ID A0A182GW59_AEDAL Unreviewed; 555 AA.
AC A0A182GW59;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Alkaline phosphatase {ECO:0000256|ARBA:ARBA00012647, ECO:0000256|RuleBase:RU003947};
DE EC=3.1.3.1 {ECO:0000256|ARBA:ARBA00012647, ECO:0000256|RuleBase:RU003947};
GN ORFNames=RP20_CCG016851 {ECO:0000313|EMBL:KXJ72944.1};
OS Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7160 {ECO:0000313|EMBL:KXJ72944.1};
RN [1] {ECO:0000313|EMBL:KXJ72944.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ72944.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ72944.1};
RX PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA Yan G., Tu Z.J., Fang X., James A.A.;
RT "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT insights into its biology, genetics, and evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN [2] {ECO:0000313|EMBL:KXJ72944.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ72944.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ72944.1};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000256|RuleBase:RU003947};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ564002; KXJ72944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182GW59; -.
DR VEuPathDB; VectorBase:AALC636_034501; -.
DR VEuPathDB; VectorBase:AALF016851; -.
DR VEuPathDB; VectorBase:AALFPA_062902; -.
DR Proteomes; UP000249989; Unassembled WGS sequence.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|RuleBase:RU003947};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR601952-2};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000249989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT ACT_SITE 129
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 479
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 555 AA; 60735 MW; CAE3EDE7C9CB0AA0 CRC64;
MRAAGILFAN ILVAVVATNE VHQTYDNDHQ HQRSSPASSR QAVNVDPAEL QSDFWRQMAQ
ETLKAKLQEE PIASKAKNVI YFIADGMSSQ TIAATRMYLG NENKMLSFEQ FPYLATAKTY
CVNRQVADSA CTATAYLSGV KTNYGMINVG PHVPRYNCVY NRTDSEFFGL LKWAQDSGMA
TGVVTNARIT HATPAGAYAS VANRDWEDDS AVTSGGCDAT KYPDVAHQLV HGEVGKKLNV
ALGGGRRHFV PKTQLDDESV AGYRSDGRNL IDEWKAVHPN NAAYVWNKTA LQSIDVASTE
NVLGLFDTGH IQFNLEIDEL QLGAVKPKLT EMVDAALKML TKNKDKGYFL FVEGARIDMA
HHDSRPRLAL DETAEFSRAI ELARATTSVE DTLIVVSSDH GHTMTYNGYP KRGNDILGIG
GVSDEDGLPY TTLSYANGEG YYTTYKQENP AERADISGYD FTDYHTLYMA TVPLDTESHG
GEDVAVFASG PMGHIFRGNM EQNVLPDLIA YAARIGQYKE DGGQDGEPGS AHATTVCIQL
MVVCGMSALL SQLKW
//
