IMPA3_RAT
ID IMPA3_RAT Reviewed; 356 AA.
AC D4AD37;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase {ECO:0000250|UniProtKB:Q80V26};
DE Short=Golgi-resident PAP phosphatase {ECO:0000250|UniProtKB:Q80V26};
DE Short=gPAPP {ECO:0000250|UniProtKB:Q80V26};
DE EC=3.1.3.7 {ECO:0000250|UniProtKB:Q80V26};
DE AltName: Full=3'(2'), 5'-bisphosphate nucleotidase 2;
DE AltName: Full=Inositol monophosphatase domain-containing protein 1 {ECO:0000250|UniProtKB:Q80V26};
DE AltName: Full=Myo-inositol monophosphatase A3 {ECO:0000250|UniProtKB:Q9NX62};
DE AltName: Full=Phosphoadenosine phosphate 3'-nucleotidase {ECO:0000250|UniProtKB:Q80V26};
GN Name=Bpnt2; Synonyms=Impa3, Impad1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exhibits 3'-nucleotidase activity toward adenosine 3',5'-
CC bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into
CC adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in
CC the formation of skeletal elements derived through endochondral
CC ossification, possibly by clearing adenosine 3',5'-bisphosphate
CC produced by Golgi sulfotransferases during glycosaminoglycan sulfation.
CC Has no activity toward 3'-phosphoadenosine 5'-phosphosulfate (PAPS) or
CC inositol phosphate (IP) substrates including I(1)P, I(1,4)P2,
CC I(1,3,4)P3, I(1,4,5)P3 and I(1,3,4,5)P4.
CC {ECO:0000250|UniProtKB:Q80V26}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC Evidence={ECO:0000250|UniProtKB:Q80V26};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Strongly inhibited by lithium.
CC {ECO:0000250|UniProtKB:Q80V26}.
CC -!- PATHWAY: Sulfur metabolism. {ECO:0000250|UniProtKB:Q80V26}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q80V26,
CC ECO:0000250|UniProtKB:Q9NX62}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NX62}.
CC Note=The catalytic core is predicted to reside within the Golgi lumen.
CC {ECO:0000250|UniProtKB:Q9NX62}.
CC -!- PTM: Contains N-linked glycan resistant to endoglycosydase H.
CC {ECO:0000250|UniProtKB:Q9NX62}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; CH473984; EDM11627.1; -; Genomic_DNA.
DR RefSeq; NP_001008772.2; NM_001008772.2.
DR RefSeq; XP_008761786.1; XM_008763564.2.
DR RefSeq; XP_008774114.1; XM_008775892.2.
DR AlphaFoldDB; D4AD37; -.
DR SMR; D4AD37; -.
DR GlyGen; D4AD37; 1 site.
DR iPTMnet; D4AD37; -.
DR PhosphoSitePlus; D4AD37; -.
DR jPOST; D4AD37; -.
DR PaxDb; D4AD37; -.
DR PeptideAtlas; D4AD37; -.
DR PRIDE; D4AD37; -.
DR Ensembl; ENSRNOT00000072803; ENSRNOP00000067120; ENSRNOG00000046647.
DR GeneID; 312952; -.
DR KEGG; rno:312952; -.
DR UCSC; RGD:1306455; rat.
DR CTD; 54928; -.
DR RGD; 1306455; Impad1.
DR eggNOG; KOG3853; Eukaryota.
DR GeneTree; ENSGT00940000160216; -.
DR HOGENOM; CLU_034742_0_0_1; -.
DR InParanoid; D4AD37; -.
DR OrthoDB; 1096950at2759; -.
DR PhylomeDB; D4AD37; -.
DR TreeFam; TF314300; -.
DR Reactome; R-RNO-156584; Cytosolic sulfonation of small molecules.
DR PRO; PR:D4AD37; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000027079; Expressed in testis and 4 other tissues.
DR ExpressionAtlas; D4AD37; baseline and differential.
DR Genevisible; D4AD37; RN.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0097657; F:3',5'-nucleotide bisphosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0008254; F:3'-nucleotidase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002063; P:chondrocyte development; ISO:RGD.
DR GO; GO:0030204; P:chondroitin sulfate metabolic process; ISO:RGD.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0001958; P:endochondral ossification; ISO:RGD.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Acetylation; Glycoprotein; Golgi apparatus; Hydrolase; Magnesium; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..356
FT /note="Golgi-resident adenosine 3',5'-bisphosphate 3'-
FT phosphatase"
FT /id="PRO_0000413415"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..356
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 82..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX62"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 38569 MW; 847D257B4C40DBE9 CRC64;
MAPMGIRLSP LGVAVFFLLG LGVLYHLYSG FLAGRFSLFG LGGEPAGGAA EVAVDGGTVD
LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA EDKMTSGDVL SNRKMFYLLK
TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY
TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDS GSNVKARSSY NEKTPKIIVS
RSHAGMVKQV ALQTFGNQTL IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC
AGNAILKALG GHMTTLSGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGH
