ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P05187


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PPB1_HUMAN
Primary accession number P05187
Secondary accession numbers P05188 P06861 Q53S78 Q96DB7
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on July 1, 1989 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 113)
Name and origin of the protein
Protein name Alkaline phosphatase, placental type [Precursor]
Synonyms EC 3.1.3.1
PLAP-1
Alkaline phosphatase Regan isozyme
Gene name
Name: ALPP
Synonyms: PLAP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3042787 [NCBI, ExPASy, EBI, Israel, Japan]
Knoll B.J., Rothblum K.N., Longley M.A.;
"Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution.";
J. Biol. Chem. 263:12020-12027(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3512548 [NCBI, ExPASy, EBI, Israel, Japan]
Millan J.L.;
"Molecular cloning and sequence analysis of human placental alkaline phosphatase.";
J. Biol. Chem. 261:3112-3115(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT LEU-25.
PubMed=3461452 [NCBI, ExPASy, EBI, Israel, Japan]
Henthorn P.S., Knoll B.J., Raducha M., Rothblum K.N., Slaughter C., Weiss M., Lafferty M.A., Fischer T., Harris H.;
"Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids.";
Proc. Natl. Acad. Sci. U.S.A. 83:5597-5601(1986).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-535, AND VARIANT LEU-25.
PubMed=3001717 [NCBI, ExPASy, EBI, Israel, Japan]
Kam W., Clauser E., Kim Y.S., Kan Y.W., Rutter W.J.;
"Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 82:8715-8719(1985).
[7]
PROTEIN SEQUENCE OF 23-64.
DOI=10.1016/S0006-291X(83)80252-6; PubMed=6651840 [NCBI, ExPASy, EBI, Israel, Japan]
Ezra E., Blacher R., Udenfriend S.;
"Purification and partial sequencing of human placental alkaline phosphatase.";
Biochem. Biophys. Res. Commun. 116:1076-1083(1983).
[8]
NUCLEOTIDE SEQUENCE OF 382-535.
PubMed=3459156 [NCBI, ExPASy, EBI, Israel, Japan]
Ovitt C.E., Strauss A.W., Alpers D.H., Chou J.Y., Boime I.;
"Expression of different-sized placental alkaline phosphatase mRNAs in placenta and choriocarcinoma cells.";
Proc. Natl. Acad. Sci. U.S.A. 83:3781-3785(1986).
[9]
PROTEIN SEQUENCE OF 485-535.
PubMed=3422741 [NCBI, ExPASy, EBI, Israel, Japan]
Micanovic R., Bailey C.A., Brink L., Gerber L., Pan Y.C.E., Hulmes J.D., Udenfriend S.;
"Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 85:1398-1402(1988).
[10]
GPI-ANCHOR AT ASP-506.
PubMed=2153284 [NCBI, ExPASy, EBI, Israel, Japan]
Micanovic R., Gerber L.D., Berger J., Kodukula K., Udenfriend S.;
"Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 87:157-161(1990).
[11]
EFFECT OF MUTAGENESIS OF C-TERMINAL PEPTIDE ON GPI-ANCHORING.
DOI=10.1083/jcb.116.3.799; PubMed=1730777 [NCBI, ExPASy, EBI, Israel, Japan]
Lowe M.E.;
"Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein.";
J. Cell Biol. 116:799-807(1992).
[12]
DISULFIDE BONDS.
DOI=10.1074/jbc.M202298200; PubMed=11937510 [NCBI, ExPASy, EBI, Israel, Japan]
Kozlenkov A., Manes T., Hoylaerts M.F., Millan J.L.;
"Function assignment to conserved residues in mammalian alkaline phosphatases.";
J. Biol. Chem. 277:22992-22999(2002).
[13]
X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 56-535.
DOI=10.1074/jbc.M009250200; PubMed=11124260 [NCBI, ExPASy, EBI, Israel, Japan]
Le Du M.H., Stigbrand T., Taussig M.J., Menez A., Stura E.A.;
"Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity.";
J. Biol. Chem. 276:9158-9165(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M19159; AAA51710.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M13077; AAC97139.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14169; AAA51708.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14170; AAA51709.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC068134; AAY24087.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009647; AAH09647.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC068501; AAH68501.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC094743; AAH94743.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12551; AAA51706.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A31074; PAHUA.
RefSeq NP_001623.3; -.
UniGene Hs.284255
3D structure databases
PDB
1EW2; X-ray; 1.82 A; A=23-535.[ExPASy / RCSB / EBI]
1ZEB; X-ray; 1.90 A; A=23-506.[ExPASy / RCSB / EBI]
1ZED; X-ray; 1.57 A; A=23-506.[ExPASy / RCSB / EBI]
1ZEF; X-ray; 1.90 A; A=23-506.[ExPASy / RCSB / EBI]
2GLQ; X-ray; 1.60 A; A=23-506.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EW2; -.
1ZEB; -.
1ZED; -.
1ZEF; -.
2GLQ; -.
ModBase P05187.
Organism-specific databases
H-InvDB HIX0002924; -.
HGNC HGNC:439; ALPP.
GenAtlas ALPP.
HPA CAB000067; -.
MIM 171800; gene. [NCBI / EBI]
PharmGKB PA24730; -.
GeneCards P05187.
Gene expression databases
ArrayExpress P05187; -.
CleanEx HS_ALPP; -.
GermOnline ENSG00000163283; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0004035; Molecular function: alkaline phosphatase activity (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR017849; Alkaline_Pase-like_a/b/a.
IPR001952; Alkaline_phosphatase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.720.10; Alk_phosphtse; 1.
Pfam PF00245; Alk_phosphatase; 1.
Pfam graphical view of domain structure.
PRINTS PR00113; ALKPHPHTASE.
SMART SM00098; alkPPc; 1.
SMART graphical view of domain structure.
PROSITE PS00123; ALKALINE_PHOSPHATASE; 1.
BLOCKS P05187.
ProtoNet P05187.
Genome annotation databases
Ensembl ENSG00000163283; Homo sapiens. [Contig view]
GeneID 250; -.
KEGG hsa:250; -.
NMPDR fig|9606.3.peg.19512; -.
Phylogenomic databases
HOGENOM P05187; -.
HOVERGEN P05187; -.
Other
NextBio 1001; -.
SOURCE ALPP; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Signal; Transmembrane; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    22  22      
CHAIN   23   506  484     Alkaline phosphatase, placental type. PRO_0000024031
PROPEP   507   535  29     Removed in mature form. PRO_0000024032
TRANSMEM   513   529  17      
ACT_SITE   114   114        Phosphoserine intermediate. 
METAL   64    64        Magnesium (Potential). 
METAL   64    64        Zinc 2 (Potential). 
METAL   333   333        Magnesium (Potential). 
METAL   338   338        Zinc 1 (Potential). 
METAL   342   342        Zinc 1 (Potential). 
METAL   379   379        Zinc 2 (Potential). 
METAL   380   380        Zinc 2 (Potential). 
METAL   454   454        Zinc 1 (Potential). 
LIPID   506   506        GPI-anchor amidated aspartate. 
CARBOHYD   144   144        N-linked (GlcNAc...) (Potential). 
CARBOHYD   271   271        N-linked (GlcNAc...) (Potential). 
DISULFID   143   205         
DISULFID   489   496         
VARIANT   25    25  1     P -> L (in dbSNP:rs1130335 [NCBI]). VAR_017419 
CONFLICT   66    66        M -> V (in Ref. 3; AAA51709). 
CONFLICT   89    89        I -> L (in Ref. 5; AAH09647). 
CONFLICT   231   231        R -> P (in Ref. 2; AAC97139). 
CONFLICT   261   262        AK -> GE (in Ref. 6; AAA51706). 
CONFLICT   263   263        R -> H (in Ref. 3; AAA51709). 
CONFLICT   277   277        Q -> R (in Ref. 3; AAA51709). 
CONFLICT   285   285        T -> A (in Ref. 3; AAA51709). 
CONFLICT   324   324        N -> H (in Ref. 6; AAA51706). 
CONFLICT   389   389        Y -> C (in Ref. 3; AAA51709). 
CONFLICT   394   394        S -> G (in Ref. 3; AAA51709). 
CONFLICT   396   397        IF -> FI (in Ref. 6; AAA51706). 
CONFLICT   401   401        P -> A (in Ref. 6; AAA51706). 
CONFLICT   436   436        S -> T (in Ref. 8). 
HELIX   26    29  4      
HELIX   31    47  17      
STRAND   56    63  8      
HELIX   68    81  14      
HELIX   92    95  4      
STRAND   97   103  7      
STRAND   107   111  5      
HELIX   114   123  10      
STRAND   132   134  3      
HELIX   143   145  3      
HELIX   154   160  7      
STRAND   164   172  9      
HELIX   176   179  4      
TURN   180   182  3      
HELIX   193   195  3      
HELIX   198   202  5      
HELIX   208   214  7      
STRAND   219   224  6      
HELIX   227   229  3      
HELIX   243   245  3      
STRAND   249   251  3      
HELIX   255   261  7      
STRAND   266   269  4      
HELIX   272   280  9      
STRAND   286   290  5      
STRAND   292   295  4      
HELIX   299   301  3      
TURN   304   306  3      
HELIX   310   321  12      
STRAND   328   334  7      
HELIX   337   342  6      
HELIX   346   366  21      
TURN   369   371  3      
STRAND   372   379  8      
STRAND   381   386  6      
STRAND   411   418  8      
HELIX   433   436  4      
STRAND   445   447  3      
STRAND   459   465  7      
HELIX   468   470  3      
STRAND   473   476  4      
HELIX   479   487  9      
Sequence information
Length: 535 AA [This is the length of the unprocessed precursor] Molecular weight: 57954 Da [This is the MW of the unprocessed precursor] CRC64: 13C136679A70C76B [This is a checksum on the sequence]
        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 

P05187 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!