MVD1_RAT
ID MVD1_RAT Reviewed; 401 AA.
AC Q62967; Q642E5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 125.
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; Synonyms=Mpd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pheochromocytoma;
RA Jeng C.-J., Schweitzer E.S.;
RT "Rat mevalonate pyrophosphate decarboxylase.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11725955; DOI=10.1248/bpb.24.1235;
RA Michihara A., Sawamura M., Yamori Y., Akasaki K., Tsuji H.;
RT "Mevalonate pyrophosphate decarboxylase is predominantly located in the
RT cytosol of rat hepatocytes.";
RL Biol. Pharm. Bull. 24:1235-1240(2001).
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:11725955}.
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:11725955). {ECO:0000250|UniProtKB:P53602,
CC ECO:0000269|PubMed:11725955}.
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DR EMBL; U53706; AAB00192.1; -; mRNA.
DR EMBL; AABR07072659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473972; EDL92747.1; -; Genomic_DNA.
DR EMBL; BC081784; AAH81784.1; -; mRNA.
DR RefSeq; NP_112324.1; NM_031062.2.
DR AlphaFoldDB; Q62967; -.
DR SMR; Q62967; -.
DR STRING; 10116.ENSRNOP00000018145; -.
DR ChEMBL; CHEMBL4296309; -.
DR GuidetoPHARMACOLOGY; 642; -.
DR iPTMnet; Q62967; -.
DR PhosphoSitePlus; Q62967; -.
DR jPOST; Q62967; -.
DR PaxDb; Q62967; -.
DR PRIDE; Q62967; -.
DR GeneID; 81726; -.
DR KEGG; rno:81726; -.
DR UCSC; RGD:621292; rat.
DR CTD; 4597; -.
DR RGD; 621292; Mvd.
DR VEuPathDB; HostDB:ENSRNOG00000013376; -.
DR eggNOG; KOG2833; Eukaryota.
DR HOGENOM; CLU_040369_4_4_1; -.
DR InParanoid; Q62967; -.
DR OMA; LTLHAMM; -.
DR OrthoDB; 1065019at2759; -.
DR PhylomeDB; Q62967; -.
DR TreeFam; TF105952; -.
DR BRENDA; 4.1.1.33; 5301.
DR Reactome; R-RNO-191273; Cholesterol biosynthesis.
DR Reactome; R-RNO-446199; Synthesis of Dolichyl-phosphate.
DR SABIO-RK; Q62967; -.
DR UniPathway; UPA00063; -.
DR PRO; PR:Q62967; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Proteomes; UP000234681; Chromosome 19.
DR Bgee; ENSRNOG00000013376; Expressed in ovary and 20 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IDA:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0006695; P:cholesterol biosynthetic process; NAS:RGD.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IDA:RGD.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 Acetylation; ATP-binding; Cholesterol biosynthesis; Cholesterol metabolism;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Lyase; Nucleotide-binding;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW 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_0000087014"
FT REGION 382..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 38
FT /note="S -> P (in Ref. 1; AAB00192)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 43893 MW; B23F5BC857957118 CRC64;
MASEKPQDLM VTCTAPVNIA VIKYWGKRDE ALILPINSSL SVTLHQDQLK TTTTAAISKD
FTEDRIWLNG REEDVGQPRL QACLREIRRL ARKRRSTGDG DALPLSLGYK VHVASVNNFP
TAAGLASSAA GYACLAYTLA RVYGVEGDLS EVARRGSGSA CRSLYGGFVE WQMGEQADGK
DSIARQIAPE WHWPQLRVLI LVVSAEKKPT GSTVGMQTSV ATSTLLKFRA ESIVPERMKE
MTRCIQEQDF QAFAQLTMKD SNQFHATCLD TFPPISYLND TSRRIIQLVH RFNAHHGQTK
VAYTFDAGPN AVIFTLEDTV AEFVAAVRHS FPPAANGDKF LKGLQVAPVL LSDELKTSLA
TEPSPGGVQY IIATQVGPGP QVLDDPHHHL LGPDGLPQRD L
