Reviewed, UniProtKB/Swiss-Prot Q9Z0S1 (BPNT1_MOUSE)

Names and origin

Protein names

Recommended name:
    3'(2'),5'-bisphosphate nucleotidase 1
    EC=3.1.3.7
Alternative name(s):
    Bisphosphate 3'-nucleotidase 1
    PAP-inositol-1,4-phosphatase
      Short name=PIP

Gene names

Name:

Bpnt1

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

Protein attributes

Sequence length	308 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	Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins1P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6.
Catalytic activity	Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Cofactor	Magnesium.
Enzyme regulation	Uncompetitive inhibition by micromolar concentrations of lithium. Competitive inhibition by inositol 1,4-bisphosphate.
Sequence similarities	Belongs to the inositol monophosphatase family.

Ontologies

Keywords
Ligand	Lithium Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Acetylation
Gene Ontology (GO)
Molecular function	3'(2'),5'-bisphosphate nucleotidase activity Ref.1 Inferred from direct assay. Source: MGI inositol or phosphatidylinositol phosphatase activity Inferred from electronic annotation. Source: InterPro lithium ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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 – 308	307	3'(2'),5'-bisphosphate nucleotidase 1		PRO_0000142528
Regions
	Region	195 – 198	4	Substrate binding By similarity
Sites
	Metal binding	74	1	Magnesium 1 By similarity
	Metal binding	117	1	Magnesium 1 By similarity
	Metal binding	117	1	Magnesium 2 By similarity
	Metal binding	119	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	120	1	Magnesium 2 By similarity
	Metal binding	247	1	Magnesium 2 By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
Experimental info
	Sequence conflict	164	1	A → V in AAH11036. Ref.3
	Sequence conflict	190	1	H → R in AAH11036. Ref.3
	Sequence conflict	276	1	V → A in AAD17330. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9Z0S1-1 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: D941FEA4C2E59E9D	FASTA	308	33,196
	10 20 30 40 50 60 MASSHTVLMR LVASAYSIAQ KAGTIVRCVI AEGDLGIVQK TSATDLQTKA DRLVQMSICS 70 80 90 100 110 120 SLARKFPKLT IIGEEDLPPG EVDQELIEDG QWEEILKQPC PSQYSAIKEE DLVVWVDPLD 130 140 150 160 170 180 GTKEYTEGLL DNVTVLIGIA YEGKAIAGII NQPYYNYQAG PDAALGRTIW GVLGLGAFGF 190 200 210 220 230 240 QLKEAPAGKH IITTTRSHSN QLVTDCISAM NPDTVLRVGG AGNKIIQLIE GKASAYVFAS 250 260 270 280 290 300 PGCKKWDTCA PEVILHAVGG KLTDIHGNAL QYNKEVKHMN SAGVLAALRN YEYYASHVPE SVKNALIP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate." Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D. J. Biol. Chem. 274:13619-13628(1999) [PubMed: 10224133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]	"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: Bone marrow and Stomach.
[3]	"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]. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF125043 mRNA. Translation: AAD17330.1. AK008714 mRNA. Translation: BAB25850.1. AK151931 mRNA. Translation: BAE30807.1. AK152009 mRNA. Translation: BAE30872.1. BC011036 mRNA. Translation: AAH11036.1.
IPI	IPI00318545.
RefSeq	NP_035924.2.
UniGene	Mm.227549
3D structure databases
HSSP	HSSP built from PDB template 1INP based on UniProtKB P21327.
SMR	Q9Z0S1. Positions 5-308.
ModBase	Search...
PTM databases
PhosphoSite	Q9Z0S1.
2-D gel databases
REPRODUCTION-2DPAGE	Q9Z0S1.
Proteomic databases
PRIDE	Q9Z0S1.
Genome annotation databases
Ensembl	ENSMUSG00000026617. Mus musculus. [Contig view]
GeneID	23827.
KEGG	mmu:23827.
Organism-specific databases
MGI	MGI:1338800. Bpnt1.
Phylogenomic databases
HOGENOM	Q9Z0S1.
HOVERGEN	Q9Z0S1.
OMA	Q9Z0S1. GFQLKEA.
Enzyme and pathway databases
BRENDA	3.1.3.7. 244.
Gene expression databases
ArrayExpress	Q9Z0S1.
Bgee	Q9Z0S1.
CleanEx	MM_BPNT1.
GermOnline	ENSMUSG00000026617. Mus musculus.
Family and domain databases
InterPro	IPR000760. Inositol_P. [Graphical view]
PANTHER	PTHR20854. Inositol_P. 1 hit.
Pfam	PF00459. Inositol_P. 1 hit. [Graphical view]
PRINTS	PR00378. INOSPHPHTASE.
PROSITE	PS00629. IMP_1. 1 hit. PS00630. IMP_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	303481.
SOURCE	Search...

Entry information

Entry name

BPNT1_MOUSE

Accession

Primary (citable) accession number: Q9Z0S1
Secondary accession number(s): Q3U8Z5, Q91XB9, Q9D7Y0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)