ID  P12684;
PN  3-hydroxy-3-methylglutaryl-coenzyme A reductase 2;
GN  HMG2;
OS  559292;
SL  Nucleus Position: SL-0178;
SL  Comments: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8744950}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:14562095}.
DR  UNIPROT: P12684;
DR  UNIPROT: D6VZ84;
DR  UNIPROT: E9P8X3;
DR  Pfam: PF00368;
DR  Pfam: PF13323;
DR  Pfam: PF12349;
DR  PROSITE: PS00066;
DR  PROSITE: PS00318;
DR  PROSITE: PS01192;
DR  PROSITE: PS50065;
DR  PROSITE: PS50156;
DE  Function: HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway constitutes by the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:3065625, PubMed:3526336). HMG1 and HMG2 catalyze the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate that is the rate- limiting step within the first mosule (PubMed:3526336). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl- CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3- methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are derived from a single ancestral HMGR gene by gene duplication (PubMed:32679672). {ECO:0000269|PubMed:3065625, ECO:0000269|PubMed:3526336, ECO:0000303|PubMed:32679672}.
DE  Reference Proteome: Yes;
DE  Interaction: P12683; IntAct: EBI-803408; Score: 0.67
DE  Interaction: Q06449; IntAct: EBI-601343; Score: 0.37
DE  Interaction: P38219; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P16140; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P09733; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P36008; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P02994; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P11484; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P33299; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P40069; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P30822; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P00330; IntAct: EBI-787291; Score: 0.35
DE  Interaction: P40341; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P16521; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P10592; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P26783; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P32905; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P26321; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P38706; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P41805; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P41940; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P12709; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P06169; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P04147; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P15108; IntAct: EBI-806785; Score: 0.35
DE  Interaction: P39925; IntAct: EBI-806785; Score: 0.35
DE  Interaction: Q02159; IntAct: EBI-860875; Score: 0.00
DE  Interaction: P25694; IntAct: EBI-1008636; Score: 0.35
DE  Interaction: P53044; IntAct: EBI-1008636; Score: 0.35
DE  Interaction: Q04228; IntAct: EBI-1008636; Score: 0.35
DE  Interaction: Q03010; IntAct: EBI-6316649; Score: 0.00
DE  Interaction: P38837; IntAct: EBI-6316638; Score: 0.00
DE  Interaction: P12684; IntAct: EBI-21320996; Score: 0.55
DE  Interaction: Q12469; IntAct: EBI-16282981; Score: 0.35
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0005635;
GO  GO:0034399;
GO  GO:0005778;
GO  GO:0000502;
GO  GO:0004420;
GO  GO:0015936;
GO  GO:0006696;
GO  GO:0008299;
GO  GO:0016126;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSLPLKTIVHLVKPFACTARFSARYPIHVIVVAVLLSAAAYLSVTQSYLNEWKLDSNQYSTYLSIKPDELFEKCTHYYRS
SQ  PVSDTWKLLSSKEAADIYTPFHYYLSTISFQSKDNSTTLPSLDDVIYSVDHTRYLLSEEPKIPTELVSENGTKWRLRNNS
SQ  NFILDLHNIYRNMVKQFSNKTSEFDQFDLFIILAAYLTLFYTLCCLFNDMRKIGSKFWLSFSALSNSACALYLSLYTTHS
SQ  LLKKPASLLSLVIGLPFIVVIIGFKHKVRLAAFSLQKFHRISIDKKITVSNIIYEAMFQEGAYLIRDYLFYISSFIGCAI
SQ  YARHLPGLVNFCILSTFMLVFDLLLSATFYSAILSMKLEINIIHRSTVIRQTLEEDGVVPTTADIIYKDETASEPHFLRS
SQ  NVAIILGKASVIGLLLLINLYVFTDKLNATILNTVYFDSTIYSLPNFINYKDIGNLSNQVIISVLPKQYYTPLKKYHQIE
SQ  DSVLLIIDSVSNAIRDQFISKLLFFAFAVSISINVYLLNAAKIHTGYMNFQPQSNKIDDLVVQQKSATIEFSETRSMPAS
SQ  SGLETPVTAKDIIISEEIQNNECVYALSSQDEPIRPLSNLVELMEKEQLKNMNNTEVSNLVVNGKLPLYSLEKKLEDTTR
SQ  AVLVRRKALSTLAESPILVSEKLPFRNYDYDRVFGACCENVIGYMPIPVGVIGPLIIDGTSYHIPMATTEGCLVASAMRG
SQ  CKAINAGGGATTVLTKDGMTRGPVVRFPTLIRSGACKIWLDSEEGQNSIKKAFNSTSRFARLQHIQTCLAGDLLFMRFRT
SQ  TTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVKSVLKSDVSA
SQ  LVELNISKNLVGSAMAGSVGGFNAHAANLVTALFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIGGGTV
SQ  LEPQGAMLDLLGVRGPHPTEPGANARQLARIIACAVLAGELSLCSALAAGHLVQSHMTHNRKTNKANELPQPSNKGPPCK
SQ  TSALL
//