ID H9FE39_MACMU Unreviewed; 89 AA.
AC H9FE39;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Alkaline phosphatase, tissue-nonspecific isozyme {ECO:0000256|ARBA:ARBA00040525};
DE EC=3.1.3.1 {ECO:0000256|ARBA:ARBA00012647};
DE EC=3.9.1.1 {ECO:0000256|ARBA:ARBA00039023};
DE AltName: Full=Alkaline phosphatase liver/bone/kidney isozyme {ECO:0000256|ARBA:ARBA00041665};
DE AltName: Full=Phosphoamidase {ECO:0000256|ARBA:ARBA00042603};
DE AltName: Full=Phosphocreatine phosphatase {ECO:0000256|ARBA:ARBA00042681};
DE Flags: Fragment;
GN Name=ALPL {ECO:0000313|EMBL:AFE72898.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE72898.1};
RN [1] {ECO:0000313|EMBL:AFE72898.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE72898.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036139};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC Evidence={ECO:0000256|ARBA:ARBA00036139};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H2O = adenosine + phosphate; Xref=Rhea:RHEA:29375,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00036923};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29376;
CC Evidence={ECO:0000256|ARBA:ARBA00036923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00034440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00034440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-phosphocreatine = creatine + phosphate;
CC Xref=Rhea:RHEA:12977, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57947, ChEBI:CHEBI:58092; EC=3.9.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00036122};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12978;
CC Evidence={ECO:0000256|ARBA:ARBA00036122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + phosphoethanolamine = ethanolamine + phosphate;
CC Xref=Rhea:RHEA:16089, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:58190;
CC Evidence={ECO:0000256|ARBA:ARBA00036048};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16090;
CC Evidence={ECO:0000256|ARBA:ARBA00036048};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal;
CC Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00035851};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534;
CC Evidence={ECO:0000256|ARBA:ARBA00035851};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00036105};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC Evidence={ECO:0000256|ARBA:ARBA00036105};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000256|ARBA:ARBA00035865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24577;
CC Evidence={ECO:0000256|ARBA:ARBA00035865};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Extracellular vesicle membrane
CC {ECO:0000256|ARBA:ARBA00037828}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00037828}. Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00037800}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00037800}.
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DR EMBL; JU329142; AFE72898.1; -; mRNA.
DR AlphaFoldDB; H9FE39; -.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF74; ALKALINE PHOSPHATASE, TISSUE-NONSPECIFIC ISOZYME; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFE72898.1"
FT NON_TER 89
FT /evidence="ECO:0000313|EMBL:AFE72898.1"
SQ SEQUENCE 89 AA; 10609 MW; D0898AB15C98B059 CRC64;
IRDIDEIMGG GRKYMYPKNK TDVEYEIDEK ARGTRLDGLD LVNIWKSFKP RHKHSHFIWN
RTELLTLDPH NVDYLLGLFE PGDMEYELN
//
