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UniProtKB - P53602 (MVD1_HUMAN)

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Protein

Diphosphomevalonate decarboxylase

Gene

MVD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Performs the first committed step in the biosynthesis of isoprenes.

Catalytic activityi

ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2.1 Publication

Kineticsi

  1. KM=7.4 µM for (R)-5-diphosphomevalonate1 Publication
  2. KM=0.32 mM for ATP1 Publication

    Pathwayi: cholesterol biosynthesis

    This protein is involved in the pathway cholesterol biosynthesis, which is part of Steroid biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway cholesterol biosynthesis and in Steroid biosynthesis.

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • diphosphomevalonate decarboxylase activity Source: UniProtKB
    • Hsp70 protein binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    Keywordsi

    Molecular functionLyase
    Biological processCholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000167508-MONOMER
    BRENDAi4.1.1.33 2681
    ReactomeiR-HSA-191273 Cholesterol biosynthesis
    R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
    R-HSA-446199 Synthesis of Dolichyl-phosphate
    SABIO-RKiP53602
    UniPathwayiUPA00063

    Chemistry databases

    SwissLipidsiSLP:000001242

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diphosphomevalonate decarboxylase (EC:4.1.1.33)
    Alternative name(s):
    Mevalonate (diphospho)decarboxylase
    Short name:
    MDDase
    Mevalonate pyrophosphate decarboxylase
    Gene namesi
    Name:MVD
    Synonyms:MPD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    Proteomesi
    • UP000005640 Componenti: Chromosome 16

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000167508.10
    HGNCiHGNC:7529 MVD
    MIMi603236 gene
    neXtProtiNX_P53602

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Pathology & Biotechi

    Involvement in diseasei

    Porokeratosis 7, multiple types (POROK7)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported.
    See also OMIM:614714
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_075052101P → R in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs200033380Ensembl.1
    Natural variantiVAR_075053128A → V in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776358937Ensembl.1
    Natural variantiVAR_075054161R → L in POROK7; unknown pathological significance. 1 Publication1
    Natural variantiVAR_075055161R → Q in POROK7; 1000-fold diminution in specific activity. 2 PublicationsCorresponds to variant dbSNP:rs144010349Ensembl.1
    Natural variantiVAR_075056228R → Q in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs770939767Ensembl.1
    Natural variantiVAR_075057228R → W in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776684503Ensembl.1
    Natural variantiVAR_075058249F → S in POROK7. 1 PublicationCorresponds to variant dbSNP:rs761991070EnsemblClinVar.1
    Natural variantiVAR_075059292N → S in POROK7. 1 PublicationCorresponds to variant dbSNP:rs755948940EnsemblClinVar.1
    Natural variantiVAR_075060371Missing in POROK7; unknown pathological significance. 1 Publication1
    Natural variantiVAR_075061376G → R in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs546127665Ensembl.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi17N → A: 15-fold inflation in K(m) for mevalonate diphosphate. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi4597
    MalaCardsiMVD
    MIMi614714 phenotype
    OpenTargetsiENSG00000167508
    PharmGKBiPA31330

    Chemistry databases

    ChEMBLiCHEMBL4340
    GuidetoPHARMACOLOGYi642

    Polymorphism and mutation databases

    BioMutaiMVD
    DMDMi1706681

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000870122 – 400Diphosphomevalonate decarboxylaseAdd BLAST399

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1
    Modified residuei96PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiP53602
    MaxQBiP53602
    PaxDbiP53602
    PeptideAtlasiP53602
    PRIDEiP53602
    ProteomicsDBi56588

    PTM databases

    iPTMnetiP53602
    PhosphoSitePlusiP53602

    Expressioni

    Tissue specificityi

    Expressed in heart, skeletal muscle, lung, liver, brain, pancreas, kidney and placenta.1 Publication

    Gene expression databases

    BgeeiENSG00000167508
    CleanExiHS_MVD
    ExpressionAtlasiP53602 baseline and differential
    GenevisibleiP53602 HS

    Organism-specific databases

    HPAiHPA041404
    HPA048250

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    GO - Molecular functioni

    • Hsp70 protein binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    BioGridi110682, 37 interactors
    IntActiP53602, 9 interactors
    STRINGi9606.ENSP00000301012

    Chemistry databases

    BindingDBiP53602

    Structurei

    Secondary structure

    1400
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi10 – 14Combined sources5
    Beta strandi17 – 21Combined sources5
    Beta strandi26 – 28Combined sources3
    Turni29 – 32Combined sources4
    Beta strandi33 – 36Combined sources4
    Beta strandi38 – 43Combined sources6
    Turni45 – 47Combined sources3
    Beta strandi50 – 56Combined sources7
    Beta strandi64 – 67Combined sources4
    Helixi77 – 88Combined sources12
    Beta strandi110 – 118Combined sources9
    Turni120 – 122Combined sources3
    Helixi126 – 139Combined sources14
    Turni140 – 143Combined sources4
    Helixi149 – 155Combined sources7
    Helixi157 – 163Combined sources7
    Beta strandi164 – 170Combined sources7
    Beta strandi178 – 180Combined sources3
    Beta strandi183 – 187Combined sources5
    Helixi189 – 191Combined sources3
    Beta strandi195 – 202Combined sources8
    Helixi211 – 221Combined sources11
    Helixi223 – 231Combined sources9
    Helixi233 – 245Combined sources13
    Helixi249 – 268Combined sources20
    Beta strandi270 – 272Combined sources3
    Helixi279 – 295Combined sources17
    Beta strandi300 – 303Combined sources4
    Beta strandi306 – 308Combined sources3
    Beta strandi310 – 315Combined sources6
    Helixi316 – 318Combined sources3
    Helixi319 – 329Combined sources11
    Turni337 – 339Combined sources3
    Beta strandi340 – 343Combined sources4
    Helixi352 – 358Combined sources7
    Beta strandi366 – 375Combined sources10
    Helixi385 – 387Combined sources3
    Beta strandi392 – 394Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3D4JX-ray2.40A/B1-400[»]
    ProteinModelPortaliP53602
    SMRiP53602
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53602

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the diphosphomevalonate decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiKOG2833 Eukaryota
    COG3407 LUCA
    GeneTreeiENSGT00390000015359
    HOVERGENiHBG051503
    InParanoidiP53602
    KOiK01597
    OMAiLTLHAMM
    OrthoDBiEOG091G0EUU
    PhylomeDBiP53602
    TreeFamiTF105952

    Family and domain databases

    Gene3Di3.30.230.10, 1 hit
    3.30.70.890, 1 hit
    InterProiView protein in InterPro
    IPR036554 GHMP_kinase_C_sf
    IPR006204 GHMP_kinase_N_dom
    IPR005935 Mev_decarb
    IPR029765 Mev_diP_decarb
    IPR020568 Ribosomal_S5_D2-typ_fold
    IPR014721 Ribosomal_S5_D2-typ_fold_subgr
    PfamiView protein in Pfam
    PF00288 GHMP_kinases_N, 1 hit
    PIRSFiPIRSF015950 Mev_P_decrbx, 1 hit
    SUPFAMiSSF54211 SSF54211, 1 hit
    SSF55060 SSF55060, 1 hit
    TIGRFAMsiTIGR01240 mevDPdecarb, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P53602-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASEKPLAAV TCTAPVNIAV IKYWGKRDEE LVLPINSSLS VTLHQDQLKT 
            60         70         80         90        100
    TTTAVISKDF TEDRIWLNGR EEDVGQPRLQ ACLREIRCLA RKRRNSRDGD 
           110        120        130        140        150
    PLPSSLSCKV HVASVNNFPT AAGLASSAAG YACLAYTLAR VYGVESDLSE 
           160        170        180        190        200
    VARRGSGSAC RSLYGGFVEW QMGEQADGKD SIARQVAPES HWPELRVLIL 
           210        220        230        240        250
    VVSAEKKLTG STVGMRASVE TSPLLRFRAE SVVPARMAEM ARCIRERDFP 
           260        270        280        290        300
    SFAQLTMKDS NQFHATCLDT FPPISYLNAI SWRIIHLVHR FNAHHGDTKV 
           310        320        330        340        350
    AYTFDAGPNA VIFTLDDTVA EFVAAVWHGF PPGSNGDTFL KGLQVRPAPL 
           360        370        380        390        400
    SAELQAALAM EPTPGGVKYI IVTQVGPGPQ ILDDPCAHLL GPDGLPKPAA
    Length:400
    Mass (Da):43,405
    Last modified:October 1, 1996 - v1
    Checksum:i3FD4741BCC4B68D8
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_075052101P → R in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs200033380Ensembl.1
    Natural variantiVAR_075053128A → V in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776358937Ensembl.1
    Natural variantiVAR_075054161R → L in POROK7; unknown pathological significance. 1 Publication1
    Natural variantiVAR_075055161R → Q in POROK7; 1000-fold diminution in specific activity. 2 PublicationsCorresponds to variant dbSNP:rs144010349Ensembl.1
    Natural variantiVAR_075056228R → Q in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs770939767Ensembl.1
    Natural variantiVAR_075057228R → W in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776684503Ensembl.1
    Natural variantiVAR_075058249F → S in POROK7. 1 PublicationCorresponds to variant dbSNP:rs761991070EnsemblClinVar.1
    Natural variantiVAR_051605278N → H. Corresponds to variant dbSNP:rs34519538Ensembl.1
    Natural variantiVAR_075059292N → S in POROK7. 1 PublicationCorresponds to variant dbSNP:rs755948940EnsemblClinVar.1
    Natural variantiVAR_075060371Missing in POROK7; unknown pathological significance. 1 Publication1
    Natural variantiVAR_075061376G → R in POROK7; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs546127665Ensembl.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		U49260 mRNA Translation: AAC50440.1
    BT006930 mRNA Translation: AAP35576.1
    CH471184 Genomic DNA Translation: EAW66792.1
    BC000011 mRNA Translation: AAH00011.1
    CCDSiCCDS10968.1
    RefSeqiNP_002452.1, NM_002461.2
    UniGeneiHs.252457

    Genome annotation databases

    EnsembliENST00000301012; ENSP00000301012; ENSG00000167508
    GeneIDi4597
    KEGGihsa:4597
    UCSCiuc002flg.2 human

    Keywords - Coding sequence diversityi

    Polymorphism

    Similar proteinsi

    Entry informationi

    Entry nameiMVD1_HUMAN
    AccessioniPrimary (citable) accession number: P53602
    Secondary accession number(s): Q53Y65
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: June 20, 2018
    This is version 159 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

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