[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Columbia; Cheong J.-J., Kwon H.-B., Goodman H.M.; "A cDNA clone encoding Arabidopsis HAL2-like (AHL) protein."; (er) Plant Gene Register PGR96-042.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Landsberg erecta; Cheong J.-J., Kwon H.-B., Goodman H.M.; "Arabidopsis Ahl encodes a PAP-specific phosphatase that is sensitive to toxic metal ions."; Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. STRAIN=cv. Columbia; PubMed=10205895 [NCBI, ExPASy, EBI, Israel, Japan] Gil-Mascarell R., Lopez-Coronado J.M., Belles J.M., Serrano R., Rodriguez P.L.; "The Arabidopsis HAL2-like gene family includes a novel sodium-sensitive phosphatase."; Plant J. 17:373-383(1999).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 5. XI."; Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Empirical analysis of transcriptional activity in the Arabidopsis genome."; Science 302:842-846(2003).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.; "Full-length cDNA from Arabidopsis thaliana."; Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]	3D-STRUCTURE MODELING. Lim Y., Jung J.; "Theoretical structure of Arabidopsis thaliana PAP-specific phosphatase (AHL)."; Submitted (AUG-2000) to the PDB data bank.

Comments

FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS (By similarity). Prevents both the toxicity of PAP on RNA processing enzymes as well as the product inhibition by PAP of sulfate conjugation.
CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H₂O = adenosine 5'-phosphate + phosphate.
COFACTOR: Magnesium (By similarity).
ENZYME REGULATION: Inhibited by Li(+) (IC₅₀=10 millimolar), Na(+) (IC₅₀=50 millimolar) and Ca(2+) (IC₅₀=0.06 millimolar).
TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and siliques.
MISCELLANEOUS: Substrate preference is 3'-phosphoadenosine 5'-phosphate (PAP) > adenosine 3'-phosphate 5'-phosphosulfate (PAPS). No activity observed against 3' or 5'-AMP, inositol mono and diphosphates and fructose-1,6-bisphosphate.
SIMILARITY: Belongs to the inositol monophosphatase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U55205; AAB52964.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF016644; AAB94051.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB026634; BAA97512.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY045848; AAK76522.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY091377; AAM14316.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086488; AAM63490.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_200250.1; -.

UniGene

At.9004

3D structure databases

PDB

1FLF; Model; -; A=1-373.	[ExPASy / RCSB / EBI]
1Q00; Model; -; A=1-373.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1FLF; -.
1Q00; -.

ModBase

Q38945.

Organism-specific databases

GeneFarm

2322; -.

TAIR

At5g54390; -.

Gene expression databases

ArrayExpress

Q38945; -.

GermOnline

AT5G54390; Arabidopsis thaliana.

Ontologies

GO:0008441;	Molecular function: 3'(2'),5'-bisphosphate nucleotidase activity (inferred from electronic annotation from InterPro).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004437;	Molecular function: inositol or phosphatidylinositol phosphatase activity (inferred from electronic annotation from InterPro).
GO:0031403;	Molecular function: lithium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006790;	Biological process: sulfur metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006239; Bisphos_HAL2.
IPR000760; Inositol_P.
Graphical view of domain structure.

PANTHER

PTHR20854; Inositol_P; 1.

Pfam

PF00459; Inositol_P; 1.
Pfam graphical view of domain structure.

PRINTS

PR00378; INOSPHPHTASE.

TIGRFAMs

TIGR01330; bisphos_HAL2; 1.

PROSITE

PS00629; IMP_1; 1.
PS00630; IMP_2; 1.

ProtoNet

Q38945.

Genome annotation databases

GeneID

835527; -.

GenomeReviews

BA000015_GR; AT5G54390.

KEGG

ath:AT5G54390; -.

NMPDR

fig|3702.1.peg.27347; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Complete proteome; Hydrolase; Lithium; Magnesium; Metal-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 373`	`373`	`PAP-specific phosphatase HAL2-like.`	`PRO_0000142534`
`METAL`	`77 77`		`Magnesium 1 (By similarity).`
`METAL`	`144 144`		`Magnesium 1 (By similarity).`
`METAL`	`144 144`		`Magnesium 2 (By similarity).`
`METAL`	`146 146`		`Magnesium 1; via carbonyl oxygen (By similarity).`
`METAL`	`147 147`		`Magnesium 2 (By similarity).`
`METAL`	`310 310`		`Magnesium 2 (By similarity).`
`CONFLICT`	`107 108`		`QN -> SK (in Ref. 2; AAB94051).`
`HELIX`	`7 32`	`26`
`STRAND`	`39 41`	`3`
`STRAND`	`47 49`	`3`
`HELIX`	`50 63`	`14`
`HELIX`	`64 66`	`3`
`STRAND`	`76 79`	`4`
`STRAND`	`82 86`	`5`
`STRAND`	`99 102`	`4`
`STRAND`	`110 113`	`4`
`STRAND`	`132 137`	`6`
`STRAND`	`141 146`	`6`
`TURN`	`147 149`	`3`
`HELIX`	`150 154`	`5`
`STRAND`	`161 166`	`6`
`STRAND`	`169 174`	`6`
`STRAND`	`179 181`	`3`
`STRAND`	`212 216`	`5`
`STRAND`	`218 220`	`3`
`STRAND`	`231 235`	`5`
`STRAND`	`242 244`	`3`
`STRAND`	`255 258`	`4`
`STRAND`	`264 266`	`3`
`STRAND`	`272 275`	`4`
`TURN`	`289 292`	`4`
`HELIX`	`311 320`	`10`
`STRAND`	`330 332`	`3`
`TURN`	`366 368`	`3`

Sequence information

Length: 373 AA [This is the length of the unprocessed precursor]

Molecular weight: 39374 Da [This is the MW of the unprocessed precursor]

CRC64: CC0B3F3487859EC8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVDSLETEI DTAVRVVHLA SSLCVKVQEK LHLPNGGHVK SKDDDSPVTV ADFGVQAIVS 

        70         80         90        100        110        120 
WVLAEVFGDQ NLSIVAEEDT ETLSEADSLG LLGAVSNAVN EALSEAQNYG LPKPVKPLGS 

       130        140        150        160        170        180 
SEILKAISRC NSVGGPKGRH WVLDPVDGTL GFVRGDQYAV ALALIENGKV LLGVLGCPNY 

       190        200        210        220        230        240 
PVKKECLSNG CNQAMKTKAV AGSVSKGCVM YAKRGSGQAW MQPLIVGGIP ESATLLKVSS 

       250        260        270        280        290        300 
VDDPVLATVC EPVERANSNH LFTAGLANSM GVRKQPMRVY SMVKYAAIAR GDAEVFMKFA 

       310        320        330        340        350        360 
QSSYKEKIWD HAAGVVIVEE AGGVVTDAGG RNLDFSKGVY LEGLDRGIIA CSGQVLHEKI 

       370 
IGAVYASWES SSL

Q38945 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools