P56380 (AP4A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
EC=3.6.1.17

Alternative name(s):
Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
Short name=Ap4A hydrolase
Short name=Ap4Aase
Short name=Diadenosine tetraphosphatase
Nucleoside diphosphate-linked moiety X motif 2
Short name=Nudix motif 2

Gene names

Name:	Nudt2
Synonyms:	Apah1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis By similarity.
Catalytic activity	P1,P(4)-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP.
Cofactor	Divalent ions By similarity.
Sequence similarities	Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain.

Ontologies

Keywords
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 147	146	Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]		PRO_0000057103
Regions
	Domain	1 – 139	139	Nudix hydrolase
	Motif	43 – 64	22	Nudix box
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
Experimental info
	Sequence conflict	19	1	M → V in BAB31399. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P56380 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A634D19F1E8CCE34	FASTA	147	16,989
	10 20 30 40 50 60 MALRACGLII FRRHLIPKMD NSTIEFLLLQ ASDGIHHWTP PKGHVDPGEN DLETALRETR 70 80 90 100 110 120 EETGIEASQL TIIEGFRREL NYVARQKPKT VIYWLAEVKD YNVEIRLSQE HQAYRWLGLE 130 140 EACQLAQFKE MKATLQEGHQ FLCSTPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum and Tongue.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney.
[3]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 5-12; 43-57; 61-77; 90-99 AND 116-129, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK009933 mRNA. Translation: BAB26592.1. AK018771 mRNA. Translation: BAB31399.1. BC025153 mRNA. Translation: AAH25153.1.
IPI	IPI00135345.
RefSeq	NP_079815.2. NM_025539.2.
UniGene	Mm.28574.
3D structure databases
ProteinModelPortal	P56380.
SMR	P56380. Positions 1-147.
ModBase	Search...
Protein-protein interaction databases
STRING	P56380.
Proteomic databases
PRIDE	P56380.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030154; ENSMUSP00000030154; ENSMUSG00000028443.
GeneID	66401.
KEGG	mmu:66401.
Organism-specific databases
CTD	318.
MGI	MGI:1913651. Nudt2.
Phylogenomic databases
HOGENOM	HBG741910.
HOVERGEN	HBG002853.
InParanoid	P56380.
OMA	RRRLIPK.
OrthoDB	EOG4FTW20.
PhylomeDB	P56380.
Gene expression databases
ArrayExpress	P56380.
Bgee	P56380.
Genevestigator	P56380.
GermOnline	ENSMUSG00000028443. Mus musculus.
Family and domain databases
InterPro	IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. IPR003565. Tetra_PHTase. [Graphical view]
Gene3D	G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
KO	K01518.
Pfam	PF00293. NUDIX. 1 hit. [Graphical view]
PRINTS	PR01405. TETRPHPHTASE.
SUPFAM	SSF55811. NUDIX_hydrolase. 1 hit.
PROSITE	PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	321571.
SOURCE	Search...

Entry information

Entry name

AP4A_MOUSE

Accession

Primary (citable) accession number: P56380
Secondary accession number(s): Q9D2U6, Q9D6V2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program