ID   MLECB_XENLA             Reviewed;         276 AA.
AC   Q8AVF4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Malectin-B {ECO:0000250|UniProtKB:Q6INX3};
DE   Flags: Precursor;
GN   Name=mlec-b {ECO:0000250|UniProtKB:Q6INX3};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:AAH42341.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH42341.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Carbohydrate-binding protein with a strong ligand preference
CC       for Glc2-N-glycan. May play a role in the early steps of protein N-
CC       glycosylation. Can bind di- or higher oligomers but not monomers of
CC       glucose, including maltose, maltotriose, maltotetraose, maltoheptaose,
CC       nigerose, kojibose, cellobiose and isomaltose, although based on their
CC       subcellular locations, these are unlikely to all be physiological
CC       ligands (By similarity). {ECO:0000250|UniProtKB:Q6INX3}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q6INX3, ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000250|UniProtKB:Q6INX3, ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the malectin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH42341.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC042341; AAH42341.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001080532.1; NM_001087063.1.
DR   RefSeq; XP_018124265.1; XM_018268776.1.
DR   AlphaFoldDB; Q8AVF4; -.
DR   SMR; Q8AVF4; -.
DR   DNASU; 380224; -.
DR   GeneID; 380224; -.
DR   KEGG; xla:380224; -.
DR   CTD; 380224; -.
DR   Xenbase; XB-GENE-6253921; mlec.L.
DR   OMA; LCMAMRR; -.
DR   OrthoDB; 1057965at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 380224; Expressed in pancreas and 19 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR021720; Malectin_dom.
DR   InterPro; IPR039155; MLEC.
DR   PANTHER; PTHR13460; PTHR13460; 1.
DR   Pfam; PF11721; Malectin; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Endoplasmic reticulum; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..276
FT                   /note="Malectin-B"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000358591"
FT   TOPO_DOM        27..253
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          202..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         67
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q6INX3"
FT   BINDING         89
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q6INX3"
FT   BINDING         116
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q6INX3"
FT   BINDING         117
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q6INX3"
FT   BINDING         186
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q6INX3"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   276 AA;  30673 MW;  D5F5C3EF5D9970F1 CRC64;
     MLSIRTVLGP LAAILLTVIG PFGAHGSGLA DKVMWAVNAG GESHVDVHGI HYRKDPLEGR
     VGRASDYGMK LPILRSNPED QVLYQTERYN EDSFGYDIPI KEEGEYVIVL KFAEVYFAQS
     QQKVFDIRVN GHTVVKDLDI FDRVGHSTAH DEIIPISIKK GKLSVQGEVS TFTGKLSVEF
     VKGYYDNPKV CALYIMKGTA DDVPQLQPHP GLEKKEEEEE EEEEEGSPSK KQSNKNRVQS
     GPRTPNPYAS DNSSLMFPIL VAFGVFIPTL FCLCRL