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Alkaline phosphatase, placental-like (EC 3.1.3.1) (ALP-1) (Alkaline phosphatase Nagao isozyme) (Germ cell alkaline phosphatase) (GCAP) (Placental alkaline phosphatase-like) (PLAP-like)

 PPBN_HUMAN              Reviewed;         532 AA.
P10696; A8KAF2; Q16727; Q53S81; Q96CM1;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 4.
27-SEP-2017, entry version 174.
RecName: Full=Alkaline phosphatase, placental-like;
EC=3.1.3.1;
AltName: Full=ALP-1;
AltName: Full=Alkaline phosphatase Nagao isozyme;
AltName: Full=Germ cell alkaline phosphatase;
Short=GCAP;
AltName: Full=Placental alkaline phosphatase-like;
Short=PLAP-like;
Flags: Precursor;
Name=ALPPL2; Synonyms=ALPPL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2834730; DOI=10.1073/pnas.85.9.3024;
Millan J.L., Manes T.;
"Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline
phosphatase gene.";
Proc. Natl. Acad. Sci. U.S.A. 85:3024-3028(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Choriocarcinoma;
PubMed=2745460;
Watanabe S., Watanabe T., Li W.L., Soong B.-W., Chou J.Y.;
"Expression of the germ cell alkaline phosphatase gene in human
choriocarcinoma cells.";
J. Biol. Chem. 264:12611-12619(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS MET-273 AND ARG-316.
TISSUE=Colon;
PubMed=2297757;
Gum J.R. Jr., Hicks J.W., Sack T.L., Kim Y.S.;
"Molecular cloning of complementary DNAs encoding alkaline phosphatase
in human colon cancer cells.";
Cancer Res. 50:1085-1091(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-316.
PubMed=2162249;
Lowe M.E., Strauss A.W.;
"Expression of a Nagao-type, phosphatidylinositol-glycan anchored
alkaline phosphatase in human choriocarcinomas.";
Cancer Res. 50:3956-3962(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-316.
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-316.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-273 AND
ARG-316.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
PubMed=3443302; DOI=10.1016/0378-1119(87)90235-6;
Knoll B.J., Rothblum K.N., Longley M.;
"Two gene duplication events in the evolution of the human heat-stable
alkaline phosphatases.";
Gene 60:267-276(1987).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-157.
PubMed=3387245; DOI=10.1093/nar/16.12.5694;
Shen L.P., Liu H., Kan Y.W., Kam W.;
"5' nucleotide sequence of a putative human placental alkaline
phosphatase-like gene.";
Nucleic Acids Res. 16:5694-5694(1988).
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 1 Mg(2+) ion. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions. {ECO:0000250};
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
-!- TISSUE SPECIFICITY: Trace amounts in the testis and thymus, and in
elevated amounts in germ cell tumors.
-!- MISCELLANEOUS: In most mammals there are four different isozymes:
placental, placental-like, intestinal and tissue non-specific
(liver/bone/kidney).
-!- SIMILARITY: Belongs to the alkaline phosphatase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA30232.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; J03252; AAA98616.1; -; Genomic_DNA.
EMBL; J04948; AAA51700.1; -; mRNA.
EMBL; X53279; CAA37374.1; -; mRNA.
EMBL; X55958; CAA39425.1; -; mRNA.
EMBL; AK293017; BAF85706.1; -; mRNA.
EMBL; AC068134; AAY24088.1; -; Genomic_DNA.
EMBL; CH471063; EAW70994.1; -; Genomic_DNA.
EMBL; BC014139; AAH14139.1; -; mRNA.
EMBL; M19160; AAA51707.1; -; Genomic_DNA.
EMBL; X07247; CAA30232.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS2491.1; -.
PIR; S12076; S12076.
RefSeq; NP_112603.2; NM_031313.2.
UniGene; Hs.333509; -.
ProteinModelPortal; P10696; -.
SMR; P10696; -.
BioGrid; 106752; 9.
IntAct; P10696; 2.
STRING; 9606.ENSP00000295453; -.
BindingDB; P10696; -.
ChEMBL; CHEMBL3402; -.
DrugBank; DB01143; Amifostine.
DrugBank; DB00848; Levamisole.
DrugBank; DB09322; Zinc sulfate.
DEPOD; P10696; -.
iPTMnet; P10696; -.
PhosphoSitePlus; P10696; -.
BioMuta; ALPPL2; -.
DMDM; 145559564; -.
MaxQB; P10696; -.
PaxDb; P10696; -.
PeptideAtlas; P10696; -.
PRIDE; P10696; -.
Ensembl; ENST00000295453; ENSP00000295453; ENSG00000163286.
GeneID; 251; -.
KEGG; hsa:251; -.
UCSC; uc002vss.5; human.
CTD; 251; -.
DisGeNET; 251; -.
EuPathDB; HostDB:ENSG00000163286.7; -.
GeneCards; ALPPL2; -.
HGNC; HGNC:441; ALPPL2.
HPA; CAB020698; -.
HPA; HPA038764; -.
HPA; HPA038765; -.
HPA; HPA051699; -.
MIM; 171810; gene.
neXtProt; NX_P10696; -.
OpenTargets; ENSG00000163286; -.
PharmGKB; PA24731; -.
eggNOG; KOG4126; Eukaryota.
eggNOG; COG1785; LUCA.
GeneTree; ENSGT00390000008704; -.
HOGENOM; HOG000099118; -.
HOVERGEN; HBG007345; -.
InParanoid; P10696; -.
KO; K01077; -.
OMA; MKNKDFM; -.
OrthoDB; EOG091G067H; -.
PhylomeDB; P10696; -.
TreeFam; TF323513; -.
Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
GenomeRNAi; 251; -.
PRO; PR:P10696; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163286; -.
CleanEx; HS_ALPPL2; -.
Genevisible; P10696; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0004035; F:alkaline phosphatase activity; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006501; P:C-terminal protein lipidation; TAS:Reactome.
CDD; cd16012; ALP; 1.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR001952; Alkaline_phosphatase.
InterPro; IPR018299; Alkaline_phosphatase_AS.
InterPro; IPR017850; Alkaline_phosphatase_core.
PANTHER; PTHR11596; PTHR11596; 1.
Pfam; PF00245; Alk_phosphatase; 1.
PRINTS; PR00113; ALKPHPHTASE.
SMART; SM00098; alkPPc; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
GPI-anchor; Hydrolase; Lipoprotein; Magnesium; Membrane;
Metal-binding; Polymorphism; Reference proteome; Signal; Zinc.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 503 Alkaline phosphatase, placental-like.
/FTId=PRO_0000024033.
PROPEP 504 532 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000024034.
ACT_SITE 111 111 Phosphoserine intermediate.
METAL 61 61 Magnesium. {ECO:0000250}.
METAL 61 61 Zinc 1. {ECO:0000250}.
METAL 111 111 Zinc 1. {ECO:0000250}.
METAL 174 174 Magnesium. {ECO:0000250}.
METAL 330 330 Magnesium. {ECO:0000250}.
METAL 335 335 Zinc 2. {ECO:0000250}.
METAL 339 339 Zinc 2; via tele nitrogen. {ECO:0000250}.
METAL 376 376 Zinc 1. {ECO:0000250}.
METAL 377 377 Zinc 1; via tele nitrogen. {ECO:0000250}.
METAL 451 451 Zinc 2; via tele nitrogen. {ECO:0000250}.
LIPID 503 503 GPI-anchor amidated aspartate.
{ECO:0000250}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 140 202 {ECO:0000250}.
DISULFID 486 493 {ECO:0000250}.
VARIANT 273 273 L -> M (in dbSNP:rs17416141).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2297757}.
/FTId=VAR_027553.
VARIANT 316 316 L -> R (in dbSNP:rs183793479).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2162249,
ECO:0000269|PubMed:2297757,
ECO:0000269|Ref.7}.
/FTId=VAR_027554.
VARIANT 527 527 G -> E (in dbSNP:rs1048999).
/FTId=VAR_027555.
CONFLICT 57 57 I -> M (in Ref. 1; AAA98616).
{ECO:0000305}.
CONFLICT 152 152 M -> V (in Ref. 1; AAA98616 and 4;
CAA39425). {ECO:0000305}.
CONFLICT 178 178 A -> T (in Ref. 1; AAA98616, 2; AAA51700
and 4; CAA39425). {ECO:0000305}.
CONFLICT 260 260 H -> R (in Ref. 8; AAH14139).
{ECO:0000305}.
CONFLICT 380 380 V -> L (in Ref. 2; AAA51700).
{ECO:0000305}.
CONFLICT 498 498 R -> P (in Ref. 1; AAA98616 and 4;
CAA39425). {ECO:0000305}.
CONFLICT 498 498 R -> S (in Ref. 3; CAA37374).
{ECO:0000305}.
CONFLICT 531 531 A -> T (in Ref. 3; CAA37374).
{ECO:0000305}.
SEQUENCE 532 AA; 57377 MW; 25EB56C901B61505 CRC64;
MQGPWVLLLL GLRLQLSLGI IPVEEENPDF WNRQAAEALG AAKKLQPAQT AAKNLIIFLG
DGMGVSTVTA ARILKGQKKD KLGPETFLAM DRFPYVALSK TYSVDKHVPD SGATATAYLC
GVKGNFQTIG LSAAARFNQC NTTRGNEVIS VMNRAKKAGK SVGVVTTTRV QHASPAGAYA
HTVNRNWYSD ADVPASARQE GCQDIATQLI SNMDIDVILG GGRKYMFPMG TPDPEYPDDY
SQGGTRLDGK NLVQEWLAKH QGARYVWNRT ELLQASLDPS VTHLMGLFEP GDMKYEIHRD
STLDPSLMEM TEAALLLLSR NPRGFFLFVE GGRIDHGHHE SRAYRALTET IMFDDAIERA
GQLTSEEDTL SLVTADHSHV FSFGGYPLRG SSIFGLAPGK ARDRKAYTVL LYGNGPGYVL
KDGARPDVTE SESGSPEYRQ QSAVPLDGET HAGEDVAVFA RGPQAHLVHG VQEQTFIAHV
MAFAACLEPY TACDLAPRAG TTDAAHPGPS VVPALLPLLA GTLLLLGTAT AP


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