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UniProtKB/Swiss-Prot entry P32179


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HAL2_YEAST
Primary accession number P32179
Secondary accession number Q6RFY5
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 77)
Name and origin of the protein
Protein name 3'(2'),5'-bisphosphate nucleotidase
Synonyms EC 3.1.3.7
3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase
DPNPase
Halotolerance protein HAL2
Gene name
Name: HAL2
Synonyms: MET22
OrderedLocusNames: YOL064C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8393782 [NCBI, ExPASy, EBI, Israel, Japan]
Glaeser H.-U., Thomas D., Gaxiola R., Montrichard F., Surdin-Kerjan Y., Serrano R.;
"Salt tolerance and methionine biosynthesis in Saccharomyces cerevisiae involve a putative phosphatase gene.";
EMBO J. 12:3105-3110(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Montrache;
Thanananta N., Apisitwanich S., Peyachoknagul S.;
"Cloning of HAL2 gene from Saccharomyces cerevisiae Montrache.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/(SICI)1097-0061(199705)13:6<583::AID-YEA111>3.0.CO;2-Y; PubMed=9178509 [NCBI, ExPASy, EBI, Israel, Japan]
Tzermia M., Katsoulou C., Alexandraki D.;
"Sequence analysis of a 33.2 kb segment from the left arm of yeast chromosome XV reveals eight known genes and ten new open reading frames including homologues of ABC transporters, inositol phosphatases and human expressed sequence tags.";
Yeast 13:583-589(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND AMP.
DOI=10.1006/jmbi.1999.3408; PubMed=10656801 [NCBI, ExPASy, EBI, Israel, Japan]
Albert A., Yenush L., Gil-Mascarell M.R., Rodriguez P.L., Patel S., Martinez-Ripoll M., Blundell T.L., Serrano R.;
"X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity.";
J. Mol. Biol. 295:927-938(2000).
Comments
  • FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. Involved in salt tolerance. Confers resistance to lithium.
  • CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
  • COFACTOR: Magnesium.
  • INDUCTION: By salt stress.
  • MISCELLANEOUS: Present with 7330 molecules/cell in log phase SD medium.
  • 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
X72847; CAA51361.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY500154; AAR89916.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74806; CAA99074.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S35318; S35318.
RefSeq NP_014577.1; -.
3D structure databases
PDB
1K9Y; X-ray; 1.90 A; A=1-357.[ExPASy / RCSB / EBI]
1K9Z; X-ray; 1.50 A; A=1-357.[ExPASy / RCSB / EBI]
1KA0; X-ray; 1.80 A; A=1-357.[ExPASy / RCSB / EBI]
1KA1; X-ray; 1.30 A; A=1-357.[ExPASy / RCSB / EBI]
1QGX; X-ray; 1.60 A; A=1-357.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1K9Y; -.
1K9Z; -.
1KA0; -.
1KA1; -.
1QGX; -.
ModBase P32179.
Protein-protein interaction databases
DIP DIP:4072N; -.
IntAct P32179; -.
Organism-specific databases
CYGD YOL064c; -.
SGD S000005425; MET22.
Yeast-GFP YOL064C.
Gene expression databases
GermOnline YOL064C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0008441; Molecular function: 3'(2'),5'-bisphosphate nucleotidase activity (inferred from electronic annotation from InterPro).
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:0042538; Biological process: hyperosmotic salinity response (traceable author statement from SGD).
GO:0009086; Biological process: methionine biosynthetic process (traceable author statement from SGD).
GO:0042493; Biological process: response to drug (inferred from mutant phenotype from SGD).
GO:0000103; Biological process: sulfate assimilation (traceable author statement from SGD).
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.
BLOCKS P32179.
ProtoNet P32179.
Proteomic databases
PeptideAtlas P32179; -.
Genome annotation databases
Ensembl YOL064C; Saccharomyces cerevisiae. [Contig view]
GeneID 854090; -.
GenomeReviews Y13140_GR; YOL064C.
KEGG sce:YOL064C; -.
NMPDR fig|4932.3.peg.5669; -.
Phylogenomic databases
HOGENOM P32179; -.
Other
DrugBank DB00131; Adenosine monophosphate.
LinkHub P32179; -.
NextBio 975743; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Hydrolase; Lithium; Magnesium; Metal-binding; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   357  357     3'(2'),5'-bisphosphate nucleotidase. PRO_0000142537
METAL   72    72        Magnesium 1. 
METAL   142   142        Magnesium 1. 
METAL   142   142        Magnesium 2. 
METAL   144   144        Magnesium 1; via carbonyl oxygen. 
METAL   145   145        Magnesium 2. 
METAL   294   294        Magnesium 2. 
VARIANT   40    40  1     N -> S (in strain: Montrache). 
VARIANT   61    61  1     K -> M (in strain: Montrache). 
VARIANT   63    63  1     N -> S (in strain: Montrache). 
VARIANT   308   308  1     I -> V (in strain: Montrache). 
HELIX   4    30  27      
TURN   31    34  4      
STRAND   35    38  4      
STRAND   44    46  3      
HELIX   47    63  17      
STRAND   69    72  4      
HELIX   80   100  21      
STRAND   111   113  3      
HELIX   118   126  9      
STRAND   134   145  12      
HELIX   147   151  5      
STRAND   157   164  8      
STRAND   167   175  9      
HELIX   180   183  4      
TURN   189   194  6      
STRAND   196   201  6      
STRAND   206   210  5      
TURN   211   213  3      
HELIX   228   230  3      
STRAND   232   235  4      
TURN   239   241  3      
HELIX   244   253  10      
STRAND   258   261  4      
HELIX   266   273  8      
STRAND   277   281  5      
HELIX   292   294  3      
HELIX   296   304  9      
STRAND   308   310  3      
STRAND   312   314  3      
STRAND   322   325  4      
STRAND   327   329  3      
STRAND   331   335  5      
HELIX   338   353  16      
Sequence information
Length: 357 AA [This is the length of the unprocessed precursor] Molecular weight: 39149 Da [This is the MW of the unprocessed precursor] CRC64: AB2E5F90B285702B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALERELLVA TQAVRKASLL TKRIQSEVIS HKDSTTITKN DNSPVTTGDY AAQTIIINAI 

        70         80         90        100        110        120 
KSNFPDDKVV GEESSSGLSD AFVSGILNEI KANDEVYNKN YKKDDFLFTN DQFPLKSLED 

       130        140        150        160        170        180 
VRQIIDFGNY EGGRKGRFWC LDPIDGTKGF LRGEQFAVCL ALIVDGVVQL GCIGCPNLVL 

       190        200        210        220        230        240 
SSYGAQDLKG HESFGYIFRA VRGLGAFYSP SSDAESWTKI HVRHLKDTKD MITLEGVEKG 

       250        260        270        280        290        300 
HSSHDEQTAI KNKLNISKSL HLDSQAKYCL LALGLADVYL RLPIKLSYQE KIWDHAAGNV 

       310        320        330        340        350 
IVHEAGGIHT DAMEDVPLDF GNGRTLATKG VIASSGPREL HDLVVSTSCD VIQSRNA 

P32179 in FASTA format

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