MLECA_XENLA
ID MLECA_XENLA Reviewed; 276 AA.
AC Q6INX3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Malectin-A {ECO:0000250|UniProtKB:Q14165};
DE Flags: Precursor;
GN Name=mlec-a {ECO:0000250|UniProtKB:Q14165};
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], STRUCTURE BY NMR OF 27-213 IN COMPLEX WITH
RP NIGEROSE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Pancreas {ECO:0000269|PubMed:18524852};
RX PubMed=18524852; DOI=10.1091/mbc.e08-04-0354;
RA Schallus T., Jaeckh C., Feher K., Palma A.S., Liu Y., Simpson J.C.,
RA Mackeen M., Stier G., Gibson T.J., Feizi T., Pieler T., Muhle-Goll C.;
RT "Malectin: a novel carbohydrate-binding protein of the endoplasmic
RT reticulum and a candidate player in the early steps of protein N-
RT glycosylation.";
RL Mol. Biol. Cell 19:3404-3414(2008).
RN [2] {ECO:0000312|EMBL:AAH72149.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH72149.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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. {ECO:0000269|PubMed:18524852}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18524852}; Single-pass type I membrane protein
CC {ECO:0000255, ECO:0000269|PubMed:18524852}.
CC -!- TISSUE SPECIFICITY: Widely expressed throughout development including
CC the anterior neuroectoderm and neural crest at stages 18 and 20, and
CC the retina, hatching gland, otic vesicle, epibranchial placodes,
CC pronephros and tail tip of later states. At stage 41, expressed in the
CC liver, pancreas, branchial arches and proctodeum. Expressed broadly in
CC adults in fat, intestine, gall bladder, eye, muscle, kidney, stomach,
CC liver, heart, pancreas and lung. {ECO:0000269|PubMed:18524852}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:18524852}.
CC -!- SIMILARITY: Belongs to the malectin family. {ECO:0000305}.
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DR EMBL; BC072149; AAH72149.1; -; mRNA.
DR RefSeq; NP_001085212.1; NM_001091743.1.
DR PDB; 2JWP; NMR; -; A=28-201.
DR PDB; 2K46; NMR; -; A=27-213.
DR PDB; 2KR2; NMR; -; A=27-213.
DR PDBsum; 2JWP; -.
DR PDBsum; 2K46; -.
DR PDBsum; 2KR2; -.
DR AlphaFoldDB; Q6INX3; -.
DR SMR; Q6INX3; -.
DR CAZy; CBM57; Carbohydrate-Binding Module Family 57.
DR UniLectin; Q6INX3; -.
DR DNASU; 432306; -.
DR GeneID; 432306; -.
DR KEGG; xla:432306; -.
DR CTD; 432306; -.
DR Xenbase; XB-GENE-5734882; mlec.S.
DR OMA; PNPYSMD; -.
DR OrthoDB; 1057965at2759; -.
DR EvolutionaryTrace; Q6INX3; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 432306; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IC:UniProtKB.
DR InterPro; IPR021720; Malectin_dom.
DR InterPro; IPR039155; MLEC.
DR PANTHER; PTHR13460; PTHR13460; 1.
DR Pfam; PF11721; Malectin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000305"
FT CHAIN 27..276
FT /note="Malectin-A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000358590"
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 204..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
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:0000269|PubMed:18524852"
FT BINDING 89
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:18524852"
FT BINDING 116
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:18524852"
FT BINDING 117
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:18524852"
FT BINDING 186
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:18524852"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2JWP"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2K46"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2JWP"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:2JWP"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:2JWP"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2JWP"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:2JWP"
SQ SEQUENCE 276 AA; 30688 MW; 9F3D37BF107E7F0A CRC64;
MLSIRTVLGP LATILLTVLG PFGAHGSGLA DKVIWAVNAG GESHVDVHGI HYRKDPLEGR
VGRASDYGMK LPILRSNPED QVLYQTERYN EDSFGYDIPI KEEGEYVLVL KFAEVYFAQS
QQKVFDVRVN GHTVVKDLDI FDRVGHSTAH DEIIPISIKK GKLSVQGEVS TFTGKLSVEF
VKGYYDNPKV CALFIMKGTA DDVPMLQPHP GLEKKEEEEE EEEEEGSTSK KQINKNRVQS
GPRTPNPYAS DNSSLMFPIL VAFGVFIPTL FCLCRL
