IMPA3_BOVIN
ID IMPA3_BOVIN Reviewed; 362 AA.
AC Q2KJ53;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-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; BC105514; AAI05515.1; -; mRNA.
DR RefSeq; NP_001039800.1; NM_001046335.1.
DR AlphaFoldDB; Q2KJ53; -.
DR SMR; Q2KJ53; -.
DR STRING; 9913.ENSBTAP00000020766; -.
DR PaxDb; Q2KJ53; -.
DR PRIDE; Q2KJ53; -.
DR GeneID; 532797; -.
DR KEGG; bta:532797; -.
DR CTD; 54928; -.
DR eggNOG; KOG3853; Eukaryota.
DR HOGENOM; CLU_034742_0_0_1; -.
DR InParanoid; Q2KJ53; -.
DR OrthoDB; 1096950at2759; -.
DR TreeFam; TF314300; -.
DR Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Glycoprotein; Golgi apparatus; Hydrolase; Magnesium; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..362
FT /note="Golgi-resident adenosine 3',5'-bisphosphate 3'-
FT phosphatase"
FT /id="PRO_0000289040"
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..362
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 88..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 303
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 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 362 AA; 38924 MW; 2F8EBBE45DB03520 CRC64;
MAPMGIRLSP LGVAVFCLLG LGVLYHLYSG FLAGRFSLFG LGGEPGGGAA GPAGPAASAD
GGTVDLREML AVSVLAAVRG GEEVRRVRES NVLHEKSKGK TREGADDKMT SGDVLSNRKM
FYLLKTAFPS VQINTEEHVD ASDQEVILWD RKIPEDILKE IATPQEVPAE SVTVWIDPLD
ATQEYTEDLR KYVTTMVCVA VNGKPVLGVI HKPFSEYTAW AMVDGGSNVK ARTSYNEKTP
RIVVSRSHSG MVKQVALQTF GNQTTIIPAG GAGYKVLALL DVPDKSQEKA DLYIHVTYIK
KWDICAGNAI LKALGGHMTT LSGEEISYTG SDGIEGGLLA SIRMNHQALV RKLPDLEKTG
HK
