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Database: UniProt
Entry: G7PBW1_MACFA
LinkDB: G7PBW1_MACFA
Original site: G7PBW1_MACFA 
ID   G7PBW1_MACFA            Unreviewed;       278 AA.
AC   G7PBW1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase {ECO:0000256|ARBA:ARBA00039400};
DE            EC=3.1.3.7 {ECO:0000256|ARBA:ARBA00012633};
DE   AltName: Full=3'(2'), 5'-bisphosphate nucleotidase 2 {ECO:0000256|ARBA:ARBA00043030};
DE   AltName: Full=Inositol monophosphatase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042166};
DE   AltName: Full=Myo-inositol monophosphatase A3 {ECO:0000256|ARBA:ARBA00042119};
DE   AltName: Full=Phosphoadenosine phosphate 3'-nucleotidase {ECO:0000256|ARBA:ARBA00042064};
DE   Flags: Fragment;
GN   ORFNames=EGM_17337 {ECO:0000313|EMBL:EHH64182.1};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1] {ECO:0000313|EMBL:EHH64182.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CE-4 {ECO:0000313|EMBL:EHH64182.1};
RX   PubMed=22002653; DOI=10.1038/nbt.1992;
RA   Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA   Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA   Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA   Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA   Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA   Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT   "Genome sequencing and comparison of two nonhuman primate animal models,
RT   the cynomolgus and Chinese rhesus macaques.";
RL   Nat. Biotechnol. 29:1019-1023(2011).
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:0000256|ARBA:ARBA00001625};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Sulfur metabolism. {ECO:0000256|ARBA:ARBA00004678}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000256|ARBA:ARBA00037848}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00037848}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759}.
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DR   EMBL; CM001283; EHH64182.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7PBW1; -.
DR   eggNOG; KOG3853; Eukaryota.
DR   Proteomes; UP000009130; Chromosome 8.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01640; IPPase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   PANTHER; PTHR43028; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE 1; 1.
DR   PANTHER; PTHR43028:SF6; GOLGI-RESIDENT ADENOSINE 3',5'-BISPHOSPHATE 3'-PHOSPHATASE; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHH64182.1"
FT   NON_TER         278
FT                   /evidence="ECO:0000313|EMBL:EHH64182.1"
SQ   SEQUENCE   278 AA;  30733 MW;  78454F85542916C2 CRC64;
     RRVRESNVLH EKSKGKTREG AEDKMTSGDV LSNRKMFYLL KTAFPSVQIN TEEHVDAADQ
     EVILWDHKIP EDILKEVTTP KEVPAESVTV WIDPLDATQE YTEDLRKYVT TMVCVAVNGK
     PVLGVIHKPF SEYTAWAMVD GGSNVKARSS YNEKTPRIVV SRSHSGMVRQ VALQTFGNQT
     TIIPAGGAGY KVLALLDVPD KSQEKADLYI HVTYIKKWDI CAGNAILKAL GGHMTTLSGE
     EISYTGSDGI EGGLLASIRM NHQALVRKLP DLEKTGHK
//
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