MVD1_MOUSE
ID MVD1_MOUSE Reviewed; 401 AA.
AC Q99JF5; Q3TCD8; Q8BTM4; Q922D7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Diphosphomevalonate decarboxylase;
DE EC=4.1.1.33 {ECO:0000250|UniProtKB:P53602};
DE AltName: Full=Mevalonate (diphospho)decarboxylase;
DE Short=MDDase;
DE AltName: Full=Mevalonate pyrophosphate decarboxylase;
GN Name=Mvd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Van Veldhoven P.P.;
RT "Search for PTS2 proteins.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12736493; DOI=10.1248/bpb.26.579;
RA Michihara A., Akasaki K., Yamori Y., Tsuji H.;
RT "Subcellular distribution of mouse mevalonate pyrophosphate
RT decarboxylase.";
RL Biol. Pharm. Bull. 26:579-584(2003).
CC -!- FUNCTION: Catalyzes the ATP dependent decarboxylation of (R)-5-
CC diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in
CC the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP),
CC a key precursor for the biosynthesis of isoprenoids and sterol
CC synthesis. {ECO:0000250|UniProtKB:P53602}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl
CC diphosphate + phosphate; Xref=Rhea:RHEA:23732, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57557,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=4.1.1.33;
CC Evidence={ECO:0000250|UniProtKB:P53602};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P53602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12736493}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be located in the peroxisome (By
CC similarity). However, was later shown to be cytosolic
CC (PubMed:12736493). {ECO:0000250|UniProtKB:P53602,
CC ECO:0000269|PubMed:12736493}.
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DR EMBL; AJ309922; CAC35731.1; -; mRNA.
DR EMBL; AK089354; BAC40852.1; -; mRNA.
DR EMBL; AK154883; BAE32901.1; -; mRNA.
DR EMBL; AK170773; BAE42019.1; -; mRNA.
DR EMBL; BC008526; AAH08526.1; -; mRNA.
DR CCDS; CCDS22738.1; -.
DR RefSeq; NP_619597.2; NM_138656.2.
DR PDB; 3F0N; X-ray; 1.90 A; A/B=6-401.
DR PDBsum; 3F0N; -.
DR AlphaFoldDB; Q99JF5; -.
DR SMR; Q99JF5; -.
DR BioGRID; 228648; 19.
DR STRING; 10090.ENSMUSP00000006692; -.
DR iPTMnet; Q99JF5; -.
DR PhosphoSitePlus; Q99JF5; -.
DR EPD; Q99JF5; -.
DR MaxQB; Q99JF5; -.
DR PaxDb; Q99JF5; -.
DR PRIDE; Q99JF5; -.
DR ProteomicsDB; 287333; -.
DR Antibodypedia; 30739; 207 antibodies from 28 providers.
DR DNASU; 192156; -.
DR Ensembl; ENSMUST00000006692; ENSMUSP00000006692; ENSMUSG00000006517.
DR GeneID; 192156; -.
DR KEGG; mmu:192156; -.
DR UCSC; uc009nss.2; mouse.
DR CTD; 4597; -.
DR MGI; MGI:2179327; Mvd.
DR VEuPathDB; HostDB:ENSMUSG00000006517; -.
DR eggNOG; KOG2833; Eukaryota.
DR GeneTree; ENSGT00390000015359; -.
DR HOGENOM; CLU_040369_4_4_1; -.
DR InParanoid; Q99JF5; -.
DR OMA; LTLHAMM; -.
DR OrthoDB; 1065019at2759; -.
DR PhylomeDB; Q99JF5; -.
DR TreeFam; TF105952; -.
DR Reactome; R-MMU-191273; Cholesterol biosynthesis.
DR Reactome; R-MMU-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00063; -.
DR BioGRID-ORCS; 192156; 24 hits in 76 CRISPR screens.
DR ChiTaRS; Mvd; mouse.
DR EvolutionaryTrace; Q99JF5; -.
DR PRO; PR:Q99JF5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q99JF5; protein.
DR Bgee; ENSMUSG00000006517; Expressed in lip and 198 other tissues.
DR ExpressionAtlas; Q99JF5; baseline and differential.
DR Genevisible; Q99JF5; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; ISO:MGI.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR005935; Mev_decarb.
DR InterPro; IPR029765; Mev_diP_decarb.
DR InterPro; IPR041431; Mvd1_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF18376; MDD_C; 1.
DR PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR01240; mevDPdecarb; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cholesterol biosynthesis;
KW Cholesterol metabolism; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Nucleotide-binding; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P53602"
FT CHAIN 2..401
FT /note="Diphosphomevalonate decarboxylase"
FT /id="PRO_0000087013"
FT BINDING 24..27
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 79
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 157..162
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 213
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P53602"
FT CONFLICT 229
FT /note="R -> Q (in Ref. 2; BAE32901/BAC40852)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="V -> G (in Ref. 1; CAC35731)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="A -> G (in Ref. 1; CAC35731)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="A -> V (in Ref. 2; BAE32901/BAC40852)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Q -> H (in Ref. 2; BAE42019 and 3; AAH08526)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="A -> V (in Ref. 3; AAH08526)"
FT /evidence="ECO:0000305"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3F0N"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3F0N"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 127..143
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 250..269
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 280..296
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 367..376
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:3F0N"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:3F0N"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:3F0N"
SQ SEQUENCE 401 AA; 44072 MW; BDF58921709C55AE CRC64;
MASEKPQDLM VTCTAPVNIA VIKYWGKRDE ALILPINSSL SVTLHQDQLK TTTTVAISKD
FTEDRIWLNG REEDVGQPRL QACLREIRRL ARKRRSTEDG DTLPLSLSYK VHVASVNNFP
TAAGLASSAA GYACLAYTLA QVYGVEGDLS EVARRGSGSA CRSLYGGFVE WQMGEQADGK
DSIARQIAPE WHWPQLRILI LVVSADKKQT GSTVGMQTSV ETSTLLKFRA ESVVPERMKE
MTRCIQEQDF QGFAQLTMKD SNQFHATCLD TFPPISYLND TSRRIIQLVH RFNTHQGQTK
VAYTFDAGPN AVIFTLEDTV AEFVAAVRHS FPPAANGDKF LKGLQVAPVL LSDELKAALA
VEPSPGGVQY IIATQVGPGP QVLDDTHDHL LGQDGLPQRD L
