ID PPBN_MOUSE Reviewed; 529 AA. AC P24823; Q3ULC9; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 25-MAY-2022, entry version 163. DE RecName: Full=Alkaline phosphatase, germ cell type {ECO:0000305}; DE EC=3.1.3.1 {ECO:0000255|PROSITE-ProRule:PRU10042}; DE AltName: Full=Alkaline phosphatase 5; DE AltName: Full=Alkaline phosphatase, placental-like; DE AltName: Full=Embryonic alkaline phosphatase {ECO:0000303|PubMed:9056646}; DE Short=EAP {ECO:0000303|PubMed:9056646}; DE AltName: Full=Embryonic-type alkaline phosphatase; DE Flags: Precursor; GN Name=Alpg; Synonyms=Akp5, Alppl2 {ECO:0000312|MGI:MGI:108009}, Eap; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX PubMed=2286375; DOI=10.1016/0888-7543(90)90042-s; RA Manes T., Glade K., Ziomek C.A., Millan J.L.; RT "Genomic structure and comparison of mouse tissue-specific alkaline RT phosphatase genes."; RL Genomics 8:541-554(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP DISRUPTION PHENOTYPE. RX PubMed=9056646; RX DOI=10.1002/(sici)1097-0177(199703)208:3<432::aid-aja13>3.0.co;2-1; RA Narisawa S., Froehlander N., Millan J.L.; RT "Inactivation of two mouse alkaline phosphatase genes and establishment of RT a model of infantile hypophosphatasia."; RL Dev. Dyn. 208:432-446(1997). CC -!- FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate CC compounds. {ECO:0000250|UniProtKB:P10696}. 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 -!- 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: Inhibited by L-leucine, EDTA and heat. CC {ECO:0000250|UniProtKB:P10696}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P05187}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. CC -!- TISSUE SPECIFICITY: Embryo and testis. {ECO:0000269|PubMed:2286375}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:9056646). Mice CC reproduce normally, give birth to live offspring and do not display any CC obvious phenotypic abnormalities (PubMed:9056646). CC {ECO:0000269|PubMed:9056646}. CC -!- MISCELLANEOUS: In most mammals there are four different isozymes: CC placental (ALPP), germ cell (ALPG), intestinal (ALPI) and tissue non- CC specific (liver/bone/kidney) (ALPL/TNAP). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M61704; AAA37531.1; -; Genomic_DNA. DR EMBL; AK145571; BAE26520.1; -; mRNA. DR EMBL; CH466520; EDL40194.1; -; Genomic_DNA. DR CCDS; CCDS15126.1; -. DR RefSeq; NP_031459.3; NM_007433.3. DR RefSeq; XP_006529145.1; XM_006529082.3. DR RefSeq; XP_011246206.1; XM_011247904.2. DR AlphaFoldDB; P24823; -. DR SMR; P24823; -. DR STRING; 10090.ENSMUSP00000027455; -. DR BindingDB; P24823; -. DR ChEMBL; CHEMBL3112374; -. DR GlyGen; P24823; 3 sites. DR iPTMnet; P24823; -. DR PhosphoSitePlus; P24823; -. DR MaxQB; P24823; -. DR PaxDb; P24823; -. DR PeptideAtlas; P24823; -. DR PRIDE; P24823; -. DR ProteomicsDB; 289734; -. DR DNASU; 11650; -. DR Ensembl; ENSMUST00000027455; ENSMUSP00000027455; ENSMUSG00000026246. DR Ensembl; ENSMUST00000188310; ENSMUSP00000139887; ENSMUSG00000026246. DR GeneID; 11650; -. DR KEGG; mmu:11650; -. DR UCSC; uc007bvy.1; mouse. DR CTD; 11650; -. DR MGI; MGI:108009; Alppl2. DR VEuPathDB; HostDB:ENSMUSG00000026246; -. DR eggNOG; KOG4126; Eukaryota. DR GeneTree; ENSGT00950000183063; -. DR HOGENOM; CLU_008539_4_0_1; -. DR InParanoid; P24823; -. DR OMA; MFRMGTP; -. DR OrthoDB; 454880at2759; -. DR PhylomeDB; P24823; -. DR TreeFam; TF323513; -. DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins. DR Reactome; R-MMU-6811438; Intra-Golgi traffic. DR BioGRID-ORCS; 11650; 2 hits in 74 CRISPR screens. DR PRO; PR:P24823; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P24823; protein. DR Bgee; ENSMUSG00000026246; Expressed in embryo and 65 other tissues. DR Genevisible; P24823; MM. DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0030016; C:myofibril; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0002020; F:protease binding; ISO:MGI. DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central. 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 2: Evidence at transcript level; KW Calcium; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; KW Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding; KW Reference proteome; Signal; Zinc. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..502 FT /note="Alkaline phosphatase, germ cell type" FT /id="PRO_0000024045" FT PROPEP 503..529 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000024046" FT ACT_SITE 110 FT /note="Phosphoserine intermediate" FT METAL 60 FT /note="Magnesium" FT /evidence="ECO:0000250|UniProtKB:P05187" FT METAL 60 FT /note="Zinc 1" FT /evidence="ECO:0000250|UniProtKB:P05187" FT METAL 110 FT /note="Zinc 1" FT /evidence="ECO:0000250|UniProtKB:P05187" FT METAL 173 FT /note="Magnesium" FT /evidence="ECO:0000250|UniProtKB:P05187" FT METAL 234 FT /note="Calcium" FT /evidence="ECO:0000250|UniProtKB:P05186" FT METAL 287 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000250|UniProtKB:P05186" FT METAL 288 FT /note="Calcium" FT /evidence="ECO:0000250|UniProtKB:P05186" FT METAL 303 FT /note="Calcium" FT /evidence="ECO:0000250|UniProtKB:P05186" FT METAL 329 FT /note="Magnesium" FT /evidence="ECO:0000250|UniProtKB:P05187" FT METAL 334 FT /note="Zinc 2" FT /evidence="ECO:0000250|UniProtKB:P05187" FT METAL 338 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000250|UniProtKB:P05187" FT METAL 375 FT /note="Zinc 1" FT /evidence="ECO:0000250|UniProtKB:P05187" FT METAL 376 FT /note="Zinc 1; via tele nitrogen" FT /evidence="ECO:0000250|UniProtKB:P05187" FT METAL 450 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000250|UniProtKB:P05187" FT LIPID 502 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 267 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 277 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 139..201 FT /evidence="ECO:0000250" FT DISULFID 485..492 FT /evidence="ECO:0000250" FT CONFLICT 80..81 FT /note="HL -> LS (in Ref. 1; AAA37531)" FT /evidence="ECO:0000305" FT CONFLICT 361..362 FT /note="KL -> IR (in Ref. 1; AAA37531)" FT /evidence="ECO:0000305" FT CONFLICT 442 FT /note="A -> C (in Ref. 1; AAA37531)" FT /evidence="ECO:0000305" SQ 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 //