ID   MLEC_DANRE              Reviewed;         285 AA.
AC   A9C3P0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Malectin {ECO:0000250|UniProtKB:Q14165};
DE   Flags: Precursor;
GN   Name=mlec {ECO:0000250|UniProtKB:Q14165}; ORFNames=si:dkey-117k10.5;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
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|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}.
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DR   EMBL; CR376731; CAP19582.1; -; Genomic_DNA.
DR   RefSeq; NP_001107090.1; NM_001113618.1.
DR   AlphaFoldDB; A9C3P0; -.
DR   SMR; A9C3P0; -.
DR   STRING; 7955.ENSDARP00000077503; -.
DR   CAZy; CBM57; Carbohydrate-Binding Module Family 57.
DR   PaxDb; A9C3P0; -.
DR   PeptideAtlas; A9C3P0; -.
DR   Ensembl; ENSDART00000131372; ENSDARP00000112772; ENSDARG00000059630.
DR   GeneID; 569613; -.
DR   KEGG; dre:569613; -.
DR   CTD; 9761; -.
DR   ZFIN; ZDB-GENE-081105-187; mlec.
DR   eggNOG; KOG3593; Eukaryota.
DR   GeneTree; ENSGT00390000016504; -.
DR   HOGENOM; CLU_065446_1_0_1; -.
DR   InParanoid; A9C3P0; -.
DR   OMA; LCMAMRR; -.
DR   OrthoDB; 1057965at2759; -.
DR   PhylomeDB; A9C3P0; -.
DR   TreeFam; TF314856; -.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   PRO; PR:A9C3P0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 8.
DR   Bgee; ENSDARG00000059630; Expressed in early embryo and 20 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:0016020; C:membrane; IBA:GO_Central.
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   3: Inferred from homology;
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..285
FT                   /note="Malectin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000358589"
FT   TOPO_DOM        27..262
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..285
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          209..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         71
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q6INX3"
FT   BINDING         93
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q6INX3"
FT   BINDING         120
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q6INX3"
FT   BINDING         121
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q6INX3"
FT   BINDING         190
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q6INX3"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   285 AA;  31986 MW;  7A8E64D951569EF2 CRC64;
     MRRVTLHCAA RLVIAALWLL VEVCRAESGA QSLAERVIWA VNAGGDTHTD VHGIQFKKDP
     LEGKVGKASD YGVRLPILRS SPEDQILYQT ERYNEDTFGY EVPIREEGDY ILVMKYAEVY
     FAQSQQKVFD VRLNGHVVVK DLDIFDRVGH STAHDEIVPF SIKRGKLSVH GEVSTFNGKL
     TVEFVKGYYD NPKICALYVM KGKLEDVPKL QPHPGLEKRE EEEEEEEEGE GPEGEKKSAS
     TSPKNPVRSG PRTPNPYATD NSSLMFPILV AFGVFIPTLF CLCRL