MALT_CULPI
ID MALT_CULPI Reviewed; 580 AA.
AC Q95WY5;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Alpha-glucosidase {ECO:0000303|PubMed:11483434};
DE EC=3.2.1.20 {ECO:0000305|PubMed:11483434};
DE AltName: Full=Binary toxin-binding alpha-glucosidase {ECO:0000303|PubMed:11483434};
DE AltName: Full=Culex pipiens maltase 1 {ECO:0000303|Ref.2};
DE Short=Cpm1 {ECO:0000303|Ref.2};
DE Flags: Precursor;
GN Name=CPM1 {ECO:0000303|Ref.2};
OS Culex pipiens (House mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7175;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS AN ALPHA-GLUCOSIDASE, FUNCTION AS
RP BINB TOXIN RECEPTOR (MICROBIAL INFECTION), AND INTERACTION WITH
RP LYSINIBACILLUS SPHAERICUS BINB (MICROBIAL INFECTION).
RC STRAIN=IP;
RX PubMed=11483434; DOI=10.1016/s0965-1748(01)00046-7;
RA Darboux I., Nielsen-LeRoux C., Charles J.F., Pauron D.;
RT "The receptor of Bacillus sphaericus binary toxin in Culex pipiens
RT (Diptera: Culicidae) midgut: molecular cloning and expression.";
RL Insect Biochem. Mol. Biol. 31:981-990(2001).
RN [2]
RP PROTEIN SEQUENCE OF 30-44; 64-80 AND 85-99, FUNCTION AS BINB TOXIN RECEPTOR
RP (MICROBIAL INFECTION), INTERACTION WITH LYSINIBACILLUS SPHAERICUS BINB
RP (MICROBIAL INFECTION), AND DEVELOPMENTAL STAGE.
RC STRAIN=IP;
RA Silva-Filha M.H., Nielsen-LeRoux C., Charles J.F.;
RT "Identification of the receptor for Bacillus sphaericus crystal toxin in
RT the brush border membrane of the mosquito Culex pipiens (Diptera:
RT Culicidae).";
RL Insect Biochem. Mol. Biol. 29:711-721(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF GEO MUTANT, MECHANISM OF RESISTANCE TO
RP L.SPHAERICUS (MICROBIAL INFECTION), AND DEVELOPMENTAL STAGE.
RC STRAIN=GEO, and IP;
RX PubMed=11983886; DOI=10.1073/pnas.092615399;
RA Darboux I., Pauchet Y., Castella C., Silva-Filha M.H., Nielsen-LeRoux C.,
RA Charles J.F., Pauron D.;
RT "Loss of the membrane anchor of the target receptor is a mechanism of
RT bioinsecticide resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5830-5835(2002).
CC -!- FUNCTION: Probably an alpha-glucosidase, it has no alpha-amylase
CC function. {ECO:0000305|Ref.2}.
CC -!- FUNCTION: (Microbial infection) Serves as the larval receptor for
CC Lysinibacillus sphaericus BinB toxin (Ref.2). {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC Evidence={ECO:0000305|PubMed:11483434};
CC -!- SUBUNIT: (Microbial infection) Binds to L.sphaericus BinB subunit of
CC the binary toxin BinAB. {ECO:0000269|PubMed:11483434,
CC ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In 4th-instar larvae produced in the brush border
CC membranes of the gastric caeca and the posterior stomach cells (at
CC protein level). {ECO:0000269|PubMed:11983886}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 4th-instar larval midgut, in the
CC brush border membranes of the gastric cesum and the posterior stomach
CC cells (at protein level). {ECO:0000269|PubMed:11483434,
CC ECO:0000269|PubMed:11983886, ECO:0000269|Ref.2}.
CC -!- POLYMORPHISM: In mosquito strain GEO, which is 10(5)-fold more
CC resistant to L.sphaericus than wild-type, a premature stop codon at
CC Leu-569 leads to loss of the probable GPI anchor and disrupts the
CC correct subcellular location. Restoration of Leu-269 rescues the
CC subcellular location and binary Bin toxin binding to transfected Sf9
CC cells in culture (PubMed:11983886). {ECO:0000269|PubMed:11983886}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AF222024; AAL05443.1; -; mRNA.
DR AlphaFoldDB; Q95WY5; -.
DR SMR; Q95WY5; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..580
FT /note="Alpha-glucosidase"
FT /evidence="ECO:0000255"
FT /id="PRO_5004321121"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 224
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT ACT_SITE 290
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A0R6E0"
FT SITE 358
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 95
FT /note="A -> D (in strain: GEO)"
FT /evidence="ECO:0000269|PubMed:11983886"
FT VARIANT 115
FT /note="K -> M (in strain: GEO)"
FT /evidence="ECO:0000269|PubMed:11983886"
FT VARIANT 178
FT /note="A -> T (in strain: GEO)"
FT /evidence="ECO:0000269|PubMed:11983886"
FT VARIANT 230
FT /note="F -> H (in strain: GEO)"
FT /evidence="ECO:0000269|PubMed:11983886"
FT VARIANT 265
FT /note="N -> D (in strain: GEO)"
FT /evidence="ECO:0000269|PubMed:11983886"
FT VARIANT 486
FT /note="L -> M (in strain: GEO)"
FT /evidence="ECO:0000269|PubMed:11983886"
FT VARIANT 569..580
FT /note="Missing (in strain: GEO)"
FT /evidence="ECO:0000269|PubMed:11983886"
SQ SEQUENCE 580 AA; 66121 MW; 38E33CA5EDFC6657 CRC64;
MRPLGALSLF ALLATTVSGL AIREPDAKDW YQHATFYQIY PRSFLDSNGD GIGDLAGITS
KMKYLADIGI DATWLSPPFK SPLKDFGYDV SDFYAIQPEY GNLTDFDKLV EEAHKNGIKL
MLDFIPNHSS DQHEWFVKSV ARDPEYSEFY VWKPPATGGG PPNNWISVFG GPAWTYNAAR
GEYYLHQFTP QQPDLNYRNP KLLAEMTKML FFWLDRGVDG FRLDAINHMF EDEQFRDEPV
SGWGQPGEYD SLDHIYTKDI PDVYNVVYNW RDQMDKYSAE KGRTIILMTE AYSSIEGTML
YYESADRKRQ GAHMPFNFQL IYDFKKEQNA VGLKSSIDWW MNNMPARHTP SWVAGSHDHS
RVASRVGLDR VDQVMTLMHT LPGTSITYYG EEVAMQDFKE AQQFDNRDPN RTPMQWDSST
SAGFSTNTNT WLRVHPDYAR YNVDVMQKNP QSTFHHFQHL TKLRGHRTMQ SGEYVHKTVG
TKVYALLREL RGEDSFLTVL NMAGAEDTVD LGDFVNLPQK MRVEVAQPNS KSKAGNEVDI
SKLTLGPYDS VVLRATVSSA AAINLSIGLL LAIMARYIFV
