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Reviewed, UniProtKB/Swiss-Prot Q9NX62 (IMPA3_HUMAN)

Last modified February 9, 2010. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Inositol monophosphatase 3
      Short name=IMPase 3
      Short name=IMP 3
    EC=3.1.3.25
Alternative name(s):
    Inositol-1(or 4)-monophosphatase 3
    Myo-inositol monophosphatase A3
    Inositol monophosphatase domain-containing protein 1
Gene names
Name: IMPAD1
Synonyms: IMPA3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Myo-inositol phosphate + H2O = myo-inositol + phosphate.

Cofactor

Magnesium By similarity.

Pathway

Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the inositol monophosphatase family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentGolgi apparatus

Inferred from direct assay. Source: MGI

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioninositol-1(or 4)-monophosphatase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Inositol monophosphatase 3
PRO_0000289041

Regions

Transmembrane13 – 3321 Potential
Region176 – 1794Substrate binding By similarity
Compositional bias53 – 564Poly-Ala

Sites

Metal binding1331Magnesium 1 By similarity
Metal binding1741Magnesium 1 By similarity
Metal binding1741Magnesium 2 By similarity
Metal binding1761Magnesium 1; via carbonyl oxygen By similarity
Metal binding1771Magnesium 2 By similarity
Metal binding3001Magnesium 2 By similarity
Binding site1331Substrate By similarity
Binding site3001Substrate By similarity

Experimental info

Sequence conflict511G → E in AAH67814. Ref.3
Sequence conflict1231T → A in AAH67814. Ref.3
Sequence conflict1561K → E in AAH67814. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9NX62-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4818E989A9684847

FASTA35938,681
        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 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of human myo-inositol monophosphatase A3 cDNA (IMPA3)."
Parthasarathy L., Parthasarathy R.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin and Testis.
[4]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000428 mRNA. Translation: BAA91158.1.
AY032885 mRNA. Translation: AAK52336.1.
BC017797 mRNA. Translation: AAH17797.1.
BC067814 mRNA. Translation: AAH67814.1.
IPIIPI00787853.
RefSeqNP_060283.3.

3D structure databases

HSSPHSSP built from PDB template 1JP4 based on UniProtKB Q9Z1N4.
SMRQ9NX62. Positions 63-353.
ModBaseSearch...

Proteomic databases

PeptideAtlasQ9NX62.
PRIDEQ9NX62.

Genome annotation databases

EnsemblENST00000262644; ENSP00000262644; ENSG00000104331; Homo sapiens. [Genome view]
GeneID54928.
KEGGhsa:54928.
UCSCuc003xte.2. human.

Organism-specific databases

CTD54928.
GeneCardsGC08M058039.
HGNCHGNC:26019. IMPAD1.
HPAHPA009411.
PharmGKBPA142671657.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG09579.
HOGENOMHBG717298.
HOVERGENQ9NX62.
InParanoidQ9NX62.
OMANVQINTE.
OrthoDBEOG9K9DZ4.
PhylomeDBQ9NX62.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000104331-MONOMER.
BRENDA3.1.3.25. 247.

Gene expression databases

ArrayExpressQ9NX62.
BgeeQ9NX62.
CleanExHS_IMPAD1.
GenevestigatorQ9NX62.

Family and domain databases

InterProIPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEPS00629. IMP_1. False negative.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio58023.

Entry information

Entry nameIMPA3_HUMAN
AccessionPrimary (citable) accession number: Q9NX62
Secondary accession number(s): Q6NVY7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents