IMPA3_CALJA
ID IMPA3_CALJA Reviewed; 358 AA.
AC F6Y5S8;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
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 Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) 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; ACFV01107430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACFV01107431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACFV01107432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACFV01107433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002758970.1; XM_002758924.4.
DR AlphaFoldDB; F6Y5S8; -.
DR SMR; F6Y5S8; -.
DR STRING; 9483.ENSCJAP00000030514; -.
DR Ensembl; ENSCJAT00000032244; ENSCJAP00000030514; ENSCJAG00000016573.
DR GeneID; 100395037; -.
DR KEGG; cjc:100395037; -.
DR CTD; 54928; -.
DR eggNOG; KOG3853; Eukaryota.
DR GeneTree; ENSGT00940000160216; -.
DR InParanoid; F6Y5S8; -.
DR OMA; GNSMSEY; -.
DR OrthoDB; 1096950at2759; -.
DR TreeFam; TF314300; -.
DR Proteomes; UP000008225; Chromosome 16.
DR Bgee; ENSCJAG00000016573; Expressed in heart and 6 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
DR GO; GO:0030204; P:chondroitin sulfate metabolic process; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
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; IEA:Ensembl.
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..358
FT /note="Golgi-resident adenosine 3',5'-bisphosphate 3'-
FT phosphatase"
FT /id="PRO_0000413413"
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..358
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 85..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
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 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N4"
FT BINDING 176
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 300
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 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 38547 MW; BF8A1FBBF453019C CRC64;
MAPMGIRLSP LGVAVFCLLG LGVLYHLYSG FLAGRFSLFG LGGEPAGGAA GPPAAADGGT
VDLREMLAVS VLAAVRGGDE VRRVRESNVL HEKSKGKTRE GADDKMTSGD VLSNRKMFYL
LKTAFPSVQI NTEEHVDAAD QEVILWDHKI PEDILKEVTA PKEVPAESVT VWIDPLDATQ
EYTEDLRKYV TTMVCVAVNG KPVLGVIHKP FSEYTAWAMV DGGSNVKARS SYNEKTPRIV
VSRSHSGMVK QVALQTFGNQ TTIIPAGGAG YKVLALLDVP DKSQEKADLY IHVTYIKKWD
ICAGNAILKA LGGHMTTLSG EEISYTGSDG IEGGLLASIR MNHQALVRKL PDLEKMGH
