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P09242 (PPBT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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-anchorGPI-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 componentCell membrane
Membrane
   DomainSignal
   LigandMagnesium
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to organic cyclic compound

Inferred from direct assay PubMed 15728361. Source: MGI

cementum mineralization

Inferred from electronic annotation. Source: Ensembl

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

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to vitamin D

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix

Inferred from direct assay PubMed 19874193. Source: MGI

extracellular membrane-bounded organelle

Inferred from direct assay PubMed 19874193. Source: MGI

extracellular space

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 10787428PubMed 7533563. Source: MGI

   Molecular_functionalkaline phosphatase activity

Inferred from direct assay PubMed 10787428PubMed 18031938PubMed 7533563. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 23055941. Source: MGI

pyrophosphatase activity

Inferred from mutant phenotype PubMed 19874193. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717
Chain18 – 503486Alkaline phosphatase, tissue-nonspecific isozyme
PRO_0000024025
Propeptide504 – 52421Removed in mature form Potential
PRO_0000024026

Sites

Active site1101Phosphoserine intermediate
Metal binding601Magnesium By similarity
Metal binding601Zinc 1 By similarity
Metal binding1101Zinc 1 By similarity
Metal binding1731Magnesium By similarity
Metal binding3321Magnesium By similarity
Metal binding3371Zinc 2 By similarity
Metal binding3411Zinc 2; via tele nitrogen By similarity
Metal binding3781Zinc 1 By similarity
Metal binding3791Zinc 1; via tele nitrogen By similarity
Metal binding4541Zinc 2; via tele nitrogen By similarity

Amino acid modifications

Lipidation5031GPI-anchor amidated glycine Potential
Glycosylation1401N-linked (GlcNAc...) Ref.6
Glycosylation2301N-linked (GlcNAc...) Ref.6
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Ref.6
Glycosylation4301N-linked (GlcNAc...) Ref.6
Glycosylation4391N-linked (GlcNAc...); atypical Ref.6
Disulfide bond139 ↔ 201 By similarity
Disulfide bond489 ↔ 497 By similarity

Experimental info

Sequence conflict5211R → P in AAA39928. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P09242 [UniParc].

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

FASTA52457,514
        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' 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. expand/collapse author list , 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.
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. expand/collapse author list , 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.
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.
+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.
CCDSCCDS18821.1.
RefSeqNP_001274101.1. NM_001287172.1.
NP_001274105.1. NM_001287176.1.
NP_031457.2. NM_007431.3.
XP_006538560.1. XM_006538497.1.
XP_006538561.1. XM_006538498.1.
XP_006538562.1. XM_006538499.1.
XP_006538563.1. XM_006538500.1.
UniGeneMm.288186.

3D structure databases

ProteinModelPortalP09242.
SMRP09242. Positions 19-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198053. 1 interaction.
IntActP09242. 1 interaction.

Chemistry

ChEMBLCHEMBL2660.

PTM databases

PhosphoSiteP09242.

Proteomic databases

MaxQBP09242.
PaxDbP09242.
PRIDEP09242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030551; ENSMUSP00000030551; ENSMUSG00000028766.
GeneID11647.
KEGGmmu:11647.
UCSCuc008vjr.2. mouse.

Organism-specific databases

CTD249.
MGIMGI:87983. Alpl.

Phylogenomic databases

eggNOGCOG1785.
GeneTreeENSGT00390000008704.
HOGENOMHOG000099118.
HOVERGENHBG007345.
InParanoidQ6P1B0.
KOK01077.
OMARGNCAST.
OrthoDBEOG7SN8CH.
TreeFamTF323513.

Enzyme and pathway databases

SABIO-RKP09242.

Gene expression databases

ArrayExpressP09242.
BgeeP09242.
CleanExMM_ALPL.
GenevestigatorP09242.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00113. ALKPHPHTASE.
SMARTSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279245.
PROP09242.
SOURCESearch...

Entry information

Entry namePPBT_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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