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   27-NOV-2024, entry version 150.
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 = isopentenyl diphosphate +
CC         ADP + phosphate + CO2; 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   PaxDb; 10090-ENSMUSP00000006692; -.
DR   ProteomicsDB; 287333; -.
DR   Pumba; Q99JF5; -.
DR   Antibodypedia; 30739; 194 antibodies from 27 providers.
DR   DNASU; 192156; -.
DR   Ensembl; ENSMUST00000006692.6; ENSMUSP00000006692.5; ENSMUSG00000006517.6.
DR   GeneID; 192156; -.
DR   KEGG; mmu:192156; -.
DR   UCSC; uc009nss.2; mouse.
DR   AGR; MGI:2179327; -.
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; 458712at2759; -.
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 81 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 201 other cell types or tissues.
DR   ExpressionAtlas; Q99JF5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:InterPro.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   FunFam; 3.30.230.10:FF:000018; Diphosphomevalonate decarboxylase; 1.
DR   FunFam; 3.30.70.890:FF:000005; Diphosphomevalonate decarboxylase; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR005935; Mev_decarb.
DR   InterPro; IPR029765; Mev_diP_decarb.
DR   InterPro; IPR053859; MVD-like_N.
DR   InterPro; IPR041431; Mvd1_C.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR01240; mevDPdecarb; 1.
DR   PANTHER; PTHR10977; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR10977:SF3; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR   Pfam; PF18376; MDD_C; 1.
DR   Pfam; PF22700; MVD-like_N; 1.
DR   PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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
//