Alkaline phosphatase, tissue-nonspecific isozyme precursor

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P09242 (PPBT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alkaline phosphatase, tissue-nonspecific isozyme
Short name=AP-TNAP
Short name=TNSALP
EC=3.1.3.1

Alternative name(s):
Alkaline phosphatase 2
Alkaline phosphatase liver/bone/kidney isozyme

Gene names

Name:	Alpl
Synonyms:	Akp-2, Akp2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	A phosphate monoester + H₂O = an alcohol + phosphate.
Cofactor	Binds 1 magnesium ion By similarity. Binds 2 zinc ions By similarity.
Subunit structure	Homodimer.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor.
Miscellaneous	In most mammals there are four different isozymes: placental, placental-like, intestinal and tissue non-specific (liver/bone/kidney).
Sequence similarities	Belongs to the alkaline phosphatase family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Magnesium Metal-binding Zinc
Molecular function	Hydrolase
PTM	GPI-anchor Glycoprotein Lipoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to organic cyclic compound Inferred from direct assay PubMed 15728361. Source: MGI cementum mineralization Inferred from electronic annotation. Source: Compara developmental process involved in reproduction Inferred from genetic interaction PubMed 17540358. Source: MGI endochondral ossification Inferred from mutant phenotype PubMed 20684022. Source: MGI response to antibiotic Inferred from direct assay PubMed 2133555. Source: MGI response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to vitamin D Inferred from electronic annotation. Source: Compara
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix part Inferred from direct assay PubMed 19874193. Source: MGI extracellular space Inferred from electronic annotation. Source: Compara plasma membrane Inferred from direct assay PubMed 10787428 PubMed 7533563. Source: MGI
Molecular_function	alkaline phosphatase activity Inferred from direct assay PubMed 10787428 PubMed 18031938 PubMed 7533563. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyrophosphatase activity Inferred from mutant phenotype PubMed 19874193. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

Chain

18 – 503

486

Alkaline phosphatase, tissue-nonspecific isozyme

PRO_0000024025

Propeptide

504 – 524

Removed in mature form Potential

PRO_0000024026

Sites

Active site

110

Phosphoserine intermediate

Metal binding

Magnesium Potential

Metal binding

Zinc 2 Potential

Metal binding

173

Magnesium Potential

Metal binding

332

Magnesium Potential

Metal binding

337

Zinc 1 Potential

Metal binding

341

Zinc 1 Potential

Metal binding

378

Zinc 2 Potential

Metal binding

379

Zinc 2 Potential

Metal binding

454

Zinc 1 Potential

Amino acid modifications

Lipidation

503

GPI-anchor amidated glycine Potential

Glycosylation

140

N-linked (GlcNAc...) Ref.6

Glycosylation

230

N-linked (GlcNAc...) Ref.6

Glycosylation

271

N-linked (GlcNAc...) Potential

Glycosylation

303

N-linked (GlcNAc...) Ref.6

Glycosylation

430

N-linked (GlcNAc...) Ref.6

Glycosylation

439

N-linked (GlcNAc...) Ref.6

Experimental info

Sequence conflict

521

R → P in AAA39928. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P09242 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 59D99110C60FA050
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FASTA

524

57,514

        10         20         30         40         50         60 
MISPFLVLAI GTCLTNSFVP EKERDPSYWR QQAQETLKNA LKLQKLNTNV AKNVIMFLGD 

        70         80         90        100        110        120 
GMGVSTVTAA RILKGQLHHN TGEETRLEMD KFPFVALSKT YNTNAQVPDS AGTATAYLCG 

       130        140        150        160        170        180 
VKANEGTVGV SAATERTRCN TTQGNEVTSI LRWAKDAGKS VGIVTTTRVN HATPSAAYAH 

       190        200        210        220        230        240 
SADRDWYSDN EMPPEALSQG CKDIAYQLMH NIKDIDVIMG GGRKYMYPKN RTDVEYELDE 

       250        260        270        280        290        300 
KARGTRLDGL DLISIWKSFK PRHKHSHYVW NRTELLALDP SRVDYLLGLF EPGDMQYELN 

       310        320        330        340        350        360 
RNNLTDPSLS EMVEVALRIL TKNLKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDQAIG 

       370        380        390        400        410        420 
KAGAMTSQKD TLTVVTADHS HVFTFGGYTP RGNSIFGLAP MVSDTDKKPF TAILYGNGPG 

       430        440        450        460        470        480 
YKVVDGEREN VSMVDYAHNN YQAQSAVPLR HETHGGEDVA VFAKGPMAHL LHGVHEQNYI 

       490        500        510        520 
PHVMAYASCI GANLDHCAWA GSGSAPSPGA LLLPLAVLSL RTLF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a cDNA coding for mouse placental alkaline phosphatase." Terao M., Mintz B. Proc. Natl. Acad. Sci. U.S.A. 84:7051-7055(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"The transcriptional landscape of the mammalian genome." 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. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Forelimb.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[5]	"Induction of alkaline phosphatase in mouse L cells by overexpression of the catalytic subunit of cAMP-dependent protein kinase." Brown N.A., Stofko R.E., Uhler M.D. J. Biol. Chem. 265:13181-13189(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-6.
[6]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140; ASN-230; ASN-303; ASN-430 AND ASN-439, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02980 mRNA. Translation: AAA39928.1. AK161780 mRNA. Translation: BAE36569.1. AK167023 mRNA. Translation: BAE39196.1. AL805954, AL807764 Genomic DNA. Translation: CAM19406.1. AL807764, AL805954 Genomic DNA. Translation: CAM23370.1. BC065175 mRNA. Translation: AAH65175.1. M54798 mRNA. Translation: AAA37217.1.
IPI	IPI00134743.
RefSeq	NP_031457.2. NM_007431.2.
UniGene	Mm.288186.
3D structure databases
HSSP	HSSP built from PDB template 1K7H based on UniProtKB Q9BHT8.
ProteinModelPortal	P09242.
SMR	P09242. Positions 19-490.
ModBase	Search...
PTM databases
PhosphoSite	P09242.
Proteomic databases
PaxDb	P09242.
PRIDE	P09242.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030551; ENSMUSP00000030551; ENSMUSG00000028766.
GeneID	11647.
KEGG	mmu:11647.
Organism-specific databases
CTD	249.
MGI	MGI:87983. Alpl.
Phylogenomic databases
eggNOG	COG1785.
GeneTree	ENSGT00390000008704.
HOGENOM	HOG000099118.
HOVERGEN	HBG007345.
InParanoid	Q6P1B0.
KO	K01077.
OMA	MVTGVKT.
OrthoDB	EOG4NGGMN.
Enzyme and pathway databases
SABIO-RK	P09242.
Gene expression databases
ArrayExpress	P09242.
Bgee	P09242.
CleanEx	MM_ALPL.
Genevestigator	P09242.
GermOnline	ENSMUSG00000028766. Mus musculus.
Family and domain databases
Gene3D	3.40.720.10. 1 hit.
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR001952. Alkaline_phosphatase. IPR018299. Alkaline_phosphatase_AS. IPR017850. Alkaline_phosphatase_core. [Graphical view]
Pfam	PF00245. Alk_phosphatase. 1 hit. [Graphical view]
PRINTS	PR00113. ALKPHPHTASE.
SMART	SM00098. alkPPc. 1 hit. [Graphical view]
SUPFAM	SSF53649. Alkaline_phosphatase_core. 1 hit.
PROSITE	PS00123. ALKALINE_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL2660.
NextBio	279245.
SOURCE	Search...

Entry information

Entry name

PPBT_MOUSE

Accession

Primary (citable) accession number: P09242
Secondary accession number(s): Q6P1B0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents