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UniProtKB/Swiss-Prot entry Q9NX62


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

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Entry information
Entry name IMPA3_HUMAN
Primary accession number Q9NX62
Secondary accession number Q6NVY7
Integrated into Swiss-Prot on May 29, 2007
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 54)
Name and origin of the protein
Protein name Inositol monophosphatase 3
Synonyms EC 3.1.3.25
Inositol-1(or 4)-monophosphatase 3
IMPase 3
IMP 3
Myo-inositol monophosphatase A3
Inositol monophosphatase domain-containing protein 1
Gene name
Name: IMPAD1
Synonyms: IMPA3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Parthasarathy L., Parthasarathy R.;
"Molecular cloning and expression of human myo-inositol monophosphatase A3 cDNA (IMPA3).";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
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
AK000428; BAA91158.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY032885; AAK52336.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017797; AAH17797.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067814; AAH67814.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_060283.3; -.
UniGene Hs.438689
3D structure databases
HSSP Q9Z1N4; 1JP4. [HSSP ENTRY / PDB]
ModBase Q9NX62.
PTM databases
PhosphoSite Q9NX62; -.
Organism-specific databases
HGNC HGNC:26019; IMPAD1.
GenAtlas IMPAD1.
HPA HPA009411; -.
PharmGKB PA142671657; -.
GeneCards Q9NX62.
Gene expression databases
ArrayExpress Q9NX62; -.
CleanEx HS_IMPAD1; -.
Ontologies
GO
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from HPA).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0008934; Molecular function: inositol-1(or 4)-monophosphatase activity (inferred from electronic annotation from EC).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro 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.
PROSITE PS00629; IMP_1; FALSE_NEG.
PS00630; IMP_2; 1.
ProtoNet Q9NX62.
Proteomic databases
PeptideAtlas Q9NX62; -.
Genome annotation databases
Ensembl ENSG00000104331; Homo sapiens. [Contig view]
GeneID 54928; -.
KEGG hsa:54928; -.
Phylogenomic databases
HOVERGEN Q9NX62; -.
Other
NextBio 58023; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Hydrolase; Magnesium; Membrane; Metal-binding; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   359  359     Inositol monophosphatase 3. PRO_0000289041
TRANSMEM   13    33  21     Potential. 
COMPBIAS   53    56  4     Poly-Ala. 
METAL   133   133        Magnesium 1 (By similarity). 
METAL   174   174        Magnesium 1 (By similarity). 
METAL   174   174        Magnesium 2 (By similarity). 
METAL   176   176        Magnesium 1; via carbonyl oxygen (By similarity). 
METAL   177   177        Magnesium 2 (By similarity). 
METAL   300   300        Magnesium 2 (By similarity). 
CONFLICT   51    51        G -> E (in Ref. 3; AAH67814). 
CONFLICT   123   123        T -> A (in Ref. 3; AAH67814). 
CONFLICT   156   156        K -> E (in Ref. 3; AAH67814). 
Sequence information
Length: 359 AA [This is the length of the unprocessed precursor] Molecular weight: 38681 Da [This is the MW of the unprocessed precursor] CRC64: 4818E989A9684847 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPMGIRLSP LGVAVFCLLG LGVLYHLYSG FLAGRFSLFG LGGEPGGGAA GPAAAADGGT 

        70         80         90        100        110        120 
VDLREMLAVS VLAAVRGGDE VRRVRESNVL HEKSKGKTRE GAEDKMTSGD VLSNRKMFYL 

       130        140        150        160        170        180 
LKTAFPSVQI NTEEHVDAAD QEVILWDHKI PEDILKEVTT PKEVPAESVT VWIDPLDATQ 

       190        200        210        220        230        240 
EYTEDLRKYV TTMVCVAVNG KPMLGVIHKP FSEYTAWAMV DGGSNVKARS SYNEKTPRIV 

       250        260        270        280        290        300 
VSRSHSGMVK QVALQTFGNQ TTIIPAGGAG YKVLALLDVP DKSQEKADLY IHVTYIKKWD 

       310        320        330        340        350 
ICAGNAILKA LGGHMTTLSG EEISYTGSDG IEGGLLASIR MNHQALVRKL PDLEKTGHK 

Q9NX62 in FASTA format

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