Reviewed, UniProtKB/Swiss-Prot Q8GY63 (DPNP3_ARATH)

Names and origin

Protein names

Recommended name:
    Probable SAL3 phosphatase
Alternative name(s):
    3'(2'),5'-bisphosphate nucleotidase 3
    EC=3.1.3.7
    3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase 3
    DPNPase 3
    Inositol-1,4-bisphosphate 1-phosphatase 3
    EC=3.1.3.57
    Inositol polyphosphate 1-phosphatase 3
      Short name=IPPase 3

Gene names

Name:	SAL3
Ordered Locus Names:	At5g63990
ORF Names:	MBM17.9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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 By similarity. Is also able to hydrolyze inositol 1,4-bisphosphate By similarity.
Catalytic activity	Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate. 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate.
Cofactor	Magnesium By similarity.
Pathway	Signal transduction; phosphatidylinositol signaling pathway.
Sequence similarities	Belongs to the inositol monophosphatase family.
Sequence caution	The sequence BAA96902.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	sulfur metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	3'(2'),5'-bisphosphate nucleotidase activity Inferred from electronic annotation. Source: EC inositol-1,4-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q8GY63-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 357	357	Probable SAL3 phosphatase		PRO_0000142532
Sites
	Metal binding	71	1	Magnesium 1 By similarity
	Metal binding	135	1	Magnesium 1 By similarity
	Metal binding	135	1	Magnesium 2 By similarity
	Metal binding	137	1	Magnesium 1; via carbonyl oxygen By similarity
Experimental info
	Sequence conflict	212	1	A → V in AAM67202. Ref.4
	Sequence conflict	220	1	D → Y in AAM67202. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: B2570242F2B5EFA6	FASTA	357	38,385
	10 20 30 40 50 60 MSYDEMLSAA KKAVSLAARL SNEVRKSLLV TDVWNKSDDS PVTVADYGSQ AVVSLVLERE 70 80 90 100 110 120 LQNEPVSLVA EEDSGELRKI AAETVLARIT ELVKDTLASD ESYAIASPLT SDDVLNAIDR 130 140 150 160 170 180 GKSEGGPKGR HWILDPIGGT RGFIRGEQYA IGLALLVEGK VVLGVMACPK LPLASTAGNA 190 200 210 220 230 240 LKSLPEKVGC LFYGSVGNGT YVQSLSVDSL PAKVEVSSID DPAKASFFES YHTPVPIHNT 250 260 270 280 290 300 IATKLGIKES PIKINSQTKY AALSRGDGEV YLRFTRKARP ESIWNHAAGS IIVSEAGGKV 310 320 330 340 350 TDAAGNPLDF SKGKYLDYKR GIVVTTQKLL PRLLTAVRES IKEEEEEEEK AASLKLH

References

[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S. DNA Res. 7:31-63(2000) [PubMed: 10718197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB019227 Genomic DNA. Translation: BAA96902.1. Sequence problems. AK117842 mRNA. Translation: BAC42483.1. BT006247 mRNA. Translation: AAP12896.1. AY088896 mRNA. Translation: AAM67202.1.
IPI	IPI00544855.
RefSeq	NP_568983.1.
UniGene	At.28970
3D structure databases
HSSP	HSSP built from PDB template 1KA1 based on UniProtKB P32179.
ModBase	Search...
Proteomic databases
PRIDE	Q8GY63.
Genome annotation databases
GeneID	836520.
GenomeReviews	Gene locus AT5G63990 in contig BA000015_GR.
KEGG	ath:AT5G63990.
NMPDR	fig|3702.1.peg.28454.
Organism-specific databases
TAIR	At5g63990.
Enzyme and pathway databases
BRENDA	3.1.3.57. 302. 3.1.3.7. 302.
Gene expression databases
ArrayExpress	Q8GY63.
Family and domain databases
InterPro	IPR006239. Bisphos_HAL2. IPR000760. Inositol_P. [Graphical view]
PANTHER	PTHR20854. Inositol_P. 1 hit.
Pfam	PF00459. Inositol_P. 1 hit. [Graphical view]
PRINTS	PR00378. INOSPHPHTASE.
TIGRFAMs	TIGR01330. bisphos_HAL2. 1 hit.
PROSITE	PS00629. IMP_1. False negative. PS00630. IMP_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPNP3_ARATH

Accession

Primary (citable) accession number: Q8GY63
Secondary accession number(s): Q8L8N7, Q9LVN5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2003
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)