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Database: UniProt
Entry: A0A182R7M1_ANOFN
LinkDB: A0A182R7M1_ANOFN
Original site: A0A182R7M1_ANOFN 
ID   A0A182R7M1_ANOFN        Unreviewed;       924 AA.
AC   A0A182R7M1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 2.
DT   13-SEP-2023, entry version 32.
DE   RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase {ECO:0000256|ARBA:ARBA00016920};
DE            EC=1.1.1.34 {ECO:0000256|ARBA:ARBA00012999};
OS   Anopheles funestus (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN002171-PA, ECO:0000313|Proteomes:UP000075900};
RN   [1] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA   Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA   Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA   Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT   "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT   Middle East: occurrence data, distribution maps and bionomic precis.";
RL   Parasit. Vectors 3:117-117(2010).
RN   [2] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA   Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA   Besansky N.J.;
RT   "A chromosome-scale assembly of the major African malaria vector Anopheles
RT   funestus.";
RL   Gigascience 8:0-0(2019).
RN   [3] {ECO:0000313|EnsemblMetazoa:AFUN002171-PA}
RP   IDENTIFICATION.
RC   STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN002171-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00005084}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
CC       {ECO:0000256|ARBA:ARBA00007661}.
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DR   AlphaFoldDB; A0A182R7M1; -.
DR   STRING; 62324.A0A182R7M1; -.
DR   EnsemblMetazoa; AFUN002171-RA; AFUN002171-PA; AFUN002171.
DR   VEuPathDB; VectorBase:AFUN002171; -.
DR   VEuPathDB; VectorBase:AFUN2_010406; -.
DR   OrthoDB; 816560at2759; -.
DR   UniPathway; UPA00058; UER00103.
DR   Proteomes; UP000075900; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR   Gene3D; 1.10.3270.10; HMGR, N-terminal domain; 1.
DR   Gene3D; 3.30.70.420; Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain; 1.
DR   InterPro; IPR002202; HMG_CoA_Rdtase.
DR   InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf.
DR   InterPro; IPR023076; HMG_CoA_Rdtase_CS.
DR   InterPro; IPR004554; HMG_CoA_Rdtase_eu_arc.
DR   InterPro; IPR004816; HMG_CoA_Rdtase_metazoan.
DR   InterPro; IPR023282; HMG_CoA_Rdtase_N.
DR   InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR   InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR   InterPro; IPR000731; SSD.
DR   NCBIfam; TIGR00920; 2A060605; 1.
DR   PANTHER; PTHR10572; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR   PANTHER; PTHR10572:SF24; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE; 1.
DR   Pfam; PF00368; HMG-CoA_red; 1.
DR   Pfam; PF12349; Sterol-sensing; 1.
DR   PRINTS; PR00071; HMGCOARDTASE.
DR   SUPFAM; SSF55035; NAD-binding domain of HMG-CoA reductase; 1.
DR   SUPFAM; SSF56542; Substrate-binding domain of HMG-CoA reductase; 1.
DR   PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1.
DR   PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1.
DR   PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50156; SSD; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        76..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        213..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          78..235
FT                   /note="SSD"
FT                   /evidence="ECO:0000259|PROSITE:PS50156"
FT   REGION          437..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          897..924
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..462
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   924 AA;  101236 MW;  BE735277BD29BC1F CRC64;
     MRLGRLFRAH GEFCASHPWE VIIGLVSLTA CVLSIDKNNN VAQTADDPEQ LRSCTSWRYG
     QRTVDGGMCE EPTRNIIDII LMMLVRCTAI LYIYYHFCHL QKLGSKYILG LAALFALFSS
     FIFTTTVLNI LGCEISDLKD ALFLFLLLID LSRAGILAQL ALCGANQSEV TTNIARGMEV
     FGPAMSLDTL VEALVIGVGT LSGVQRLELL SGFAVLSALV NYIVFMTFYP ACLSLILELT
     HNGRNGVQQL NGERLIRHML LQEDCKPNPV VQRVKVIMSS GLFVVHVMSR FPNSDKESDA
     AEQIIASRAH EHLAAMNKTD TSEFSEMIMH LLSFSLEQIF TYILIITLGA KFLLFDRYHL
     SDHLIHAVAN EQEVAAAAAL NESRQQKQGP PAISTPPVTF TLAETVMVEE KATQSELSMI
     GNDRIGRKVR KHTLVEQNAE GEQLHETASD DDEEQVLLDS EEDEVEREPR PLEECVQILQ
     YDGHGKRLTD TEVEMIVRGC RSVCPLYKIE KIIDDAERGV RLRRSMLLKD AGCNAGLLKE
     LPYLNYDYSK VMDACCENVI GYVPIPVGYA GPLLLDGKKY FVPMATTEGA LVASTNRGCK
     AVSICGVTSY CEDIGMTRAP CVRFPNVLLA AQAKRWMESE VNFQRIKKAF DSTSRYARLQ
     DLYIAMDGPV LYIRFRAFTG DAMGMNMLSK GTEKALREIQ TVFPEGIISL SHYCSDKSAG
     INWIKGRGKR VVVKIVPADK LELIFRTNAR TLVQCNKLKN MTGSAVAGSI GGNNAHAANM
     VLPSSSRPGQ DPAQNVTSSN CSTNMETCGE MGEDLYITCT MPSLEVGTLG GGTGLPGQGA
     CLNLLGVRGS HPTNPAENSK QLARIICATV MAGGTESFVG IGHSDLVNSH MRHNRSSVAI
     NPNLHPPTPA LVKPAKEGEA STSS
//
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