MLEC_HUMAN
ID MLEC_HUMAN Reviewed; 292 AA.
AC Q14165;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Malectin {ECO:0000305};
DE Flags: Precursor;
GN Name=MLEC {ECO:0000312|HGNC:HGNC:28973}; Synonyms=KIAA0152;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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).
RN [3]
RP PROTEIN SEQUENCE OF 91-103; 127-138; 144-151 AND 178-190, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [7] {ECO:0007744|PDB:6S7T}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND INTERACTION WITH
RP OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX.
RX PubMed=31831667; DOI=10.1126/science.aaz3505;
RA Ramirez A.S., Kowal J., Locher K.P.;
RT "Cryo-electron microscopy structures of human oligosaccharyltransferase
RT complexes OST-A and OST-B.";
RL Science 366:1372-1375(2019).
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:0000269|PubMed:31831667}.
CC -!- INTERACTION:
CC Q14165; P04843: RPN1; NbExp=2; IntAct=EBI-1046466, EBI-355963;
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 -!- SEQUENCE CAUTION:
CC Sequence=BAA09773.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D63486; BAA09773.2; ALT_INIT; mRNA.
DR EMBL; BC000371; AAH00371.1; -; mRNA.
DR EMBL; BC016297; AAH16297.1; -; mRNA.
DR CCDS; CCDS9206.1; -.
DR RefSeq; NP_055545.1; NM_014730.3.
DR PDB; 6S7T; EM; 3.50 A; I=1-292.
DR PDBsum; 6S7T; -.
DR AlphaFoldDB; Q14165; -.
DR SMR; Q14165; -.
DR BioGRID; 115108; 81.
DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B.
DR IntAct; Q14165; 34.
DR MINT; Q14165; -.
DR STRING; 9606.ENSP00000228506; -.
DR CAZy; CBM57; Carbohydrate-Binding Module Family 57.
DR GlyGen; Q14165; 1 site.
DR iPTMnet; Q14165; -.
DR PhosphoSitePlus; Q14165; -.
DR SwissPalm; Q14165; -.
DR BioMuta; MLEC; -.
DR DMDM; 2495712; -.
DR OGP; Q14165; -.
DR EPD; Q14165; -.
DR jPOST; Q14165; -.
DR MassIVE; Q14165; -.
DR MaxQB; Q14165; -.
DR PaxDb; Q14165; -.
DR PeptideAtlas; Q14165; -.
DR PRIDE; Q14165; -.
DR ProteomicsDB; 59893; -.
DR Antibodypedia; 2338; 125 antibodies from 19 providers.
DR DNASU; 9761; -.
DR Ensembl; ENST00000228506.8; ENSP00000228506.3; ENSG00000110917.8.
DR GeneID; 9761; -.
DR KEGG; hsa:9761; -.
DR MANE-Select; ENST00000228506.8; ENSP00000228506.3; NM_014730.4; NP_055545.1.
DR UCSC; uc001tyy.2; human.
DR CTD; 9761; -.
DR DisGeNET; 9761; -.
DR GeneCards; MLEC; -.
DR HGNC; HGNC:28973; MLEC.
DR HPA; ENSG00000110917; Low tissue specificity.
DR MIM; 613802; gene.
DR neXtProt; NX_Q14165; -.
DR OpenTargets; ENSG00000110917; -.
DR PharmGKB; PA164723038; -.
DR VEuPathDB; HostDB:ENSG00000110917; -.
DR eggNOG; KOG3593; Eukaryota.
DR GeneTree; ENSGT00390000016504; -.
DR HOGENOM; CLU_065446_1_0_1; -.
DR InParanoid; Q14165; -.
DR OMA; PNPYSMD; -.
DR OrthoDB; 715383at2759; -.
DR PhylomeDB; Q14165; -.
DR TreeFam; TF314856; -.
DR PathwayCommons; Q14165; -.
DR Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q14165; -.
DR BioGRID-ORCS; 9761; 14 hits in 1078 CRISPR screens.
DR ChiTaRS; MLEC; human.
DR GenomeRNAi; 9761; -.
DR Pharos; Q14165; Tbio.
DR PRO; PR:Q14165; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q14165; protein.
DR Bgee; ENSG00000110917; Expressed in mucosa of sigmoid colon and 218 other tissues.
DR ExpressionAtlas; Q14165; baseline and differential.
DR Genevisible; Q14165; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
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; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..292
FT /note="Malectin"
FT /id="PRO_0000013982"
FT TOPO_DOM 29..269
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 221..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 104
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 132
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT TURN 267..271
FT /evidence="ECO:0007829|PDB:6S7T"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:6S7T"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:6S7T"
SQ SEQUENCE 292 AA; 32234 MW; 448D673A5A1A8F09 CRC64;
MLGAWAVEGT AVALLRLLLL LLPPAIRGPG LGVAGVAGAA GAGLPESVIW AVNAGGEAHV
DVHGIHFRKD PLEGRVGRAS DYGMKLPILR SNPEDQILYQ TERYNEETFG YEVPIKEEGD
YVLVLKFAEV YFAQSQQKVF DVRLNGHVVV KDLDIFDRVG HSTAHDEIIP MSIRKGKLSV
QGEVSTFTGK LYIEFVKGYY DNPKVCALYI MAGTVDDVPK LQPHPGLEKK EEEEEEEEYD
EGSNLKKQTN KNRVQSGPRT PNPYASDNSS LMFPILVAFG VFIPTLFCLC RL
