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Reviewed, UniProtKB/Swiss-Prot P08289 (PPBT_RAT)

Last modified November 3, 2009. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alkaline phosphatase, tissue-nonspecific isozyme
    EC=3.1.3.1
Alternative name(s):
    AP-TNAP
    TNSALP
    Alkaline phosphatase liver/bone/kidney isozyme
Gene names
Name: Alpl
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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. Ref.5

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.5
Chain18 – 501484Alkaline phosphatase, tissue-nonspecific isozyme
PRO_0000024027
Propeptide502 – 52423Removed in mature form Potential
PRO_0000024028

Sites

Active site1101Phosphoserine intermediate
Metal binding601Magnesium Potential
Metal binding601Zinc 2 Potential
Metal binding1731Magnesium Potential
Metal binding3321Magnesium Potential
Metal binding3371Zinc 1 Potential
Metal binding3411Zinc 1 Potential
Metal binding3781Zinc 2 Potential
Metal binding3791Zinc 2 Potential
Metal binding4541Zinc 1 Potential

Amino acid modifications

Lipidation5011GPI-anchor amidated serine Potential
Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation4301N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict121T → P in AAA41845. Ref.1
Sequence conflict1161A → Y Ref.2
Sequence conflict1931P → R in AAA41845. Ref.1
Sequence conflict2341V → E in CAA68703. Ref.2
Sequence conflict2541S → T in CAA68703. Ref.2
Sequence conflict3311V → E in CAA68703. Ref.2
Sequence conflict3741V → L in CAA68703. Ref.2
Sequence conflict380 – 3889SHVFTFGGY → HPTFSRLVA Ref.2
Sequence conflict3911R → Q Ref.2
Sequence conflict4631A → C in CAA68703. Ref.2
Sequence conflict4741V → I in CAA68703. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P08289-1 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: BD75A4B87117DF03

FASTA52457,659
        10         20         30         40         50         60 
MILPFLVLAI GTCLTNSFVP EKEKDPSYWR QQAQETLKNA LKLQKLNTNV AKNIIMFLGD 

        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 TKNPKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDEAIG 

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

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

       490        500        510        520 
PHVMAYASCI GANLDHCAWA SSASSPSPGA LLLPLALFPL RTLF

« Hide

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References

« Hide 'large scale' references
[1]"Structure and expression of rat osteosarcoma (ROS 17/2.8) alkaline phosphatase: product of a single copy gene."
Thiede M.A., Yoon K., Golub E.E., Noda M., Rodan G.A.
Proc. Natl. Acad. Sci. U.S.A. 85:319-323(1988) [PubMed: 3422431] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Primary structure of rat liver alkaline phosphatase deduced from its cDNA."
Misumi Y., Tashiro K., Hattori M., Sakaki Y., Ikehara Y.
Biochem. J. 249:661-668(1988) [PubMed: 2895632] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
[3]"Isolation and characterization of a rat liver alkaline phosphatase gene. A single gene with two promoters."
Toh Y., Yamamoto M., Endo H., Misumi Y., Ikehara Y.
Eur. J. Biochem. 182:231-237(1989) [PubMed: 2544423] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[5]"Chemical identification of lipid components in the membranous form of rat liver alkaline phosphatase."
Ogata S., Hayashi Y., Yasutake K., Ikehara Y.
J. Biochem. 102:1609-1615(1987) [PubMed: 2834351] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-47, GPI-ANCHOR.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

Y00714 mRNA. Translation: CAA68703.1.
J03572 mRNA. Translation: AAA41845.1.
X16028 expand/collapse EMBL AC list , X16029, X16030, X16031, X16032, X16033, X16034, X16035, X16036, X16037, X16038 Genomic DNA. Translation: CAA34160.1.
BC088399 mRNA. Translation: AAH88399.1.
IPIIPI00327143.
PIRA28114.
S00289.
RefSeqNP_037191.1.
UniGeneRn.82764

3D structure databases

HSSPHSSP built from PDB template 1EW2 based on UniProtKB P05187.
ModBaseSearch...

Protein-protein interaction databases

STRINGP08289.

PTM databases

GlycoSuiteDBP08289.

Genome annotation databases

EnsemblENSRNOT00000019004; ENSRNOP00000019004; ENSRNOG00000013954; Rattus norvegicus. [Genome view]
GeneID25586.
KEGGrno:25586.
NMPDRfig|10116.3.peg.24200.
UCSCNM_013059. rat.

Organism-specific databases

CTD25586.
RGD2100. Alpl.

Phylogenomic databases

HOVERGENP08289.
OMAMISPFLV.

Enzyme and pathway databases

BRENDA3.1.3.1. 248.

Gene expression databases

ArrayExpressP08289.
GenevestigatorP08289.
GermOnlineENSRNOG00000013954. Rattus norvegicus.

Family and domain databases

InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
[Graphical view]
Gene3DG3DSA:3.40.720.10. Alk_phosphtse. 1 hit.
PfamPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00113. ALKPHPHTASE.
SMARTSM00098. alkPPc. 1 hit.
[Graphical view]
PROSITEPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio607251.

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Entry information

Entry namePPBT_RAT
AccessionPrimary (citable) accession number: P08289
Secondary accession number(s): P14055, P70707
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 1992
Last modified: November 3, 2009
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents