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Protein

Nucleoside diphosphate-linked moiety X motif 19

Gene

Nudt19

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acyl-CoA diphosphatase that mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters. At low substrate concentrations medium and long-chain fatty-acyl-CoA esters are the primary substrates.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 Publication

Kineticsi

  1. KM=0.6 mM for CoA1 Publication
  2. KM=0.58 mM for oxidized CoA1 Publication
  3. KM=0.08 mM for lauroyl-CoA1 Publication
  4. KM=0.01 mM for palmitoyl-CoA1 Publication
  5. KM=0.1 mM for choloyl-CoA1 Publication
  6. KM=0.1 mM for pristanoyl-CoA1 Publication
  1. Vmax=0.56 µmol/min/mg enzyme with CoA as substrate1 Publication
  2. Vmax=0.012 µmol/min/mg enzyme with oxidized CoA as substrate1 Publication
  3. Vmax=0.2 µmol/min/mg enzyme with lauroyl-CoA as substrate1 Publication
  4. Vmax=0.013 µmol/min/mg enzyme with palmitoyl-CoA as substrate1 Publication
  5. Vmax=0.17 µmol/min/mg enzyme with choloyl-CoA as substrate1 Publication
  6. Vmax=0.009 µmol/min/mg enzyme with pristanoyl-CoA as substrate1 Publication

pH dependencei

Optimum pH is 9.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi112 – 1121Magnesium or manganeseBy similarity
Metal bindingi116 – 1161Magnesium or manganeseBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-389887. Beta-oxidation of pristanoyl-CoA.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoside diphosphate-linked moiety X motif 19 (EC:3.6.1.-)
Short name:
Nudix motif 19
Alternative name(s):
Androgen-regulated protein RP2
Testosterone-regulated RP2 protein
Short name:
RP2p
Gene namesi
Name:Nudt19
Synonyms:D7Rp2e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:94203. Nudt19.

Subcellular locationi

  • Peroxisome 1 Publication

GO - Cellular componenti

  • mitochondrion Source: MGI
  • peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357Nucleoside diphosphate-linked moiety X motif 19PRO_0000057119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei300 – 3001N6-succinyllysineCombined sources

Proteomic databases

EPDiP11930.
MaxQBiP11930.
PaxDbiP11930.
PeptideAtlasiP11930.
PRIDEiP11930.

PTM databases

iPTMnetiP11930.
PhosphoSiteiP11930.

Expressioni

Inductioni

By testosterone.1 Publication

Gene expression databases

BgeeiP11930.
GenevisibleiP11930. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiP11930. 3 interactions.
MINTiMINT-4132945.
STRINGi10090.ENSMUSP00000047778.

Structurei

3D structure databases

ProteinModelPortaliP11930.
SMRiP11930. Positions 188-226.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 242233Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi97 – 11822Nudix boxAdd
BLAST
Motifi355 – 3573Microbody targeting signalSequence analysis

Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3904. Eukaryota.
ENOG4111FKM. LUCA.
GeneTreeiENSGT00420000029858.
HOGENOMiHOG000060163.
HOVERGENiHBG017737.
InParanoidiP11930.
KOiK13355.
OMAiCDYNALL.
OrthoDBiEOG7G7KQS.
TreeFamiTF313185.

Family and domain databases

Gene3Di3.90.79.10. 3 hits.
InterProiIPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 3 hits.
PROSITEiPS51462. NUDIX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSSSWRRA ATVMLAAGWT HSSPAGFRLL LLQRAQNQRF LPGAHVFPGG
60 70 80 90 100
VLDAADSSPD WVRLFAPRHT PPRFGLGPEP PRQPPFPGLS HGDADPAALP
110 120 130 140 150
DDVALRICAI REAFEEAGVL LLRPRDAAPA SQEPSQALSP PAGLAEWRSR
160 170 180 190 200
VRSDPRCFLQ LCAHLDCTPD IWALHDWGGW LTPYGRTIRR FDTTFFLCCL
210 220 230 240 250
RDIPRVEPDV AEVVGYQWLS PSEATECFLS KEIWLAPPQF YEMRRLENFA
260 270 280 290 300
SLSALYRFCS DRPSEVPEKW LPIILLTSDG TIHLLPGDEL YVKDSDFLEK
310 320 330 340 350
NMSTDKKTEE IVKEGKVLNR VVIHSPYVYE IYMTLPSENK HVYPRNYIVN

KRCTAHL
Length:357
Mass (Da):40,320
Last modified:July 27, 2011 - v2
Checksum:i6ED30EC4BF2955FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031I → T in CAA27722 (PubMed:3755524).Curated
Sequence conflicti353 – 3531C → Y in CAA27722 (PubMed:3755524).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04097 mRNA. Translation: CAA27722.1.
BC138674 mRNA. Translation: AAI38675.1.
BC138675 mRNA. Translation: AAI38676.1.
CCDSiCCDS21152.1.
PIRiA23641.
RefSeqiNP_149071.2. NM_033080.2.
UniGeneiMm.410206.
Mm.418631.
Mm.474965.

Genome annotation databases

EnsembliENSMUST00000040962; ENSMUSP00000047778; ENSMUSG00000034875.
GeneIDi110959.
KEGGimmu:110959.
UCSCiuc009gka.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04097 mRNA. Translation: CAA27722.1.
BC138674 mRNA. Translation: AAI38675.1.
BC138675 mRNA. Translation: AAI38676.1.
CCDSiCCDS21152.1.
PIRiA23641.
RefSeqiNP_149071.2. NM_033080.2.
UniGeneiMm.410206.
Mm.418631.
Mm.474965.

3D structure databases

ProteinModelPortaliP11930.
SMRiP11930. Positions 188-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11930. 3 interactions.
MINTiMINT-4132945.
STRINGi10090.ENSMUSP00000047778.

PTM databases

iPTMnetiP11930.
PhosphoSiteiP11930.

Proteomic databases

EPDiP11930.
MaxQBiP11930.
PaxDbiP11930.
PeptideAtlasiP11930.
PRIDEiP11930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040962; ENSMUSP00000047778; ENSMUSG00000034875.
GeneIDi110959.
KEGGimmu:110959.
UCSCiuc009gka.1. mouse.

Organism-specific databases

CTDi390916.
MGIiMGI:94203. Nudt19.

Phylogenomic databases

eggNOGiKOG3904. Eukaryota.
ENOG4111FKM. LUCA.
GeneTreeiENSGT00420000029858.
HOGENOMiHOG000060163.
HOVERGENiHBG017737.
InParanoidiP11930.
KOiK13355.
OMAiCDYNALL.
OrthoDBiEOG7G7KQS.
TreeFamiTF313185.

Enzyme and pathway databases

ReactomeiR-MMU-389887. Beta-oxidation of pristanoyl-CoA.

Miscellaneous databases

ChiTaRSiNudt19. mouse.
PROiP11930.
SOURCEiSearch...

Gene expression databases

BgeeiP11930.
GenevisibleiP11930. MM.

Family and domain databases

Gene3Di3.90.79.10. 3 hits.
InterProiIPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 3 hits.
PROSITEiPS51462. NUDIX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence of the testosterone-regulated mouse kidney RP2 protein deduced from its complementary DNA sequence."
    King D., Sun Y.H., Lingrel J.B.
    Nucleic Acids Res. 14:5159-5170(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: DBA/LIHA.
    Tissue: Kidney.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity."
    Ofman R., Speijer D., Leen R., Wanders R.J.A.
    Biochem. J. 393:537-543(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBCELLULAR LOCATION.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNUD19_MOUSE
AccessioniPrimary (citable) accession number: P11930
Secondary accession number(s): B2RS21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.