MLEC_MOUSE
ID MLEC_MOUSE Reviewed; 291 AA.
AC Q6ZQI3; Q8C6C3; Q8CD40; Q8CI91;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Malectin {ECO:0000305};
DE Flags: Precursor;
GN Name=Mlec {ECO:0000312|MGI:MGI:1924015}; Synonyms=Kiaa0152;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Olfactory epithelium;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SEQUENCE CAUTION:
CC Sequence=BAC97876.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129066; BAC97876.1; ALT_INIT; mRNA.
DR EMBL; AK031525; BAC27434.1; -; mRNA.
DR EMBL; AK075940; BAC36070.1; -; mRNA.
DR EMBL; BC035300; AAH35300.2; -; mRNA.
DR EMBL; BC058245; AAH58245.1; -; mRNA.
DR CCDS; CCDS19581.1; -.
DR RefSeq; NP_780612.2; NM_175403.3.
DR AlphaFoldDB; Q6ZQI3; -.
DR SMR; Q6ZQI3; -.
DR BioGRID; 224576; 9.
DR ComplexPortal; CPX-5822; Oligosaccharyltransferase complex B.
DR IntAct; Q6ZQI3; 1.
DR STRING; 10090.ENSMUSP00000107749; -.
DR CAZy; CBM57; Carbohydrate-Binding Module Family 57.
DR GlyGen; Q6ZQI3; 1 site.
DR iPTMnet; Q6ZQI3; -.
DR PhosphoSitePlus; Q6ZQI3; -.
DR SwissPalm; Q6ZQI3; -.
DR EPD; Q6ZQI3; -.
DR jPOST; Q6ZQI3; -.
DR MaxQB; Q6ZQI3; -.
DR PaxDb; Q6ZQI3; -.
DR PeptideAtlas; Q6ZQI3; -.
DR PRIDE; Q6ZQI3; -.
DR ProteomicsDB; 252575; -.
DR Antibodypedia; 2338; 125 antibodies from 19 providers.
DR DNASU; 109154; -.
DR Ensembl; ENSMUST00000112121; ENSMUSP00000107749; ENSMUSG00000048578.
DR GeneID; 109154; -.
DR KEGG; mmu:109154; -.
DR UCSC; uc008zdf.2; mouse.
DR CTD; 9761; -.
DR MGI; MGI:1924015; Mlec.
DR VEuPathDB; HostDB:ENSMUSG00000048578; -.
DR eggNOG; KOG3593; Eukaryota.
DR GeneTree; ENSGT00390000016504; -.
DR HOGENOM; CLU_065446_1_0_1; -.
DR InParanoid; Q6ZQI3; -.
DR OMA; PNPYSMD; -.
DR OrthoDB; 1057965at2759; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 109154; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Mlec; mouse.
DR PRO; PR:Q6ZQI3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6ZQI3; protein.
DR Bgee; ENSMUSG00000048578; Expressed in saccule of membranous labyrinth and 258 other tissues.
DR Genevisible; Q6ZQI3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
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:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
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 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_0000013983"
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"
FT CONFLICT 69
FT /note="D -> G (in Ref. 2; BAC27434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32342 MW; 271EA5AA0F65214D CRC64;
MLRPRGAEGT AVALLRLLLL LLLLGPKLRG PGLGVVGAAG AGLPESVIWA VNAGGEAHVD
VHGIHFRKDP LEGRVGRASD YGMKLPILRS TPEDQILYQT ERYNEETFGY EVPVKEEGDY
VLVLKFAEVY FAQSQQKVFD VRLNGHVVVK DLDIFDRVGH STAHDEIIPM SIRKGKLSVR
GEVSTFTGKL YIEFVKGYYD NPKVCALYIL AGTVDDVPKL QPHPGLEKKE EEEEEEEYDE
GSNLKRQTNK NRVQSGPRTP NPYASDNSSL MFPILVAFGV FIPTLFCLCR L
