PPBT_RAT
ID PPBT_RAT Reviewed; 524 AA.
AC P08289; P14055; P70707;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Alkaline phosphatase, tissue-nonspecific isozyme {ECO:0000303|PubMed:32710882};
DE Short=AP-TNAP;
DE Short=TNAP {ECO:0000303|PubMed:32710882};
DE Short=TNSALP;
DE EC=3.1.3.1 {ECO:0000305|PubMed:2895632};
DE AltName: Full=Alkaline phosphatase liver/bone/kidney isozyme;
DE AltName: Full=Phosphoamidase {ECO:0000305};
DE AltName: Full=Phosphocreatine phosphatase {ECO:0000250|UniProtKB:P09242};
DE EC=3.9.1.1 {ECO:0000250|UniProtKB:P09242};
DE Flags: Precursor;
GN Name=Alpl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=3422431; DOI=10.1073/pnas.85.2.319;
RA Thiede M.A., Yoon K., Golub E.E., Noda M., Rodan G.A.;
RT "Structure and expression of rat osteosarcoma (ROS 17/2.8) alkaline
RT phosphatase: product of a single copy gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:319-323(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 355-360 AND 401-404, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=2895632; DOI=10.1042/bj2490661;
RA Misumi Y., Tashiro K., Hattori M., Sakaki Y., Ikehara Y.;
RT "Primary structure of rat liver alkaline phosphatase deduced from its
RT cDNA.";
RL Biochem. J. 249:661-668(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2544423; DOI=10.1111/j.1432-1033.1989.tb14822.x;
RA Toh Y., Yamamoto M., Endo H., Misumi Y., Ikehara Y.;
RT "Isolation and characterization of a rat liver alkaline phosphatase gene. A
RT single gene with two promoters.";
RL Eur. J. Biochem. 182:231-237(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 18-47, AND GPI-ANCHOR.
RC TISSUE=Liver;
RX PubMed=2834351; DOI=10.1093/oxfordjournals.jbchem.a122211;
RA Ogata S., Hayashi Y., Yasutake K., Ikehara Y.;
RT "Chemical identification of lipid components in the membranous form of rat
RT liver alkaline phosphatase.";
RL J. Biochem. 102:1609-1615(1987).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=32710882; DOI=10.1016/j.abb.2020.108482;
RA Favarin B.Z., Bolean M., Ramos A.P., Magrini A., Rosato N., Millan J.L.,
RA Bottini M., Costa-Filho A.J., Ciancaglini P.;
RT "Lipid composition modulates ATP hydrolysis and calcium phosphate mineral
RT propagation by TNAP-harboring proteoliposomes.";
RL Arch. Biochem. Biophys. 691:108482-108482(2020).
CC -!- FUNCTION: Alkaline phosphatase that metabolizes various phosphate
CC compounds and plays a key role in skeletal mineralization and adaptive
CC thermogenesis. Has broad substrate specificity and can hydrolyze a
CC considerable variety of compounds: however, only a few substrates, such
CC as diphosphate (inorganic pyrophosphate; PPi), pyridoxal 5'-phosphate
CC (PLP) and N-phosphocreatine are natural substrates. Plays an essential
CC role in skeletal and dental mineralization via its ability to hydrolyze
CC extracellular diphosphate, a potent mineralization inhibitor, to
CC phosphate: it thereby promotes hydroxyapatite crystal formation and
CC increases inorganic phosphate concentration. Acts in a non-redundant
CC manner with PHOSPHO1 in skeletal mineralization: while PHOSPHO1
CC mediates the initiation of hydroxyapatite crystallization in the matrix
CC vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite
CC crystallization in the extracellular matrix. Also promotes
CC dephosphorylation of osteopontin (SSP1), an inhibitor of hydroxyapatite
CC crystallization in its phosphorylated state; it is however unclear
CC whether ALPL/TNAP mediates SSP1 dephosphorylation via a direct or
CC indirect manner. Catalyzes dephosphorylation of PLP to pyridoxal (PL),
CC the 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. Additionally,
CC also able to mediate ATP degradation in a stepwise manner to adenosine,
CC thereby regulating the availability of ligands for purinergic receptors
CC (By similarity). Also capable of dephosphorylating microbial products,
CC such as lipopolysaccharides (LPS) as well as other phosphorylated
CC small-molecules, such as poly-inosine:cytosine (poly I:C) (By
CC similarity). Acts as a key regulator of adaptive thermogenesis as part
CC of the futile creatine cycle: localizes to the mitochondria of
CC thermogenic fat cells and acts by mediating hydrolysis of N-
CC phosphocreatine to initiate a futile cycle of creatine
CC dephosphorylation and phosphorylation. During the futile creatine
CC cycle, creatine and N-phosphocreatine are in a futile cycle, which
CC dissipates the high energy charge of N-phosphocreatine as heat without
CC performing any mechanical or chemical work (By similarity).
CC {ECO:0000250|UniProtKB:P05186, ECO:0000250|UniProtKB:P09242}.
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:0000305|PubMed:2895632};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018;
CC Evidence={ECO:0000305|PubMed:2895632};
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:P09242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24577;
CC Evidence={ECO:0000250|UniProtKB:P09242};
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=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:0000250|UniProtKB:P09242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12978;
CC Evidence={ECO:0000250|UniProtKB:P09242};
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:P05187};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P05187};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P05186};
CC -!- ACTIVITY REGULATION: Phosphatase activity is specifically inhibited by
CC 5-((5-chloro-2-methoxyphenyl)sulfonamido)nicotinamide (SBI-425).
CC {ECO:0000250|UniProtKB:P09242}.
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:0000269|PubMed:32710882}; Lipid-anchor, GPI-
CC anchor {ECO:0000250|UniProtKB:P09242}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P09242}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:P09242}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:P09242}. Note=Localizes to special class of
CC extracellular vesicles, named matrix vesicles (MVs), which are released
CC by osteogenic cells (PubMed:32710882). Localizes to the mitochondria of
CC thermogenic fat cells: tethered to mitochondrial membranes via a GPI-
CC anchor and probably resides in the mitochondrion intermembrane space
CC (By similarity). {ECO:0000250|UniProtKB:P09242,
CC ECO:0000269|PubMed:32710882}.
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 -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P05186}.
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR EMBL; Y00714; CAA68703.1; -; mRNA.
DR EMBL; J03572; AAA41845.1; -; mRNA.
DR EMBL; X16028; CAA34160.1; -; Genomic_DNA.
DR EMBL; X16029; CAA34160.1; JOINED; Genomic_DNA.
DR EMBL; X16030; CAA34160.1; JOINED; Genomic_DNA.
DR EMBL; X16031; CAA34160.1; JOINED; Genomic_DNA.
DR EMBL; X16032; CAA34160.1; JOINED; Genomic_DNA.
DR EMBL; X16033; CAA34160.1; JOINED; Genomic_DNA.
DR EMBL; X16034; CAA34160.1; JOINED; Genomic_DNA.
DR EMBL; X16035; CAA34160.1; JOINED; Genomic_DNA.
DR EMBL; X16036; CAA34160.1; JOINED; Genomic_DNA.
DR EMBL; X16037; CAA34160.1; JOINED; Genomic_DNA.
DR EMBL; X16038; CAA34160.1; JOINED; Genomic_DNA.
DR EMBL; BC088399; AAH88399.1; -; mRNA.
DR PIR; A28114; A28114.
DR PIR; S00289; S00289.
DR RefSeq; NP_037191.1; NM_013059.1.
DR RefSeq; XP_006239198.1; XM_006239136.3.
DR RefSeq; XP_017448654.1; XM_017593165.1.
DR AlphaFoldDB; P08289; -.
DR SMR; P08289; -.
DR BioGRID; 247616; 1.
DR IntAct; P08289; 1.
DR STRING; 10116.ENSRNOP00000019004; -.
DR BindingDB; P08289; -.
DR ChEMBL; CHEMBL2729; -.
DR GlyConnect; 12; 31 N-Linked glycans.
DR GlyGen; P08289; 6 sites, 56 N-linked glycans (1 site).
DR iPTMnet; P08289; -.
DR PhosphoSitePlus; P08289; -.
DR PaxDb; P08289; -.
DR PRIDE; P08289; -.
DR Ensembl; ENSRNOT00000019004; ENSRNOP00000019004; ENSRNOG00000013954.
DR GeneID; 25586; -.
DR KEGG; rno:25586; -.
DR UCSC; RGD:2100; rat.
DR CTD; 249; -.
DR RGD; 2100; Alpl.
DR eggNOG; KOG4126; Eukaryota.
DR GeneTree; ENSGT00950000183063; -.
DR HOGENOM; CLU_008539_4_0_1; -.
DR InParanoid; P08289; -.
DR OMA; IGQAGTM; -.
DR OrthoDB; 416703at2759; -.
DR PhylomeDB; P08289; -.
DR TreeFam; TF323513; -.
DR BRENDA; 3.1.3.1; 5301.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SABIO-RK; P08289; -.
DR PRO; PR:P08289; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013954; Expressed in adult mammalian kidney and 19 other tissues.
DR ExpressionAtlas; P08289; baseline and differential.
DR Genevisible; P08289; RN.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0065010; C:extracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IEA:RHEA.
DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016462; F:pyrophosphatase activity; ISS:UniProtKB.
DR GO; GO:0110148; P:biomineralization; ISO:RGD.
DR GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
DR GO; GO:0019725; P:cellular homeostasis; ISO:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0071529; P:cementum mineralization; IEP:RGD.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0003006; P:developmental process involved in reproduction; ISO:RGD.
DR GO; GO:0001958; P:endochondral ossification; ISO:RGD.
DR GO; GO:0140651; P:futile creatine cycle; ISO:RGD.
DR GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:0055062; P:phosphate ion homeostasis; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:UniProtKB.
DR GO; GO:0042822; P:pyridoxal phosphate metabolic process; ISO:RGD.
DR GO; GO:0046677; P:response to antibiotic; ISO:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IDA:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:1904383; P:response to sodium phosphate; ISO:RGD.
DR GO; GO:0034516; P:response to vitamin B6; ISO:RGD.
DR GO; GO:0033280; P:response to vitamin D; ISO:RGD.
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; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
KW Magnesium; Membrane; Metal-binding; Mitochondrion; Phosphoprotein;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:2834351"
FT CHAIN 18..501
FT /note="Alkaline phosphatase, tissue-nonspecific isozyme"
FT /id="PRO_0000024027"
FT PROPEP 502..524
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024028"
FT ACT_SITE 110
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P05187,
FT ECO:0000255|PROSITE-ProRule:PRU10042"
FT BINDING 60
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 235
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 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 501
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 139..201
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT DISULFID 489..497
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT CONFLICT 12
FT /note="T -> P (in Ref. 1; AAA41845)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="P -> R (in Ref. 1; AAA41845)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="V -> E (in Ref. 2; CAA68703)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="S -> T (in Ref. 2; CAA68703)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="V -> E (in Ref. 2; CAA68703)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="V -> L (in Ref. 2; CAA68703)"
FT /evidence="ECO:0000305"
FT CONFLICT 380..388
FT /note="SHVFTFGGY -> HPTFSRLVA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="R -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="A -> C (in Ref. 2; CAA68703)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="V -> I (in Ref. 2; CAA68703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 57659 MW; BD75A4B87117DF03 CRC64;
MILPFLVLAI GTCLTNSFVP EKEKDPSYWR QQAQETLKNA LKLQKLNTNV AKNIIMFLGD
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 EMVEVALRIL TKNPKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDEAIG
KAGTMTSQKD TLTVVTADHS HVFTFGGYTP RGNSIFGLAP MVSDTDKKPF TAILYGNGPG
YKVVDGEREN VSMVDYAHNN YQAQSAVPLR HETHGGEDVA VFAKGPMAHL LHGVHEQNYI
PHVMAYASCI GANLDHCAWA SSASSPSPGA LLLPLALFPL RTLF
