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Database: UniProt
Entry: L5LJT8_MYODS
LinkDB: L5LJT8_MYODS
Original site: L5LJT8_MYODS 
ID   L5LJT8_MYODS            Unreviewed;       244 AA.
AC   L5LJT8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
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};
GN   ORFNames=MDA_GLEAN10024569 {ECO:0000313|EMBL:ELK26161.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26161.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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; KB111232; ELK26161.1; -; Genomic_DNA.
DR   RefSeq; XP_006769121.1; XM_006769058.2.
DR   GeneID; 102752696; -.
DR   KEGG; myd:102752696; -.
DR   CTD; 54928; -.
DR   eggNOG; KOG3853; Eukaryota.
DR   OrthoDB; 3665671at2759; -.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   244 AA;  26800 MW;  563F2CAEE7790927 CRC64;
     MQINTEEHVD ATDQEVILWD RKIPEDILKE IATPKEVPAE SVTVWIDPLD ATQEYTEDLR
     NYVTTMVCVA VYGKPVLGVI HKPFSEYTAW AMVDGGSNVK AXXXXXXXXX XXXXSSYNEK
     TPRIVVSRSH SGMVKQVALQ TFGNQTTIIP AGGAGYKVLA LLDVPDKNQE KADVYIHVTY
     IKKWDICAGN AILKALGGHM TTLSGEEISY TGSDGIDGGL LASIRMNHQA LIKKLPDLEK
     TGHK
//
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