PPBN_MOUSE
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 03-AUG-2022, entry version 164.
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}.
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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 morula and 25 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 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 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05187"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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
