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Alkaline phosphatase, placental-like (EC 3.1.3.1) (Alkaline phosphatase 5) (Embryonic alkaline phosphatase) (EAP) (Embryonic-type alkaline phosphatase)

 PPBN_MOUSE              Reviewed;         529 AA.
P24823; Q3ULC9;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 140.
RecName: Full=Alkaline phosphatase, placental-like;
EC=3.1.3.1;
AltName: Full=Alkaline phosphatase 5;
AltName: Full=Embryonic alkaline phosphatase;
Short=EAP;
AltName: Full=Embryonic-type alkaline phosphatase;
Flags: Precursor;
Name=Alppl2; Synonyms=Akp5, Eap;
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 [GENOMIC DNA].
PubMed=2286375; DOI=10.1016/0888-7543(90)90042-S;
Manes T., Glade K., Ziomek C.A., Millan J.L.;
"Genomic structure and comparison of mouse tissue-specific alkaline
phosphatase genes.";
Genomics 8:541-554(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
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].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 1 Mg(2+) ion. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions. {ECO:0000250};
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
-!- TISSUE SPECIFICITY: Embryo and testis.
-!- 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; M61704; AAA37531.1; -; Genomic_DNA.
EMBL; AK145571; BAE26520.1; -; mRNA.
EMBL; CH466520; EDL40194.1; -; Genomic_DNA.
CCDS; CCDS15126.1; -.
RefSeq; NP_031459.3; NM_007433.3.
RefSeq; XP_006529145.1; XM_006529082.3.
RefSeq; XP_011246206.1; XM_011247904.2.
UniGene; Mm.195224; -.
ProteinModelPortal; P24823; -.
SMR; P24823; -.
STRING; 10090.ENSMUSP00000027455; -.
BindingDB; P24823; -.
ChEMBL; CHEMBL3112374; -.
PhosphoSitePlus; P24823; -.
MaxQB; P24823; -.
PaxDb; P24823; -.
PeptideAtlas; P24823; -.
PRIDE; P24823; -.
Ensembl; ENSMUST00000027455; ENSMUSP00000027455; ENSMUSG00000026246.
Ensembl; ENSMUST00000188310; ENSMUSP00000139887; ENSMUSG00000026246.
GeneID; 11650; -.
KEGG; mmu:11650; -.
UCSC; uc007bvy.1; mouse.
CTD; 251; -.
MGI; MGI:108009; Alppl2.
eggNOG; KOG4126; Eukaryota.
eggNOG; COG1785; LUCA.
GeneTree; ENSGT00390000008704; -.
HOGENOM; HOG000099118; -.
HOVERGEN; HBG007345; -.
InParanoid; P24823; -.
KO; K01077; -.
OMA; YVWSRKG; -.
OrthoDB; EOG091G067H; -.
TreeFam; TF323513; -.
Reactome; R-MMU-1483166; Synthesis of PA.
Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
Reactome; R-MMU-6811438; Intra-Golgi traffic.
Reactome; R-MMU-8935690; Digestion.
PRO; PR:P24823; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026246; -.
CleanEx; MM_AKP5; -.
Genevisible; P24823; MM.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0030016; C:myofibril; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0004035; F:alkaline phosphatase activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
GPI-anchor; Hydrolase; Lipoprotein; Magnesium; Membrane;
Metal-binding; Reference proteome; Signal; Zinc.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 502 Alkaline phosphatase, placental-like.
/FTId=PRO_0000024045.
PROPEP 503 529 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000024046.
ACT_SITE 110 110 Phosphoserine intermediate.
METAL 60 60 Magnesium. {ECO:0000250}.
METAL 60 60 Zinc 1. {ECO:0000250}.
METAL 110 110 Zinc 1. {ECO:0000250}.
METAL 173 173 Magnesium. {ECO:0000250}.
METAL 329 329 Magnesium. {ECO:0000250}.
METAL 334 334 Zinc 2. {ECO:0000250}.
METAL 338 338 Zinc 2; via tele nitrogen. {ECO:0000250}.
METAL 375 375 Zinc 1. {ECO:0000250}.
METAL 376 376 Zinc 1; via tele nitrogen. {ECO:0000250}.
METAL 450 450 Zinc 2; via tele nitrogen. {ECO:0000250}.
LIPID 502 502 GPI-anchor amidated serine.
{ECO:0000250}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 139 201 {ECO:0000250}.
DISULFID 485 492 {ECO:0000250}.
CONFLICT 80 81 HL -> LS (in Ref. 1; AAA37531).
{ECO:0000305}.
CONFLICT 361 362 KL -> IR (in Ref. 1; AAA37531).
{ECO:0000305}.
CONFLICT 442 442 A -> C (in Ref. 1; AAA37531).
{ECO:0000305}.
SEQUENCE 529 AA; 57202 MW; 540A95D21D90BDEC CRC64;
MWGACLLLLG LSLQVCPSVI PVEEENPAFW NRKAAEALDA AKKLKPIQTS AKNLVILMGD
GMGVSTVTAT RILKGQQQGH LGPETQLAMD RFPHMALSKT YNTDKQIPDS AGTGTAFLCG
VKTNMKVIGL SAAARFNQCN TTWGNEVVSV MHRAKKAGKS VGVVTTTSVQ HASPAGTYAH
TVNRGWYSDA QMPASALQDG CKDISTQLIS NMDIDVILGG GRKFMFPKGT PDQEYPTDTK
QAGTRLDGRN LVQEWLAKHQ GARYVWNRSE LIQASLNRSV THLMGLFEPN DMKYEIHRDP
AQDPSLAEMT EVAVRMLSRN PKGFYLFVEG GRIDHGHHET VAYRALTEAV MFDSAVDKAD
KLTSEQDTMI LVTADHSHVF SFGGYTQRGA SIFGLAPFKA EDGKSFTSIL YGNGPGYKLH
NGARADVTEE ESSNPTYQQQ AAVPLSSETH SGEDVAIFAR GPQAHLVHGV QEQNYIAHVM
AFAACLEPYT DCGLASPAGQ SSAVSPGYMS TLLCLLAGKM LMLMAAAEP


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