MNL1 alpha-1,2-mannosidase MNL1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: MNL1
Official Full Name: alpha-1,2-mannosidase MNL1
Primary source: SGD:S000001247
Locus tag: YHR204W
See related: AllianceGenome:SGD:S000001247; FungiDB:YHR204W; VEuPathDB:YHR204W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: HTM1
Summary: Enables carbohydrate binding activity and mannosyl-oligosaccharide 1,2-alpha-mannosidase activity. Involved in endoplasmic reticulum mannose trimming and mannose trimming involved in glycoprotein ERAD pathway. Located in endoplasmic reticulum lumen. Used to study cystic fibrosis. Orthologous to human EDEM1 (ER degradation enhancing alpha-mannosidase like protein 1). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See MNL1 in Genome Data Viewer

Location:: chromosome: VIII

Exon count:: 1

Sequence:: Chromosome: VIII; NC_001140.6 (506319..508709)

Chromosome VIII - NC_001140.6 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001140.6

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Data show that binding of mannosidase Htm1 to protein disulfide isomerase Pdi1 is required for endoplasmic reticulum (ER)-associated protein degradation (ERAD).
Title: A Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.
analysis of an Htm1 (EDEM)-dependent, Mns1-independent Endoplasmic Reticulum-associated Degradation (ERAD) pathway in Saccharomyces cerevisiae
Title: Identification of an Htm1 (EDEM)-dependent, Mns1-independent Endoplasmic Reticulum-associated Degradation (ERAD) pathway in Saccharomyces cerevisiae: application of a novel assay for glycoprotein ERAD.
Systematic analysis of model substrates revealed that glycans mark structural determinants that are sensitive to the overall folding state of the molecule.
Title: Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system.
This disulfide bond is essential for the ERAD activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p
Title: Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradation.
Htm1 protein is an alpha1,2-specific exomannosidase that generates the Man(7)GlcNAc(2) oligosaccharide with a terminal alpha1,6-linked mannosyl residue on degradation substrates.
Title: Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum.
role of the lectin Htm1p in the degradation process of CFTR
Title: Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables alpha-mannosidase activity	IEA Inferred from Electronic Annotation more info
enables calcium ion binding	IEA Inferred from Electronic Annotation more info
enables carbohydrate binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables hydrolase activity, acting on glycosyl bonds	IEA Inferred from Electronic Annotation more info
enables mannosyl-oligosaccharide 1,2-alpha-mannosidase activity	IDA Inferred from Direct Assay more info	PubMed
enables mannosyl-oligosaccharide 1,2-alpha-mannosidase activity	IEA Inferred from Electronic Annotation more info
enables mannosyl-oligosaccharide 1,2-alpha-mannosidase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in ERAD pathway	IEA Inferred from Electronic Annotation more info
involved_in carbohydrate metabolic process	IEA Inferred from Electronic Annotation more info
involved_in endoplasmic reticulum mannose trimming	IEA Inferred from Electronic Annotation more info
involved_in endoplasmic reticulum mannose trimming	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in endoplasmic reticulum unfolded protein response	IBA Inferred from Biological aspect of Ancestor more info
involved_in mannoprotein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in mannose trimming involved in glycoprotein ERAD pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in mannose trimming involved in glycoprotein ERAD pathway	IEA Inferred from Electronic Annotation more info
involved_in mannose trimming involved in glycoprotein ERAD pathway	IGI Inferred from Genetic Interaction more info	PubMed
involved_in mannose trimming involved in glycoprotein ERAD pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein alpha-1,2-demannosylation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein glycosylation	IEA Inferred from Electronic Annotation more info
involved_in response to unfolded protein	IEA Inferred from Electronic Annotation more info
involved_in ubiquitin-dependent glycoprotein ERAD pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in ubiquitin-dependent glycoprotein ERAD pathway	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in endoplasmic reticulum	HDA more info	PubMed
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
located_in endoplasmic reticulum lumen	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum lumen	IEA Inferred from Electronic Annotation more info
located_in endoplasmic reticulum quality control compartment	IEA Inferred from Electronic Annotation more info
located_in membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: alpha-1,2-mannosidase MNL1

NP_012074.3

EC 3.2.1.24

Alpha-1,2-specific exomannosidase of the endoplasmic reticulum; involved in glycan trimming of both folded and misfolded glycoproteins; complexes with Pdi1p, and trims a mannose from Man8GlcNac2 glycans to generate Man7GlcNac2, an oligosaccharide signal on glycoproteins destined for ER-associated protein degradation; requires Pdi1p for stability and substrate recognition; human homolog EDEM1 can complement yeast null mutant

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001140.6 Reference assembly

Range

506319..508709

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179335.3 → NP_012074.3 TPA: alpha-1,2-mannosidase MNL1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012074.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D3DLF3, P38888

UniProtKB/TrEMBL

A6ZTB1, B3LSW5, C8ZA05, G2WFS8, N1P2K2

Conserved Domains (2) summary

pfam01532
Location:42 → 502

Glyco_hydro_47; Glycosyl hydrolase family 47

cl00038
Location:557 → 594

BRCT; C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains