Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P05187 (PPB1_HUMAN)

Last modified November 4, 2008. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alkaline phosphatase, placental type
    EC=3.1.3.1
Alternative name(s):
    PLAP-1
    Alkaline phosphatase Regan isozyme
Gene names
Name: ALPP
Synonyms: PLAP
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length535 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 + H(2)O = 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.

Polymorphism

Placental ALP is highly polymorphic, there are at least three common alleles.

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
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
   LigandMagnesium
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMGPI-anchor
Glycoprotein
Lipoprotein
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Cellular componentcell surface

Inferred from direct assay. Source: UniProtKB

   Molecular functionalkaline phosphatase activity Ref.1

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 506484Alkaline phosphatase, placental type
PRO_0000024031
Propeptide507 – 53529Removed in mature form
PRO_0000024032

Regions

Transmembrane513 – 52917

Sites

Active site1141Phosphoserine intermediate
Metal binding641Magnesium Potential
Metal binding641Zinc 2 Potential
Metal binding3331Magnesium Potential
Metal binding3381Zinc 1 Potential
Metal binding3421Zinc 1 Potential
Metal binding3791Zinc 2 Potential
Metal binding3801Zinc 2 Potential
Metal binding4541Zinc 1 Potential

Amino acid modifications

Lipidation5061GPI-anchor amidated aspartate
Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Disulfide bond143 ↔ 205
Disulfide bond489 ↔ 496

Natural variations

Natural variant251P → L: dbSNP rs1130335.
VAR_017419

Experimental info

Sequence conflict661M → V in AAA51709. Ref.3
Sequence conflict891I → L in AAH09647. Ref.5
Sequence conflict2311R → P in AAC97139. Ref.2
Sequence conflict261 – 2622AK → GE in AAA51706. Ref.6
Sequence conflict2631R → H in AAA51709. Ref.3
Sequence conflict2771Q → R in AAA51709. Ref.3
Sequence conflict2851T → A in AAA51709. Ref.3
Sequence conflict3241N → H in AAA51706. Ref.6
Sequence conflict3891Y → C in AAA51709. Ref.3
Sequence conflict3941S → G in AAA51709. Ref.3
Sequence conflict396 – 3972IF → FI in AAA51706. Ref.6
Sequence conflict4011P → A in AAA51706. Ref.6
Sequence conflict4361S → T Ref.8

Secondary structure

................................................................................... 535
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05187-1 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 13C136679A70C76B

FASTA53557,954
        10         20         30         40         50         60 
MLGPCMLLLL LLLGLRLQLS LGIIPVEEEN PDFWNREAAE ALGAAKKLQP AQTAAKNLII 

        70         80         90        100        110        120 
FLGDGMGVST VTAARILKGQ KKDKLGPEIP LAMDRFPYVA LSKTYNVDKH VPDSGATATA 

       130        140        150        160        170        180 
YLCGVKGNFQ TIGLSAAARF NQCNTTRGNE VISVMNRAKK AGKSVGVVTT TRVQHASPAG 

       190        200        210        220        230        240 
TYAHTVNRNW YSDADVPASA RQEGCQDIAT QLISNMDIDV ILGGGRKYMF RMGTPDPEYP 

       250        260        270        280        290        300 
DDYSQGGTRL DGKNLVQEWL AKRQGARYVW NRTELMQASL DPSVTHLMGL FEPGDMKYEI 

       310        320        330        340        350        360 
HRDSTLDPSL MEMTEAALRL LSRNPRGFFL FVEGGRIDHG HHESRAYRAL TETIMFDDAI 

       370        380        390        400        410        420 
ERAGQLTSEE DTLSLVTADH SHVFSFGGYP LRGSSIFGLA PGKARDRKAY TVLLYGNGPG 

       430        440        450        460        470        480 
YVLKDGARPD VTESESGSPE YRQQSAVPLD EETHAGEDVA VFARGPQAHL VHGVQEQTFI 

       490        500        510        520        530 
AHVMAFAACL EPYTACDLAP PAGTTDAAHP GRSVVPALLP LLAGTLLLLE TATAP 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution."
Knoll B.J., Rothblum K.N., Longley M.A.
J. Biol. Chem. 263:12020-12027(1988) [PubMed: 3042787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular cloning and sequence analysis of human placental alkaline phosphatase."
Millan J.L.
J. Biol. Chem. 261:3112-3115(1986) [PubMed: 3512548] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids."
Henthorn P.S., Knoll B.J., Raducha M., Rothblum K.N., Slaughter C., Weiss M., Lafferty M.A., Fischer T., Harris H.
Proc. Natl. Acad. Sci. U.S.A. 83:5597-5601(1986) [PubMed: 3461452] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT LEU-25.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S