Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NX62 (IMPA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol monophosphatase 3

Short name=IMP 3
Short name=IMPase 3
EC=3.1.3.25
EC=3.1.3.7
Alternative name(s):
Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase
Short name=Golgi-resident PAP phosphatase
Short name=gPAPP
Inositol monophosphatase domain-containing protein 1
Inositol-1(or 4)-monophosphatase 3
Myo-inositol monophosphatase A3
Gene names
Name:IMPAD1
Synonyms:IMPA3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation By similarity.

Catalytic activity

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

Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.

Cofactor

Magnesium By similarity.

Enzyme regulation

Strongly inhibited by lithium By similarity.

Pathway

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

Subcellular location

Golgi apparatustrans-Golgi network membrane; Single-pass type II membrane protein Ref.4.

Post-translational modification

Contains N-linked glycan resistant to endoglycosydase H.

Involvement in disease

Chondrodysplasia with joint dislocations, GPAPP type (CDP-GPAPP) [MIM:614078]: A condition consisting of congenital joint dislocations, chondrodysplasia with short stature, micrognathia and cleft palate, and a distinctive face.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Belongs to the inositol monophosphatase family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DiseaseDisease mutation
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchondrocyte development

Inferred from electronic annotation. Source: Ensembl

chondroitin sulfate metabolic process

Inferred from electronic annotation. Source: Ensembl

embryonic digit morphogenesis

Inferred from electronic annotation. Source: Ensembl

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

inositol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

phosphatidylinositol phosphorylation

Inferred from electronic annotation. Source: InterPro

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.4. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function3'(2'),5'-bisphosphate nucleotidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3'-nucleotidase activity

Inferred from electronic annotation. Source: Ensembl

inositol monophosphate 1-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol monophosphate 3-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol monophosphate 4-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal 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

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3321Helical; Potential
Topological domain34 – 359326Lumenal 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

Amino acid modifications

Glycosylation2591N-linked (GlcNAc...) Probable

Natural variations

Natural variant1771D → N in CDP-GPAPP. Ref.7
VAR_065847
Natural variant1831T → P in CDP-GPAPP. Ref.7
VAR_065848

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 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin and Testis.
[4]"A role for a lithium-inhibited Golgi nucleotidase in skeletal development and sulfation."
Frederick J.P., Tafari A.T., Wu S.M., Megosh L.C., Chiou S.T., Irving R.P., York J.D.
Proc. Natl. Acad. Sci. U.S.A. 105:11605-11612(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Chondrodysplasia and abnormal joint development associated with mutations in IMPAD1, encoding the Golgi-resident nucleotide phosphatase, gPAPP."
Vissers L.E., Lausch E., Unger S., Campos-Xavier A.B., Gilissen C., Rossi A., Del Rosario M., Venselaar H., Knoll U., Nampoothiri S., Nair M., Spranger J., Brunner H.G., Bonafe L., Veltman J.A., Zabel B., Superti-Furga A.
Am. J. Hum. Genet. 88:608-615(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDP-GPAPP ASN-177 AND PRO-183.
+Additional computationally mapped references.

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.
CCDSCCDS6169.1.
RefSeqNP_060283.3. NM_017813.4.
UniGeneHs.438689.

3D structure databases

ProteinModelPortalQ9NX62.
SMRQ9NX62. Positions 63-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120268. 5 interactions.
MINTMINT-5003255.
STRING9606.ENSP00000262644.

PTM databases

PhosphoSiteQ9NX62.

Polymorphism databases

DMDM74734687.

Proteomic databases

MaxQBQ9NX62.
PaxDbQ9NX62.
PeptideAtlasQ9NX62.
PRIDEQ9NX62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262644; ENSP00000262644; ENSG00000104331.
GeneID54928.
KEGGhsa:54928.
UCSCuc003xte.4. human.

Organism-specific databases

CTD54928.
GeneCardsGC08M057870.
H-InvDBHIX0007522.
HGNCHGNC:26019. IMPAD1.
HPAHPA009411.
MIM614010. gene.
614078. phenotype.
neXtProtNX_Q9NX62.
Orphanet1388. Catel-Manzke syndrome.
280586. Chondrodysplasia with joint dislocations, gPAPP type.
PharmGKBPA142671657.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1218.
HOGENOMHOG000290671.
HOVERGENHBG062091.
InParanoidQ9NX62.
KOK15759.
OMANVQINTE.
OrthoDBEOG7CG71H.
PhylomeDBQ9NX62.
TreeFamTF314300.

Enzyme and pathway databases

BioCycMetaCyc:HS02567-MONOMER.
UniPathwayUPA00823; UER00788.

Gene expression databases

ArrayExpressQ9NX62.
BgeeQ9NX62.
CleanExHS_IMPAD1.
GenevestigatorQ9NX62.

Family and domain databases

InterProIPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERPTHR20854. PTHR20854. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEPS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi54928.
NextBio58023.
PROQ9NX62.
SOURCESearch...

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: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

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