PPBT_CHICK
ID PPBT_CHICK Reviewed; 519 AA.
AC Q92058;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Alkaline phosphatase, tissue-nonspecific isozyme {ECO:0000303|PubMed:8563025};
DE Short=AP-TNAP;
DE Short=TNSALP;
DE EC=3.1.3.1 {ECO:0000269|PubMed:20026305};
DE AltName: Full=Phosphoamidase {ECO:0000305};
DE Flags: Precursor;
GN Name=ALPL;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8563025; DOI=10.1002/aja.1002040107;
RA Crawford K., Weissig H., Binette F., Millan J.L., Goetinck P.F.;
RT "Tissue-nonspecific alkaline phosphatase participates in the establishment
RT and growth of feather germs in embryonic chick skin cultures.";
RL Dev. Dyn. 204:48-56(1995).
RN [2]
RP CATALYTIC ACTIVITY.
RX PubMed=20026305; DOI=10.1016/j.bbrc.2009.12.083;
RA Sekrecka-Belniak A., Balcerzak M., Buchet R., Pikula S.;
RT "Active creatine kinase is present in matrix vesicles isolated from femurs
RT of chicken embryo: Implications for bone mineralization.";
RL Biochem. Biophys. Res. Commun. 391:1432-1436(2010).
CC -!- FUNCTION: Alkaline phosphatase that metabolizes various phosphate
CC compounds and plays a key role in skeletal mineralization and adaptive
CC thermogenesis (By similarity). Has broad substrate specificity and can
CC hydrolyze a considerable variety of compounds: however, only a few
CC substrates, such as diphosphate (inorganic pyrophosphate; PPi) and
CC pyridoxal 5'-phosphate (PLP) are natural substrates (By similarity).
CC Plays an essential role in skeletal and dental mineralization via its
CC ability to hydrolyze extracellular diphosphate, a potent mineralization
CC inhibitor, to phosphate: it thereby promotes hydroxyapatite crystal
CC formation and increases inorganic phosphate concentration (By
CC similarity). Catalyzes dephosphorylation of PLP to pyridoxal (PL), the
CC transportable form of vitamin B6, in order to provide a sufficient
CC amount of PLP in the brain, an essential cofactor for enzymes
CC catalyzing the synthesis of diverse neurotransmitters (By similarity).
CC Additionally, also able to mediate ATP degradation in a stepwise manner
CC to adenosine, thereby regulating the availability of ligands for
CC purinergic receptors (By similarity). Involved in the establishment and
CC growth of feather germs (PubMed:8563025).
CC {ECO:0000250|UniProtKB:P05186, ECO:0000250|UniProtKB:P09242,
CC ECO:0000269|PubMed:8563025}.
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:0000255|PROSITE-ProRule:PRU10042,
CC ECO:0000269|PubMed:20026305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC Evidence={ECO:0000269|PubMed:20026305};
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:0000250|UniProtKB:P05186};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24577;
CC Evidence={ECO:0000250|UniProtKB:P05186};
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:0000250|UniProtKB:P05186};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534;
CC Evidence={ECO:0000250|UniProtKB:P05186};
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:0000250|UniProtKB:P05186};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16090;
CC Evidence={ECO:0000250|UniProtKB:P05186};
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:0000250|UniProtKB:P09242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P09242};
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:0000250|UniProtKB:P09242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC Evidence={ECO:0000250|UniProtKB:P09242};
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:0000250|UniProtKB:P09242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29376;
CC Evidence={ECO:0000250|UniProtKB:P09242};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P05187};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P05187};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P05186};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P05186};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P05186};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P05186}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05186};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P05186}. Extracellular
CC vesicle membrane {ECO:0000250|UniProtKB:P09242}; Lipid-anchor, GPI-
CC anchor {ECO:0000250|UniProtKB:P09242}. Note=Localizes to special class
CC of extracellular vesicles, named matrix vesicles (MVs), which are
CC released by osteogenic cells. {ECO:0000250|UniProtKB:P09242}.
CC -!- DOMAIN: Calcium-binding is structural and does not influence the
CC alkaline phosphatase activity. At very high concentrations, calcium can
CC however substitute for zinc at zinc-binding sites, leading to strongly
CC reduced enzyme activity. {ECO:0000250|UniProtKB:P05186}.
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR EMBL; U19108; AAA92562.1; -; mRNA.
DR RefSeq; NP_990691.1; NM_205360.1.
DR AlphaFoldDB; Q92058; -.
DR SMR; Q92058; -.
DR STRING; 9031.ENSGALP00000038334; -.
DR PaxDb; Q92058; -.
DR GeneID; 396317; -.
DR KEGG; gga:396317; -.
DR CTD; 249; -.
DR VEuPathDB; HostDB:geneid_396317; -.
DR InParanoid; Q92058; -.
DR OrthoDB; 416703at2759; -.
DR PhylomeDB; Q92058; -.
DR BRENDA; 3.1.3.1; 1306.
DR PRO; PR:Q92058; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0065010; C:extracellular membrane-bounded organelle; IDA:AgBase.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IEA:RHEA.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:AgBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:RHEA.
DR GO; GO:0050187; F:phosphoamidase activity; ISS:UniProtKB.
DR GO; GO:0052732; F:phosphoethanolamine phosphatase activity; IEA:RHEA.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016462; F:pyrophosphatase activity; ISS:UniProtKB.
DR GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:UniProtKB.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; PTHR11596; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Signal; Zinc.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..498
FT /note="Alkaline phosphatase, tissue-nonspecific isozyme"
FT /id="PRO_0000024029"
FT PROPEP 499..519
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024030"
FT ACT_SITE 109
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P05187,
FT ECO:0000255|PROSITE-ProRule:PRU10042"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT LIPID 498
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 138..200
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT DISULFID 488..496
FT /evidence="ECO:0000250|UniProtKB:P05187"
SQ SEQUENCE 519 AA; 56760 MW; 7934C0EEC3B17B89 CRC64;
MKAFLLTLLA QLCSASLVPE REKDPEYWRQ QAQETLRDAL RLQHLNQNVA KNLILFLGDG
MGVSTVTAAR ILKGQLQHRK GEESLLEMDK FPYVALAKTY NTNAQVPDSA GTATAYLCGV
KANEGTVGVS AGVTRDRCNT TKGQEVTSIL RWAKDEGKAV GIVTTTRVTH ATPSAAYAHS
ANRDWYSDGE MPLDALEGGC KDIARQLVDN IPDIEVILGG GRKYMFPKNT SDVEYPQEER
HRGTRLDGKD LVQAWHDTKP AGKVAKYVWH RRELLALNVS RVDFLLGLFE PGDMVYELDR
NNETDPSLSE MVAVAIRMLQ KNPRGFFLLV EGGRIDHGHH EGKAKQALHE AVELDRAVGL
AGRLTSPRDT LSVVTADHSH VFTFGGYTPR GNPIFGLAPM QSDVDRKPFT SILYGNGPGY
KIVGGERENV SAVDFAHANY QAQAAVPLRQ ETHGGEDVAV FARGPMAHLL HGVDEQNYIP
HAMAYAACIG PNRAHCSSAA RPAATATLLP VLLLLLLLC
