P0C024 (NUDT7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisomal coenzyme A diphosphatase NUDT7
EC=3.6.1.-

Alternative name(s):
Nucleoside diphosphate-linked moiety X motif 7
Short name=Nudix motif 7

Gene names

Name:

NUDT7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	238 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Coenzyme A diphosphatase which mediates the cleavage of CoA, CoA esters and oxidized CoA with similar efficiencies, yielding 3',5'-ADP and the corresponding 4'-phosphopantetheine derivative as products. CoA into 3',5'-ADP and 4'-phosphopantetheine. Has no activity toward NDP-sugars, CDP-alcohols, (deoxy)nucleoside 5'-triphosphates, nucleoside 5'-di or monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or thymidine-5'-monophospho-p-nitrophenyl ester. May be required to eliminate oxidized CoA from peroxisomes, or regulate CoA and acyl-CoA levels in this organelle in response to metabolic demand. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA By similarity.
Cofactor	Manganese or magnesium By similarity.
Enzyme regulation	Inhibited by fluoride By similarity.
Subcellular location	Peroxisome By similarity.
Tissue specificity	Expressed in liver, kidney, pancreas, pituitary, small intestine, spleen, heart and placenta. Weakly expressed in brain. Ref.2
Sequence similarities	Belongs to the Nudix hydrolase family. PCD1 subfamily. Contains 1 nudix hydrolase domain.

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Polymorphism
Ligand	Magnesium Manganese Metal-binding RNA-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA catabolic process Inferred from sequence or structural similarity. Source: UniProtKB brown fat cell differentiation Inferred from electronic annotation. Source: Compara coenzyme A catabolic process Inferred from sequence or structural similarity. Source: UniProtKB nucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	peroxisome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	acetyl-CoA hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: InterPro snoRNA binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 238	238	Peroxisomal coenzyme A diphosphatase NUDT7		PRO_0000057140
Regions
	Domain	37 – 172	136	Nudix hydrolase
	Motif	77 – 98	22	Nudix box
	Motif	236 – 238	3	Microbody targeting signal By similarity
Sites
	Metal binding	92	1	Magnesium or manganese By similarity
	Metal binding	96	1	Magnesium or manganese By similarity
Natural variations
	Natural variant	100	1	R → H. Corresponds to variant rs308925 [ dbSNP | Ensembl ].		VAR_050415
	Natural variant	181	1	E → G. Corresponds to variant rs16946429 [ dbSNP | Ensembl ].		VAR_050416

Sequences

	Sequence		Length	Mass (Da)
	P0C024 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 6F5BE439D609DC88	FASTA	238	26,942
	10 20 30 40 50 60 MSRLGLPEEP VRNSLLDDAK ARLRKYDIGG KYSHLPYNKY SVLLPLVAKE GKLHLLFTVR 70 80 90 100 110 120 SEKLRRAPGE VCFPGGKRDP TDMDDAATAL REAQEEVGLR PHQVEVVCCL VPCLIDTDTL 130 140 150 160 170 180 ITPFVGLIDH NFQAQPNPAE VKDVFLVPLA YFLHPQVHDQ HYVTRLGHRF INHIFEYTNP 190 200 210 220 230 EDGVTYQIKG MTANLAVLVA FIILEKKPTF EVQFNLNDVL ASSEELFLKV HKKATSRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives." Gasmi L., McLennan A.G. Biochem. J. 357:33-38(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC092134 Genomic DNA. No translation available. AC092724 Genomic DNA. No translation available.
IPI	IPI00455303.
RefSeq	NP_001099133.1. NM_001105663.2.
UniGene	Hs.282665.
3D structure databases
ProteinModelPortal	P0C024.
SMR	P0C024. Positions 38-199.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000268533.
PTM databases
PhosphoSite	P0C024.
Polymorphism databases
DMDM	68565858.
Proteomic databases
PaxDb	P0C024.
PRIDE	P0C024.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000268533; ENSP00000268533; ENSG00000140876.
GeneID	283927.
KEGG	hsa:283927.
UCSC	uc010chd.3. human.
Organism-specific databases
CTD	283927.
GeneCards	GC16P077756.
H-InvDB	HIX0038925.
HGNC	HGNC:8054. NUDT7.
HPA	HPA042042.
MIM	609231. gene.
neXtProt	NX_P0C024.
PharmGKB	PA31840.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0494.
HOGENOM	HOG000250455.
HOVERGEN	HBG082067.
InParanoid	P0C024.
OMA	FEYTNPE.
OrthoDB	EOG4MW87B.
Gene expression databases
ArrayExpress	P0C024.
Bgee	P0C024.
CleanEx	HS_NUDT7.
Genevestigator	P0C024.
GermOnline	ENSG00000140876. Homo sapiens.
Family and domain databases
Gene3D	3.90.79.10. 1 hit.
InterPro	IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. IPR000059. NUDIX_hydrolase_NudL_CS. [Graphical view]
Pfam	PF00293. NUDIX. 1 hit. [Graphical view]
SUPFAM	SSF55811. NUDIX_hydrolase. 1 hit.
PROSITE	PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. False negative. PS01293. NUDIX_COA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	283927.
NextBio	94370.
SOURCE	Search...

Entry information

Entry name

NUDT7_HUMAN

Accession

Primary (citable) accession number: P0C024

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	July 5, 2005
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.