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Alkaline phosphatase, tissue-nonspecific isozyme (AP-TNAP) (TNSALP) (EC 3.1.3.1) (Alkaline phosphatase liver/bone/kidney isozyme)

 PPBT_RAT                Reviewed;         524 AA.
P08289; P14055; P70707;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 2.
30-AUG-2017, entry version 151.
RecName: Full=Alkaline phosphatase, tissue-nonspecific isozyme;
Short=AP-TNAP;
Short=TNSALP;
EC=3.1.3.1 {ECO:0000305|PubMed:2895632};
AltName: Full=Alkaline phosphatase liver/bone/kidney isozyme;
Flags: Precursor;
Name=Alpl;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=3422431; DOI=10.1073/pnas.85.2.319;
Thiede M.A., Yoon K., Golub E.E., Noda M., Rodan G.A.;
"Structure and expression of rat osteosarcoma (ROS 17/2.8) alkaline
phosphatase: product of a single copy gene.";
Proc. Natl. Acad. Sci. U.S.A. 85:319-323(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 355-360 AND 401-404,
AND CATALYTIC ACTIVITY.
STRAIN=Wistar; TISSUE=Liver;
PubMed=2895632; DOI=10.1042/bj2490661;
Misumi Y., Tashiro K., Hattori M., Sakaki Y., Ikehara Y.;
"Primary structure of rat liver alkaline phosphatase deduced from its
cDNA.";
Biochem. J. 249:661-668(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=2544423; DOI=10.1111/j.1432-1033.1989.tb14822.x;
Toh Y., Yamamoto M., Endo H., Misumi Y., Ikehara Y.;
"Isolation and characterization of a rat liver alkaline phosphatase
gene. A single gene with two promoters.";
Eur. J. Biochem. 182:231-237(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 18-47, AND GPI-ANCHOR.
TISSUE=Liver;
PubMed=2834351;
Ogata S., Hayashi Y., Yasutake K., Ikehara Y.;
"Chemical identification of lipid components in the membranous form of
rat liver alkaline phosphatase.";
J. Biochem. 102:1609-1615(1987).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: This isozyme may play a role in skeletal mineralization.
{ECO:0000250|UniProtKB:P05186}.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042,
ECO:0000305|PubMed:2895632}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P05187};
Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P05187};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P05187};
Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P05187};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P05186}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P05186}; Lipid-anchor, GPI-anchor
{ECO:0000250|UniProtKB:P05186}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P05186}.
-!- MISCELLANEOUS: In most mammals there are four different isozymes:
placental, placental-like, intestinal and tissue non-specific
(liver/bone/kidney).
-!- SIMILARITY: Belongs to the alkaline phosphatase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y00714; CAA68703.1; -; mRNA.
EMBL; J03572; AAA41845.1; -; mRNA.
EMBL; X16028; CAA34160.1; -; Genomic_DNA.
EMBL; X16029; CAA34160.1; JOINED; Genomic_DNA.
EMBL; X16030; CAA34160.1; JOINED; Genomic_DNA.
EMBL; X16031; CAA34160.1; JOINED; Genomic_DNA.
EMBL; X16032; CAA34160.1; JOINED; Genomic_DNA.
EMBL; X16033; CAA34160.1; JOINED; Genomic_DNA.
EMBL; X16034; CAA34160.1; JOINED; Genomic_DNA.
EMBL; X16035; CAA34160.1; JOINED; Genomic_DNA.
EMBL; X16036; CAA34160.1; JOINED; Genomic_DNA.
EMBL; X16037; CAA34160.1; JOINED; Genomic_DNA.
EMBL; X16038; CAA34160.1; JOINED; Genomic_DNA.
EMBL; BC088399; AAH88399.1; -; mRNA.
PIR; A28114; A28114.
PIR; S00289; S00289.
RefSeq; NP_037191.1; NM_013059.1.
RefSeq; XP_006239198.1; XM_006239136.3.
RefSeq; XP_017448654.1; XM_017593165.1.
UniGene; Rn.82764; -.
ProteinModelPortal; P08289; -.
SMR; P08289; -.
IntAct; P08289; 1.
STRING; 10116.ENSRNOP00000019004; -.
BindingDB; P08289; -.
ChEMBL; CHEMBL2729; -.
iPTMnet; P08289; -.
PhosphoSitePlus; P08289; -.
UniCarbKB; P08289; -.
PaxDb; P08289; -.
PRIDE; P08289; -.
Ensembl; ENSRNOT00000019004; ENSRNOP00000019004; ENSRNOG00000013954.
GeneID; 25586; -.
KEGG; rno:25586; -.
UCSC; RGD:2100; rat.
CTD; 249; -.
RGD; 2100; Alpl.
eggNOG; KOG4126; Eukaryota.
eggNOG; COG1785; LUCA.
GeneTree; ENSGT00390000008704; -.
HOGENOM; HOG000099118; -.
HOVERGEN; HBG007345; -.
InParanoid; P08289; -.
KO; K01077; -.
OMA; EHTGTQL; -.
OrthoDB; EOG091G067H; -.
PhylomeDB; P08289; -.
TreeFam; TF323513; -.
BRENDA; 3.1.3.1; 5301.
Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
SABIO-RK; P08289; -.
PRO; PR:P08289; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000013954; -.
ExpressionAtlas; P08289; baseline and differential.
Genevisible; P08289; RN.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0065010; C:extracellular membrane-bounded organelle; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:Ensembl.
GO; GO:0004035; F:alkaline phosphatase activity; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016462; F:pyrophosphatase activity; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0071529; P:cementum mineralization; IEP:RGD.
GO; GO:0016311; P:dephosphorylation; IMP:RGD.
GO; GO:0003006; P:developmental process involved in reproduction; IEA:Ensembl.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IDA:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
CDD; cd16012; ALP; 1.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR001952; Alkaline_phosphatase.
InterPro; IPR018299; Alkaline_phosphatase_AS.
InterPro; IPR017850; Alkaline_phosphatase_core.
PANTHER; PTHR11596; PTHR11596; 1.
Pfam; PF00245; Alk_phosphatase; 1.
PRINTS; PR00113; ALKPHPHTASE.
SMART; SM00098; alkPPc; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
Magnesium; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Signal; Zinc.
SIGNAL 1 17 {ECO:0000269|PubMed:2834351}.
CHAIN 18 501 Alkaline phosphatase, tissue-nonspecific
isozyme.
/FTId=PRO_0000024027.
PROPEP 502 524 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000024028.
ACT_SITE 110 110 Phosphoserine intermediate.
{ECO:0000250|UniProtKB:P05187}.
METAL 60 60 Magnesium.
{ECO:0000250|UniProtKB:P05187}.
METAL 60 60 Zinc 1. {ECO:0000250|UniProtKB:P05187}.
METAL 110 110 Zinc 1. {ECO:0000250|UniProtKB:P05187}.
METAL 173 173 Magnesium.
{ECO:0000250|UniProtKB:P05187}.
METAL 332 332 Magnesium.
{ECO:0000250|UniProtKB:P05187}.
METAL 337 337 Zinc 2. {ECO:0000250|UniProtKB:P05187}.
METAL 341 341 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P05187}.
METAL 378 378 Zinc 1. {ECO:0000250|UniProtKB:P05187}.
METAL 379 379 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P05187}.
METAL 454 454 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P05187}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
LIPID 501 501 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 139 201 {ECO:0000250|UniProtKB:P05187}.
DISULFID 489 497 {ECO:0000250|UniProtKB:P05187}.
CONFLICT 12 12 T -> P (in Ref. 1; AAA41845).
{ECO:0000305}.
CONFLICT 116 116 A -> Y (in Ref. 2). {ECO:0000305}.
CONFLICT 193 193 P -> R (in Ref. 1; AAA41845).
{ECO:0000305}.
CONFLICT 234 234 V -> E (in Ref. 2; CAA68703).
{ECO:0000305}.
CONFLICT 254 254 S -> T (in Ref. 2; CAA68703).
{ECO:0000305}.
CONFLICT 331 331 V -> E (in Ref. 2; CAA68703).
{ECO:0000305}.
CONFLICT 374 374 V -> L (in Ref. 2; CAA68703).
{ECO:0000305}.
CONFLICT 380 388 SHVFTFGGY -> HPTFSRLVA (in Ref. 2).
{ECO:0000305}.
CONFLICT 391 391 R -> Q (in Ref. 2). {ECO:0000305}.
CONFLICT 463 463 A -> C (in Ref. 2; CAA68703).
{ECO:0000305}.
CONFLICT 474 474 V -> I (in Ref. 2; CAA68703).
{ECO:0000305}.
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


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