Full text data of MLEC
MLEC
(KIAA0152)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Malectin; Flags: Precursor
Malectin; Flags: Precursor
UniProt
Q14165
ID MLEC_HUMAN Reviewed; 292 AA.
AC Q14165;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Malectin;
DE Flags: Precursor;
GN Name=MLEC; Synonyms=KIAA0152;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of 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
RT project: 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 MASS
RP 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Carbohydrate-binding protein with a strong ligand
CC preference for Glc2-N-glycan. May play a role in the early steps
CC of protein N-glycosylation (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein (By similarity).
CC -!- SIMILARITY: Belongs to the malectin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09773.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D63486; BAA09773.2; ALT_INIT; mRNA.
DR EMBL; BC000371; AAH00371.1; -; mRNA.
DR EMBL; BC016297; AAH16297.1; -; mRNA.
DR RefSeq; NP_055545.1; NM_014730.2.
DR UniGene; Hs.744910; -.
DR ProteinModelPortal; Q14165; -.
DR SMR; Q14165; 43-216.
DR STRING; 9606.ENSP00000228506; -.
DR PhosphoSite; Q14165; -.
DR DMDM; 2495712; -.
DR OGP; Q14165; -.
DR PaxDb; Q14165; -.
DR PRIDE; Q14165; -.
DR Ensembl; ENST00000228506; ENSP00000228506; ENSG00000110917.
DR GeneID; 9761; -.
DR KEGG; hsa:9761; -.
DR UCSC; uc001tyy.1; human.
DR CTD; 9761; -.
DR GeneCards; GC12P121124; -.
DR HGNC; HGNC:28973; MLEC.
DR HPA; HPA007538; -.
DR MIM; 613802; gene.
DR neXtProt; NX_Q14165; -.
DR PharmGKB; PA164723038; -.
DR eggNOG; NOG271322; -.
DR HOGENOM; HOG000290695; -.
DR HOVERGEN; HBG108138; -.
DR InParanoid; Q14165; -.
DR OMA; AHDEYIP; -.
DR OrthoDB; EOG7Q2N61; -.
DR PhylomeDB; Q14165; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; MLEC; human.
DR GenomeRNAi; 9761; -.
DR NextBio; 36741; -.
DR PRO; PR:Q14165; -.
DR ArrayExpress; Q14165; -.
DR Bgee; Q14165; -.
DR CleanEx; HS_MLEC; -.
DR Genevestigator; Q14165; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0006457; P:protein folding; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR InterPro; IPR021720; Malectin.
DR Pfam; PF11721; Malectin; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 28 Potential.
FT CHAIN 29 292 Malectin.
FT /FTId=PRO_0000013982.
FT TOPO_DOM 29 269 Lumenal (Potential).
FT TRANSMEM 270 290 Helical; (Potential).
FT TOPO_DOM 291 292 Cytoplasmic (Potential).
FT COMPBIAS 231 238 Poly-Glu.
FT BINDING 82 82 Carbohydrate (By similarity).
FT BINDING 104 104 Carbohydrate (By similarity).
FT BINDING 131 131 Carbohydrate (By similarity).
FT BINDING 132 132 Carbohydrate (By similarity).
FT BINDING 201 201 Carbohydrate (By similarity).
FT CARBOHYD 268 268 N-linked (GlcNAc...) (Potential).
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
//
ID MLEC_HUMAN Reviewed; 292 AA.
AC Q14165;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Malectin;
DE Flags: Precursor;
GN Name=MLEC; Synonyms=KIAA0152;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of 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
RT project: 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 MASS
RP 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Carbohydrate-binding protein with a strong ligand
CC preference for Glc2-N-glycan. May play a role in the early steps
CC of protein N-glycosylation (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein (By similarity).
CC -!- SIMILARITY: Belongs to the malectin family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09773.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D63486; BAA09773.2; ALT_INIT; mRNA.
DR EMBL; BC000371; AAH00371.1; -; mRNA.
DR EMBL; BC016297; AAH16297.1; -; mRNA.
DR RefSeq; NP_055545.1; NM_014730.2.
DR UniGene; Hs.744910; -.
DR ProteinModelPortal; Q14165; -.
DR SMR; Q14165; 43-216.
DR STRING; 9606.ENSP00000228506; -.
DR PhosphoSite; Q14165; -.
DR DMDM; 2495712; -.
DR OGP; Q14165; -.
DR PaxDb; Q14165; -.
DR PRIDE; Q14165; -.
DR Ensembl; ENST00000228506; ENSP00000228506; ENSG00000110917.
DR GeneID; 9761; -.
DR KEGG; hsa:9761; -.
DR UCSC; uc001tyy.1; human.
DR CTD; 9761; -.
DR GeneCards; GC12P121124; -.
DR HGNC; HGNC:28973; MLEC.
DR HPA; HPA007538; -.
DR MIM; 613802; gene.
DR neXtProt; NX_Q14165; -.
DR PharmGKB; PA164723038; -.
DR eggNOG; NOG271322; -.
DR HOGENOM; HOG000290695; -.
DR HOVERGEN; HBG108138; -.
DR InParanoid; Q14165; -.
DR OMA; AHDEYIP; -.
DR OrthoDB; EOG7Q2N61; -.
DR PhylomeDB; Q14165; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; MLEC; human.
DR GenomeRNAi; 9761; -.
DR NextBio; 36741; -.
DR PRO; PR:Q14165; -.
DR ArrayExpress; Q14165; -.
DR Bgee; Q14165; -.
DR CleanEx; HS_MLEC; -.
DR Genevestigator; Q14165; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0006457; P:protein folding; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR InterPro; IPR021720; Malectin.
DR Pfam; PF11721; Malectin; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 28 Potential.
FT CHAIN 29 292 Malectin.
FT /FTId=PRO_0000013982.
FT TOPO_DOM 29 269 Lumenal (Potential).
FT TRANSMEM 270 290 Helical; (Potential).
FT TOPO_DOM 291 292 Cytoplasmic (Potential).
FT COMPBIAS 231 238 Poly-Glu.
FT BINDING 82 82 Carbohydrate (By similarity).
FT BINDING 104 104 Carbohydrate (By similarity).
FT BINDING 131 131 Carbohydrate (By similarity).
FT BINDING 132 132 Carbohydrate (By similarity).
FT BINDING 201 201 Carbohydrate (By similarity).
FT CARBOHYD 268 268 N-linked (GlcNAc...) (Potential).
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
//
MIM
613802
*RECORD*
*FIELD* NO
613802
*FIELD* TI
*613802 MALECTIN; MLEC
;;KIAA0152
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated KG-1 immature
read moremyeloid leukemia cell line cDNA library, Nagase et al. (1995) obtained
an MLEC clone, which they designated KIAA0152. The deduced 292-amino
acid protein contains a transmembrane domain. Northern blot analysis
detected MLEC expression in all human tissues and cell lines examined,
with highest expression in heart and skeletal muscle.
Schallus et al. (2008) cloned Xenopus Mlec, and they identified human
MLEC by database analysis. Both proteins contain an N-terminal signal
peptide, a globular domain of about 190 amino acids, and a transmembrane
domain near the C terminus. Database analysis revealed Mlec orthologs in
most animals, with weaker conservation in plants. Xenopus Mlec was
expressed in the endoplasmic reticulum of transfected human osteosarcoma
cells.
GENE FUNCTION
Schallus et al. (2008) showed that Xenopus Mlec bound specifically to
diglucosylated N-glycan, a conserved intermediate in the biosynthesis of
N-glycoproteins in the endoplasmic reticulum.
MAPPING
By PCR of a human/rodent hybrid panel, Nagase et al. (1995) mapped the
MLEC gene to chromosome 12. Hartz (2011) mapped the MLEC gene to
chromosome 12q24.31 based on an alignment of the MLEC sequence (GenBank
GENBANK BC00037) with the genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 3/1/2011.
2. Nagase, T.; Seki, N.; Tanaka, A.; Ishikawa, K.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. IV. The coding
sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 2: 167-174, 1995.
3. Schallus, T.; Jaeckh, C.; Feher, K.; Palma, A. S.; Liu, Y.; Simpson,
J. C.; Mackeen, M.; Stier, G.; Gibson, T. J.; Feizi, T.; Pieler, T.;
Muhle-Goll, C.: Malectin: a novel carbohydrate-binding protein of
the endoplasmic reticulum and a candidate player in the early steps
of protein N-glycosylation. Molec. Biol. Cell 19: 3404-3414, 2008.
*FIELD* CD
Patricia A. Hartz: 3/11/2011
*FIELD* ED
mgross: 03/11/2011
*RECORD*
*FIELD* NO
613802
*FIELD* TI
*613802 MALECTIN; MLEC
;;KIAA0152
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated KG-1 immature
read moremyeloid leukemia cell line cDNA library, Nagase et al. (1995) obtained
an MLEC clone, which they designated KIAA0152. The deduced 292-amino
acid protein contains a transmembrane domain. Northern blot analysis
detected MLEC expression in all human tissues and cell lines examined,
with highest expression in heart and skeletal muscle.
Schallus et al. (2008) cloned Xenopus Mlec, and they identified human
MLEC by database analysis. Both proteins contain an N-terminal signal
peptide, a globular domain of about 190 amino acids, and a transmembrane
domain near the C terminus. Database analysis revealed Mlec orthologs in
most animals, with weaker conservation in plants. Xenopus Mlec was
expressed in the endoplasmic reticulum of transfected human osteosarcoma
cells.
GENE FUNCTION
Schallus et al. (2008) showed that Xenopus Mlec bound specifically to
diglucosylated N-glycan, a conserved intermediate in the biosynthesis of
N-glycoproteins in the endoplasmic reticulum.
MAPPING
By PCR of a human/rodent hybrid panel, Nagase et al. (1995) mapped the
MLEC gene to chromosome 12. Hartz (2011) mapped the MLEC gene to
chromosome 12q24.31 based on an alignment of the MLEC sequence (GenBank
GENBANK BC00037) with the genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 3/1/2011.
2. Nagase, T.; Seki, N.; Tanaka, A.; Ishikawa, K.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. IV. The coding
sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 2: 167-174, 1995.
3. Schallus, T.; Jaeckh, C.; Feher, K.; Palma, A. S.; Liu, Y.; Simpson,
J. C.; Mackeen, M.; Stier, G.; Gibson, T. J.; Feizi, T.; Pieler, T.;
Muhle-Goll, C.: Malectin: a novel carbohydrate-binding protein of
the endoplasmic reticulum and a candidate player in the early steps
of protein N-glycosylation. Molec. Biol. Cell 19: 3404-3414, 2008.
*FIELD* CD
Patricia A. Hartz: 3/11/2011
*FIELD* ED
mgross: 03/11/2011