PPB_BOMMO
ID PPB_BOMMO Reviewed; 550 AA.
AC P29523; Q966T9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 4.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Membrane-bound alkaline phosphatase;
DE Short=M-ALP;
DE EC=3.1.3.1;
DE Flags: Precursor;
GN Name=Alp-m;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 40-46.
RC STRAIN=Aojuku; TISSUE=Midgut;
RX PubMed=1756175; DOI=10.1016/0167-4781(91)90229-f;
RA Itoh M., Takeda S., Yamamoto H., Izumi S., Tomino S., Eguchi M.;
RT "Cloning and sequence analysis of membrane-bound alkaline phosphatase cDNA
RT of the silkworm, Bombyx mori.";
RL Biochim. Biophys. Acta 1129:135-138(1991).
RN [2]
RP SEQUENCE REVISION TO 151 AND N-TERMINUS.
RA Itoh M., Takeda S., Yamamoto H., Izumi S., Tomino S., Eguchi M.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Aojuku; TISSUE=Midgut;
RX PubMed=14508679; DOI=10.1007/s00438-003-0880-9;
RA Itoh M., Inoue T., Kanamori Y., Nishida S., Yamaguchi M.;
RT "Tandem duplication of alkaline phosphatase genes and polymorphism in the
RT intergenic sequence in Bombyx mori.";
RL Mol. Genet. Genomics 270:114-120(2003).
RN [4]
RP SEQUENCE REVISION TO 59; 151; 439 AND N-TERMINUS.
RA Itoh M., Inoue T., Kanamori Y., Nishida S., Yamaguchi M.;
RL Submitted (JAN-2013) 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:0000255|PROSITE-ProRule:PRU10042};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Midgut.
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR EMBL; D90454; BAA14420.4; -; mRNA.
DR EMBL; AB055428; BAB62745.3; -; Genomic_DNA.
DR PIR; S19607; S19607.
DR RefSeq; NP_001037536.3; NM_001044071.3.
DR AlphaFoldDB; P29523; -.
DR SMR; P29523; -.
DR STRING; 7091.BGIBMGA008818-TA; -.
DR GeneID; 693074; -.
DR KEGG; bmor:693074; -.
DR CTD; 693074; -.
DR eggNOG; KOG4126; Eukaryota.
DR HOGENOM; CLU_008539_4_0_1; -.
DR InParanoid; P29523; -.
DR OrthoDB; 454880at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; -; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; PTHR11596; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..39
FT /evidence="ECO:0000269|PubMed:1756175"
FT CHAIN 40..524
FT /note="Membrane-bound alkaline phosphatase"
FT /id="PRO_0000024047"
FT PROPEP 525..550
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024048"
FT ACT_SITE 133
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT LIPID 524
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 550 AA; 60281 MW; D28C778B538EC96B CRC64;
MSTWWLVVVA AAAAAGLVRA EDRYHPERLA AGEASAATRS AAESEASFWV REAQEAIERR
EREGAGAKQA AGHAKNVVMF LGDGMSVPTL AAARTLLGQR RGQTGEEASL HFEQFPTLGL
AKTYCVNAQV PDSSCTATAY LCGVKANQGT LGVTAAVPRH DCEASTDVTK RVQSIAEWAL
ADGRDVGIVT TTRITHASPA GTFAKVANRN WENDNDVKQE GHDVNRCPDI AHQLIKMAPG
NKFKVIFGGG RREFLPTTQV DEEGTRGLRT DGRNLIEEWQ NDKESQKVSY KYLWNRQELL
KLGSSPPDYL LGLFEGSHLQ YHLEGDESTE PTLAELTDVA IRVLSRNERG FFLFVEGGRI
DHAHHDNYAH LALDETIEMD RAVKVATDAL KEDESLVVVT ADHTHVMSFN GYSPRGTDVL
GTVRSLDSNR MPFMVLSYTN GPGARIQQNG VRPDVTTDAN FGALRWRTHT DVPLDSETHG
GDDVTVFAWG VHHWMFSGLY EQTHVPHRMA WAACMGPGRH VCVSAATVPT AALLSLLLAA
FITLRHQCFL
