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Alkaline phosphatase, tissue-nonspecific isozyme (AP-TNAP) (TNSALP) (EC 3.1.3.1) (Alkaline phosphatase 2) (Alkaline phosphatase liver/bone/kidney isozyme)

 PPBT_MOUSE              Reviewed;         524 AA.
P09242; Q6P1B0;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 153.
RecName: Full=Alkaline phosphatase, tissue-nonspecific isozyme;
Short=AP-TNAP;
Short=TNSALP;
EC=3.1.3.1 {ECO:0000250|UniProtKB:P05186};
AltName: Full=Alkaline phosphatase 2;
AltName: Full=Alkaline phosphatase liver/bone/kidney isozyme;
Flags: Precursor;
Name=Alpl; Synonyms=Akp-2, Akp2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=3478679; DOI=10.1073/pnas.84.20.7051;
Terao M., Mintz B.;
"Cloning and characterization of a cDNA coding for mouse placental
alkaline phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 84:7051-7055(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Forelimb;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-6.
PubMed=2165496;
Brown N.A., Stofko R.E., Uhler M.D.;
"Induction of alkaline phosphatase in mouse L cells by overexpression
of the catalytic subunit of cAMP-dependent protein kinase.";
J. Biol. Chem. 265:13181-13189(1990).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140; ASN-230; ASN-303;
ASN-430 AND ASN-439.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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:0000250|UniProtKB:P05186, ECO:0000255|PROSITE-
ProRule:PRU10042}.
-!- 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; J02980; AAA39928.1; -; mRNA.
EMBL; AK161780; BAE36569.1; -; mRNA.
EMBL; AK167023; BAE39196.1; -; mRNA.
EMBL; AL805954; CAM19406.1; -; Genomic_DNA.
EMBL; AL807764; CAM19406.1; JOINED; Genomic_DNA.
EMBL; AL807764; CAM23370.1; -; Genomic_DNA.
EMBL; AL805954; CAM23370.1; JOINED; Genomic_DNA.
EMBL; BC065175; AAH65175.1; -; mRNA.
EMBL; M54798; AAA37217.1; -; mRNA.
CCDS; CCDS18821.1; -.
RefSeq; NP_001274101.1; NM_001287172.1.
RefSeq; NP_031457.2; NM_007431.3.
RefSeq; XP_006538560.1; XM_006538497.3.
RefSeq; XP_006538561.1; XM_006538498.3.
RefSeq; XP_006538562.1; XM_006538499.3.
RefSeq; XP_006538563.1; XM_006538500.2.
RefSeq; XP_017175413.1; XM_017319924.1.
UniGene; Mm.288186; -.
ProteinModelPortal; P09242; -.
SMR; P09242; -.
BioGrid; 198053; 2.
IntAct; P09242; 1.
STRING; 10090.ENSMUSP00000030551; -.
ChEMBL; CHEMBL2660; -.
iPTMnet; P09242; -.
PhosphoSitePlus; P09242; -.
SwissPalm; P09242; -.
MaxQB; P09242; -.
PaxDb; P09242; -.
PeptideAtlas; P09242; -.
PRIDE; P09242; -.
Ensembl; ENSMUST00000030551; ENSMUSP00000030551; ENSMUSG00000028766.
GeneID; 11647; -.
KEGG; mmu:11647; -.
UCSC; uc008vjr.3; mouse.
CTD; 249; -.
MGI; MGI:87983; Alpl.
eggNOG; KOG4126; Eukaryota.
eggNOG; COG1785; LUCA.
GeneTree; ENSGT00390000008704; -.
HOGENOM; HOG000099118; -.
HOVERGEN; HBG007345; -.
InParanoid; P09242; -.
KO; K01077; -.
OMA; EHTGTQL; -.
OrthoDB; EOG091G067H; -.
TreeFam; TF323513; -.
BRENDA; 3.1.3.1; 3474.
Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
SABIO-RK; P09242; -.
PRO; PR:P09242; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028766; -.
CleanEx; MM_ALPL; -.
ExpressionAtlas; P09242; baseline and differential.
Genevisible; P09242; MM.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0065010; C:extracellular membrane-bounded organelle; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0004035; F:alkaline phosphatase activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016462; F:pyrophosphatase activity; IMP:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
GO; GO:0071529; P:cementum mineralization; IEA:Ensembl.
GO; GO:0003006; P:developmental process involved in reproduction; IGI:MGI.
GO; GO:0001958; P:endochondral ossification; IMP:MGI.
GO; GO:0001649; P:osteoblast differentiation; ISO:MGI.
GO; GO:0046677; P:response to antibiotic; IDA:MGI.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
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; Disulfide bond; Glycoprotein;
GPI-anchor; Hydrolase; Lipoprotein; Magnesium; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Signal; Zinc.
SIGNAL 1 17
CHAIN 18 501 Alkaline phosphatase, tissue-nonspecific
isozyme.
/FTId=PRO_0000024025.
PROPEP 502 524 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000024026.
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:21183079}.
LIPID 501 501 GPI-anchor amidated glycine.
{ECO:0000255}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 439 439 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
DISULFID 139 201 {ECO:0000250|UniProtKB:P05187}.
DISULFID 489 497 {ECO:0000250|UniProtKB:P05187}.
CONFLICT 521 521 R -> P (in Ref. 1; AAA39928).
{ECO:0000305}.
SEQUENCE 524 AA; 57514 MW; 59D99110C60FA050 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 EMVEVALRIL TKNLKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDQAIG
KAGAMTSQKD TLTVVTADHS HVFTFGGYTP RGNSIFGLAP MVSDTDKKPF TAILYGNGPG
YKVVDGEREN VSMVDYAHNN YQAQSAVPLR HETHGGEDVA VFAKGPMAHL LHGVHEQNYI
PHVMAYASCI GANLDHCAWA GSGSAPSPGA LLLPLAVLSL RTLF


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