Reviewed, UniProtKB/Swiss-Prot Q9M0Y6 (DPNPM_ARATH)

Names and origin

Protein names

Recommended name:
    Putative PAP-specific phosphatase, mitochondrial
    EC=3.1.3.7
Alternative name(s):
    3'(2'),5'-bisphosphate nucleotidase
    3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase
    DPNPase

Gene names

Ordered Locus Names:	At4g05090
ORF Names:	C17L7.10, T32N4.1

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	397 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	Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP By similarity.
Catalytic activity	Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Cofactor	Magnesium By similarity.
Subcellular location	Mitochondrion Potential.
Sequence similarities	Belongs to the inositol monophosphatase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	chloroplast Inferred from direct assay. Source: TAIR mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3'(2'),5'-bisphosphate nucleotidase activity Inferred from electronic annotation. Source: EC inositol or phosphatidylinositol phosphatase activity Inferred from electronic annotation. Source: InterPro 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
	Transit peptide	1 – 16	16	Mitochondrion Potential
	Chain	17 – 397	381	Putative PAP-specific phosphatase, mitochondrial		PRO_0000015638
Sites
	Metal binding	114	1	Magnesium 1 By similarity
	Metal binding	174	1	Magnesium 1 By similarity
	Metal binding	174	1	Magnesium 2 By similarity
	Metal binding	176	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	177	1	Magnesium 2 By similarity
	Metal binding	334	1	Magnesium 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9M0Y6-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 77DB186E76DB0814	FASTA	397	43,531
	10 20 30 40 50 60 MYILDTGARF SAVRFSPVFN PPPTSLRRRY FIVRANLPFP KHQAKYHKEL EVAIDAVDRA 70 80 90 100 110 120 CRLCVDVKRS LFSSKEKIVE KNDQTPVTIA DFGVQALVSL ELSKLFPSIP LVAEEDSHFV 130 140 150 160 170 180 RANNLVSSVV SEVKSKASIG DNHLSDADVL EAIDRGGKDA YTFCNKPATY WVLDPIDGTR 190 200 210 220 230 240 GFLKGDEALY VVGLALVVDN EIVLGVMGCP NWPGDSSDGS TGTLMLSHIG CGTWTKKLQN 250 260 270 280 290 300 VSGNVAGDWI RCFVDACVLM NKARFCIQES QTWESLPLSG FFDASTVSED LKHKEILLLP 310 320 330 340 350 360 TCCGSLCKYL MVASGRASVF LLRAKTQRTI KSWDHAVGII CVHEAGGKVT DWEGDEINLE 370 380 390 EDQSERRLIF PAGGVVVSNG SLHNQILEMI SSASPTL

References

[1]

"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.

[2]

"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	AC012392 Genomic DNA. No translation available. AL161502 Genomic DNA. Translation: CAB81051.1. AF162444 Genomic DNA. Translation: AAD48973.1. Different initiation. AY085591 mRNA. Translation: AAM62812.1.
IPI	IPI00535547.
PIR	A85064.
RefSeq	NP_192418.1.
UniGene	At.33920
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9M0Y6.
Genome annotation databases
GeneID	825853.
GenomeReviews	Gene locus AT4G05090 in contig CT486007_GR.
KEGG	ath:AT4G05090.
NMPDR	fig|3702.1.peg.18325.
Organism-specific databases
TAIR	At4g05090.
Phylogenomic databases
OMA	Q9M0Y6. KYLMVAS.
Enzyme and pathway databases
BRENDA	3.1.3.7. 302.
Gene expression databases
ArrayExpress	Q9M0Y6.
GermOnline	AT4G05090. Arabidopsis thaliana.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPNPM_ARATH

Accession

Primary (citable) accession number: Q9M0Y6
Secondary accession number(s): Q9S9S9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2003
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)