ID O77579_BOVIN Unreviewed; 530 AA. AC O77579; DT 01-NOV-1998, integrated into UniProtKB/TrEMBL. DT 01-NOV-1998, sequence version 1. DT 02-OCT-2024, entry version 104. DE RecName: Full=Alkaline phosphatase {ECO:0000256|ARBA:ARBA00012647, ECO:0000256|RuleBase:RU003947}; DE EC=3.1.3.1 {ECO:0000256|ARBA:ARBA00012647, ECO:0000256|RuleBase:RU003947}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAC33854.1}; RN [1] {ECO:0000313|EMBL:AAC33854.1} RP NUCLEOTIDE SEQUENCE. RA Manes T., Hoylaerts M.F., Muller R., Lottspeich F., Hoelke W., Millan J.L.; RT "Bovine alkaline phosphatases."; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. 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|RuleBase:RU003947}; 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor CC {ECO:0000256|ARBA:ARBA00004589}. 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; AF052227; AAC33854.1; -; mRNA. DR AlphaFoldDB; O77579; -. DR SMR; O77579; -. 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:SF30; INTESTINAL-TYPE ALKALINE PHOSPHATASE; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00022622}; KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622}; KW Hydrolase {ECO:0000256|RuleBase:RU003947, ECO:0000313|EMBL:AAC33854.1}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR601952-2}; KW Membrane {ECO:0000256|ARBA:ARBA00022622}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2}; KW Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..530 FT /note="Alkaline phosphatase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004159869" FT ACT_SITE 111 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1" FT BINDING 61 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 172 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 174 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 330 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 335 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 339 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 376 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 377 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 451 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" SQ SEQUENCE 530 AA; 57106 MW; F8FEAB1D4D33D1F4 CRC64; MQWACVLLLL GLWLQLSLTF IPAEEEDPAF WNRQAAQALD VAKKLQPIQT AAKNVILFLG DGMGVPTVTA TRILKGQMNG KLGPETPLAM DQFPYVALSK TYNVDRQVPD SAGTATAYLC GVKGNYKTIG VSAAARYNQC NTTSGNEVTS VMNRAKKAGK SVGVVTTSRV QHASPAGAYA HTVNRNWYSD ADLPADAQTY GCQDIATQLV NNMDIDVILG GGRMYMFPEG TPDPEYPYDV NQTGVRKDKR NLVQEWQAKH QGAQYVWNRT ELLQAANDPS VTHLMGLFEP ADMKYNVQQD PTKDPTLEEM TEAALQVLSR NPQGFYLFVE GGRIDHGHHE GKAYMALTDT VMFDNAIAKA NELTSELDTL ILATADHSHV FSFGGYTLRG TSIFGLAPSK ASDNKSYTSI LYGNGPGYVL GGGLRPDVND SISEDPSYRQ QAAVPLSSES HGGEDVAVFA RGPQAHLVHG VQEETFVAHV MAFAGCVEPY TDCNLPAPSG LSDAAHLAAS PPSLALLAGA MLLLLAPALY //