ID B7XGA6_MOUSE Unreviewed; 524 AA. AC B7XGA6; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 24-JAN-2024, entry version 72. DE RecName: Full=Alkaline phosphatase {ECO:0000256|RuleBase:RU003947}; DE EC=3.1.3.1 {ECO:0000256|RuleBase:RU003947}; GN Name=Alpl {ECO:0000313|EMBL:BAH03518.1, ECO:0000313|MGI:MGI:87983}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAH03518.1}; RN [1] {ECO:0000313|EMBL:BAH03518.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Balb/c {ECO:0000313|EMBL:BAH03518.1}; RC TISSUE=Liver {ECO:0000313|EMBL:BAH03518.1}; RA Kanda G., Ochiai H., Hayashi Y., Harashima H., Kamiya H.; RT "Alkaline phosphatase from liver of mouse strains Balb/c and KK-Ay."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. 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 -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2}; CC Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2}; CC Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Extracellular CC vesicle membrane {ECO:0000256|ARBA:ARBA00037828}; Lipid-anchor, GPI- CC anchor {ECO:0000256|ARBA:ARBA00037828}. Membrane CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor CC {ECO:0000256|ARBA:ARBA00004589}. Mitochondrion membrane CC {ECO:0000256|ARBA:ARBA00037800}; Lipid-anchor, GPI-anchor CC {ECO:0000256|ARBA:ARBA00037800}. CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. CC {ECO:0000256|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB473959; BAH03518.1; -; mRNA. DR AlphaFoldDB; B7XGA6; -. DR IntAct; B7XGA6; 1. DR MINT; B7XGA6; -. DR SwissPalm; B7XGA6; -. DR PeptideAtlas; B7XGA6; -. DR AGR; MGI:87983; -. DR MGI; MGI:87983; Alpl. DR ChiTaRS; Alpl; mouse. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd16012; ALP; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1. DR InterPro; IPR001952; Alkaline_phosphatase. DR InterPro; IPR018299; Alkaline_phosphatase_AS. 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 PRINTS; PR00113; ALKPHPHTASE. DR SMART; SM00098; alkPPc; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1. PE 2: Evidence at transcript level; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003947}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR601952-2}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR601952-2}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}. FT SIGNAL 1..17 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 18..524 FT /note="Alkaline phosphatase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002863669" FT ACT_SITE 110 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1" FT BINDING 60 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 60 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 171 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 173 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 332 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 337 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 341 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 378 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 379 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 454 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" SQ SEQUENCE 524 AA; 57470 MW; 7821200546ABE07A CRC64; MISPFLVLAI GTCLTNSFVP EKERDPSYWR QQAQETLKNA LKLQKLNTNV AKNVIMFLGD GMGVSTVTAA RILKGQLHHN TGEETRLEMD KFPFVALSKT YNTNAQVPDS AGTATAYLCG VKANEGTVGV SAATERTRCN TTQGNEVTSI LRWAKDAGKS VGIVTTTRVN HATPSAAYAH SADRDWYSDN EMPPEALSQG CKDIAYQLMH NIKDIDVIMG GGRKYMYPKN RTDVEYELDE KARGTRLDGL DLISIWKSFK PRHKHSHYVW NRTELLALDP SRVDYLLGLF EPGDMQYELN RNNLTDPSLS EMVEVALQIL TKNPKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDQAIG KAGAMTSQKD TLTVVTADHS HVFTFGGYTP RGNSIFGLAP MVSDTDKKPF TAILYGNGPG YKVVDGEREN VSMVDYAHNN YQAQSAVPLR HETHGGEDVA VFAKGPMAHL LHGVHEQNYI PHVMAYASCI GANLDHCAWA GSGSAPSPGA LLLPLAVLSL RTLF //