Q9NX62 (IMPA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence 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 apparatus › trans-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.6
Sequence similarities	Belongs to the inositol monophosphatase family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Disease	Disease mutation
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chondrocyte development Inferred from electronic annotation. Source: Compara chondroitin sulfate metabolic process Inferred from electronic annotation. Source: Compara embryonic digit morphogenesis Inferred from electronic annotation. Source: Compara endochondral ossification Inferred from electronic annotation. Source: Compara 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: Compara
Cellular_component	Golgi apparatus Inferred from direct assay Ref.4. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	3'(2'),5'-bisphosphate nucleotidase activity Inferred from electronic annotation. Source: EC 3'-nucleotidase activity Inferred from electronic annotation. Source: Compara inositol monophosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC inositol monophosphate 3-phosphatase activity Inferred from electronic annotation. Source: EC inositol monophosphate 4-phosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	Inositol monophosphatase 3		PRO_0000289041
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 33	21	Helical; Potential
	Topological domain	34 – 359	326	Lumenal Potential
	Region	176 – 179	4	Substrate binding By similarity
	Compositional bias	53 – 56	4	Poly-Ala
Sites
	Metal binding	133	1	Magnesium 1 By similarity
	Metal binding	174	1	Magnesium 1 By similarity
	Metal binding	174	1	Magnesium 2 By similarity
	Metal binding	176	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	177	1	Magnesium 2 By similarity
	Metal binding	300	1	Magnesium 2 By similarity
	Binding site	133	1	Substrate By similarity
	Binding site	300	1	Substrate By similarity
Amino acid modifications
	Glycosylation	259	1	N-linked (GlcNAc...) Probable
Natural variations
	Natural variant	177	1	D → N in CDP-GPAPP. Ref.6		VAR_065847
	Natural variant	183	1	T → P in CDP-GPAPP. Ref.6		VAR_065848
Experimental info
	Sequence conflict	51	1	G → E in AAH67814. Ref.3
	Sequence conflict	123	1	T → A in AAH67814. Ref.3
	Sequence conflict	156	1	K → E in AAH67814. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9NX62 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 4818E989A9684847	FASTA	359	38,681
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
IPI	IPI00787853.
RefSeq	NP_060283.3. NM_017813.4.
UniGene	Hs.438689.
3D structure databases
HSSP	HSSP built from PDB template 1JP4 based on UniProtKB Q9Z1N4.
ProteinModelPortal	Q9NX62.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000262644.
PTM databases
PhosphoSite	Q9NX62.
Polymorphism databases
DMDM	74734687.
Proteomic databases
PaxDb	Q9NX62.
PeptideAtlas	Q9NX62.
PRIDE	Q9NX62.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262644; ENSP00000262644; ENSG00000104331.
GeneID	54928.
KEGG	hsa:54928.
UCSC	uc003xte.4. human.
Organism-specific databases
CTD	54928.
GeneCards	GC08M057870.
H-InvDB	HIX0007522.
HGNC	HGNC:26019. IMPAD1.
HPA	HPA009411.
MIM	614010. gene. 614078. phenotype.
neXtProt	NX_Q9NX62.
Orphanet	280586. Chondrodysplasia with joint dislocations, gPAPP type.
PharmGKB	PA142671657.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1218.
HOGENOM	HOG000290671.
HOVERGEN	HBG062091.
InParanoid	Q9NX62.
KO	K15759.
OMA	NVQINTE.
OrthoDB	EOG434W6B.
PhylomeDB	Q9NX62.
Enzyme and pathway databases
BioCyc	MetaCyc:HS02567-MONOMER.
UniPathway	UPA00823; UER00788.
Gene expression databases
ArrayExpress	Q9NX62.
Bgee	Q9NX62.
CleanEx	HS_IMPAD1.
Genevestigator	Q9NX62.
Family and domain databases
InterPro	IPR000760. Inositol_monophosphatase. IPR020550. Inositol_monophosphatase_CS. [Graphical view]
PANTHER	PTHR20854. PTHR20854. 1 hit.
Pfam	PF00459. Inositol_P. 1 hit. [Graphical view]
PROSITE	PS00629. IMP_1. False negative. PS00630. IMP_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	54928.
NextBio	58023.
SOURCE	Search...

Entry information

Entry name

IMPA3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.