Reviewed, UniProtKB/Swiss-Prot Q29RJ1 (AP4A_BOVIN)

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=Diadenosine tetraphosphatase
      Short name=Ap4A hydrolase
      Short name=Ap4Aase
    Nucleoside diphosphate-linked moiety X motif 2
      Short name=Nudix motif 2

Gene names

Name:

NUDT2

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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 transcript level.

General annotation (Comments)

Function	Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.
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
Gene Ontology (GO)
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity Inferred from electronic annotation. Source: EC
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_0000260767
Regions
	Domain	1 – 139	139	Nudix hydrolase
	Motif	43 – 64	22	Nudix box
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q29RJ1-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1BC4523DF285D130	FASTA	147	16,775
	10 20 30 40 50 60 MALRACGLII FRRRLIPKVD NTAIEFLLLQ ASDGIHHWTP PKGHVEPGES DLETALRETQ 70 80 90 100 110 120 EEAGIEAGQL TIIEGFRREL SYVARAKPKI VIYWLAEVKD CDVEVRLSRE HQAYRWLELE 130 140 DACQLAQFEE MKAALQEGHQ FLCSTAT

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Hypothalamus.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC114149 mRNA. Translation: AAI14150.1.
IPI	IPI00742579.
RefSeq	NP_001070570.1.
UniGene	Bt.2818
3D structure databases
SMR	Q29RJ1. Positions 1-144.
ModBase	Search...
Protein-protein interaction databases
STRING	Q29RJ1.
Genome annotation databases
Ensembl	ENSBTAT00000045076; ENSBTAP00000042493; ENSBTAG00000031793; Bos taurus. [Genome view]
GeneID	768044.
KEGG	bta:768044.
Organism-specific databases
CTD	768044.
Phylogenomic databases
eggNOG	maNOG19537.
HOVERGEN	Q29RJ1.
InParanoid	Q29RJ1.
OMA	HQFLCST.
OrthoDB	EOG9DZ4DR.
Enzyme and pathway databases
BRENDA	3.6.1.17. 251.
Family and domain databases
InterPro	IPR020476. Nudix_hydrolase. 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.
Pfam	PF00293. NUDIX. 1 hit. [Graphical view]
PRINTS	PR00502. NUDIXFAMILY. PR01405. TETRPHPHTASE.
PROSITE	PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AP4A_BOVIN

Accession

Primary (citable) accession number: Q29RJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 33 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)