170        180 
CYYQFCSLHR LGSKYVLGIA GLFTVFSSFI FTTAIIKFLG SDISELKDAL FFLLLVIDLS 

       190        200        210        220        230        240 
NSGRLAQLAL SGSNQAEVTQ NIARGLELLG PAISLDTIVE VLLVGVGTLS GVQRLEVLCM 

       250        260        270        280        290        300 
FAVLSVLVNY VVFMTFYPAC LSLIFDLSRS GVDMSVVREK AKGSLLLKSL TEEEQKANPV 

       310        320        330        340        350        360 
LQRVKLIMTT GLMAVHIYSR VAFSGSDYDA VDKTLTPTLS LNVSNNRTES GEIADIIIKW 

       370        380        390        400        410        420 
LTMSADHIVI SIVLIALVVK FICFDNRDPL PDQLRQSGPV AIAAKASQTT PIDEEHVEQE 

       430        440        450        460        470        480 
KDTENSAAVR TLLFTIEDQS SANASTQTDL LPLRHRLVGP IKPPRPVQEC LDILNSTEEG 

       490        500        510        520        530        540 
SGPAALSDEE IVSIVHAGGT HCPLHKIESV LDDPERGVRI RRQIIGSRAK MPVGRLDVLP 

       550        560        570        580        590        600 
YEHFDYRKVL NACCENVLGY VPIPVGYAGP LLLDGETYYV PMATTEGALV ASTNRGCKAL 

       610        620        630        640        650        660 
SVRGVRSVVE DVGMTRAPCV RFPSVARAAE AKSWIENDEN YRVVKTEFDS TSRFGRLKDC 

       670        680        690        700        710        720 
HIAMDGPQLY IRFVAITGDA MGMNMVSKGA EMALRRIQLQ FPDMQIISLS GNFCCDKKPA 

       730        740        750        760        770        780 
AINWIKGRGK RVVTECTISA ATLRSVLKTD AKTLVECNKL KNMGGSAMAG SIGGNNAHAA 

       790        800        810        820        830        840 
NMVTAVFLAT GQDPAQNVTS SNCSTAMECW AENSEDLYMT CTMPSLEVGT VGGGTGLPGQ 

       850        860        870        880        890        900 
SACLEMLGVR GAHATRPGDN AKKLAQIVCA TVMAGELSLM AALVNSDLVK SHMRHNRSSI 

       910        920 
AVNSANNPLN VTVSSCSTIS 

P14773 in FASTA format

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