ID   MLEC_RAT                Reviewed;         291 AA.
AC   Q5FVQ4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Malectin {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Mlec {ECO:0000312|RGD:1307736};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:Q14165}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the malectin family. {ECO:0000305}.
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; BC089839; AAH89839.1; -; mRNA.
DR   RefSeq; NP_001014005.1; NM_001013983.1.
DR   AlphaFoldDB; Q5FVQ4; -.
DR   SMR; Q5FVQ4; -.
DR   BioGRID; 257900; 1.
DR   IntAct; Q5FVQ4; 1.
DR   STRING; 10116.ENSRNOP00000035497; -.
DR   CAZy; CBM57; Carbohydrate-Binding Module Family 57.
DR   GlyGen; Q5FVQ4; 1 site.
DR   iPTMnet; Q5FVQ4; -.
DR   PhosphoSitePlus; Q5FVQ4; -.
DR   SwissPalm; Q5FVQ4; -.
DR   jPOST; Q5FVQ4; -.
DR   PaxDb; Q5FVQ4; -.
DR   PRIDE; Q5FVQ4; -.
DR   Ensembl; ENSRNOT00000038395; ENSRNOP00000035497; ENSRNOG00000064601.
DR   GeneID; 304543; -.
DR   KEGG; rno:304543; -.
DR   UCSC; RGD:1307736; rat.
DR   CTD; 9761; -.
DR   RGD; 1307736; Mlec.
DR   eggNOG; KOG3593; Eukaryota.
DR   GeneTree; ENSGT00390000016504; -.
DR   HOGENOM; CLU_065446_1_0_1; -.
DR   InParanoid; Q5FVQ4; -.
DR   OrthoDB; 1057965at2759; -.
DR   PhylomeDB; Q5FVQ4; -.
DR   TreeFam; TF314856; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q5FVQ4; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000021725; Expressed in jejunum and 19 other tissues.
DR   ExpressionAtlas; Q5FVQ4; baseline and differential.
DR   Genevisible; Q5FVQ4; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; ISO:RGD.
DR   GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006487; P:protein N-linked glycosylation; ISO:RGD.
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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..291
FT                   /note="Malectin"
FT                   /id="PRO_0000013984"
FT   TOPO_DOM        31..268
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          220..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         81
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   291 AA;  32418 MW;  11FA9277048361BC CRC64;
     MLKPRAAEGA AVALLRLLLL LLLLPPELRD RGLGVAGAAG AGLPESVIWA VNAGGEAHVD
     VHGIHFRKDP LEGRVGRASD YGMKLPILRS TPEDQILYQT ERYNEETFGY EVPVKEEGDY
     VLVLKFAEVY FAQSQQKVFD VRLNGHVVVK DLDIFDRVGH STAHDEIIPM SIRKGKLSVQ
     GEVSTFTGKL YIEFVKGYYD NPKVCALYIM AGTVDDVPKL QPHPGLEKKE EEEEEEEYDE
     GSNLKRQTNK NRVQSGPRTP NPYASDNSSL MFPILVAFGV FIPTLFCLCR L