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MNS1/YJR131W Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrX: 667634 to 669283 CDS: 667634 - 669283 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
MNS1	YJR131W		ORF, Verified	S000003892
Description
Alpha-1,2-mannosidase involved in ER quality control; catalyzes the removal of one mannose residue from Man9GlcNAc to produce a single isomer of Man8GlcNAc in N-linked oligosaccharide biosynthesis; integral to ER membrane

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By calcium ion binding DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001382 Assigned on 2007-05-23 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0106 Assigned on 2007-05-23 UniProtKB hydrolase activity GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0378 Assigned on 2007-05-23 UniProtKB hydrolase activity, acting on glycosyl bonds GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0326 Assigned on 2007-05-23 UniProtKB mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Camirand A, et al. (1991) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Isolation and characterization of the gene encoding a specific processing alpha-mannosidase. J Biol Chem 266(23):15120-7      IDA : Inferred from Direct Assay Assigned on 2002-09-30 SGD DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001382 Assigned on 2007-05-23 UniProtKB GOA curators and MGI curators (2001) Gene Ontology annotation based on Enzyme Commission mapping.      IEA : Inferred from Electronic Annotation with IUBMB:3.2.1.113 Assigned on 2007-05-23 UniProtKB
Biological Process Annotation(s) Reference(s) Evidence Assigned By ER-associated protein catabolic process Knop M, et al. (1996) N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 12(12):1229-38      IMP : Inferred from Mutant Phenotype Assigned on 2005-07-28 SGD metabolic process GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0326 Assigned on 2007-05-23 UniProtKB protein amino acid N-linked glycosylation Puccia R, et al. (1993) Disruption of the processing alpha-mannosidase gene does not prevent outer chain synthesis in Saccharomyces cerevisiae. Biochem J 290 ( Pt 1)():21-6      IMP : Inferred from Mutant Phenotype Assigned on 2002-09-30 SGD
Cellular Component Annotation(s) Reference(s) Evidence Assigned By endoplasmic reticulum Burke J, et al. (1996) The Saccharomyces cerevisiae processing alpha 1,2-mannosidase is localized in the endoplasmic reticulum, independently of known retrieval motifs. Eur J Cell Biol 70(4):298-305      IDA : Inferred from Direct Assay Assigned on 2002-09-30 SGD GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0256 Assigned on 2007-05-23 UniProtKB integral to membrane GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0812 Assigned on 2007-05-23 UniProtKB GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-9906 Assigned on 2009-10-01 UniProtKB membrane DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001382 Assigned on 2007-05-23 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0472 Assigned on 2007-05-23 UniProtKB

Pathways [TOP] [NEXT]
No pathways available

Summary Paragraph [TOP] [NEXT]

SUMMARY PARAGRAPH for MNS1/YJR131W for MNS1 During N-linked glycosylation of proteins, oligosaccharide chains are assembled on the carrier molecule dolichyl pyrophosphate in the following order: 2 molecules of N-acetylglucosamine (GlcNAc), 9 molecules of mannose, and 3 molecules of glucose. These 14-residue oligosaccharide cores are then transferred to asparagine residues on nascent polypeptide chains in the endoplasmic reticulum (ER). As proteins progress through the Golgi apparatus, the oligosaccharide cores are modified by trimming and extension to generate a diverse array of glycosylated proteins (reviewed in 1, 2). MNS1 encodes mannosidase I (EC 3.2.1.113), which removes one of the mannose residues added by Alg9p from N-linked core oligosaccharides (3, 4). This is the last trimming reaction that occurs in the ER before maturing proteins migrate to the Golgi apparatus. At this point, improperly folded proteins are targeted for degradation in the cytoplasm by the 26S proteasome via Mnl1p and the Sec61p pore complex (5, 6, 7, 8); mutations in MNS1 cause defects in this degradation. Although MNS1p is a type II ER membrane protein (9, 10), it lacks ER retention signals and requires Rer1p for proper localization to the ER (11). The human homolog of Mns1p is called MAN1B1 (OMIM) (12, 13). Last Updated: 2005-07-28

Basic References [TOP]

BASIC INFORMATION REFERENCES forMNS1/YJR131W for MNS1 1) Herscovics A and Orlean P (1993) Glycoprotein biosynthesis in yeast. FASEB J 7(6):540-50        2) Burda P and Aebi M (1999) The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta 1426(2):239-57      3) Camirand A, et al. (1991) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Isolation and characterization of the gene encoding a specific processing alpha-mannosidase. J Biol Chem 266(23):15120-7      4) Jelinek-Kelly S and Herscovics A (1988) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the alpha-mannosidase which removes one specific mannose residue from Man9GlcNAc. J Biol Chem 263(29):14757-63      5) Knop M, et al. (1996) N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 12(12):1229-38      6) Jakob CA, et al. (1998) Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 142(5):1223-33        7) Cabral CM, et al. (2001) Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem Sci 26(10):619-24              8) Kostova Z and Wolf DH (2003) For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J 22(10):2309-17            9) Burke J, et al. (1996) The Saccharomyces cerevisiae processing alpha 1,2-mannosidase is localized in the endoplasmic reticulum, independently of known retrieval motifs. Eur J Cell Biol 70(4):298-305      10) Grondin B and Herscovics A (1992) Topology of ER processing alpha-mannosidase of Saccharomyces cerevisiae. Glycobiology 2(4):369-72      11) Massaad MJ, et al. (1999) The processing alpha1,2-mannosidase of Saccharomyces cerevisiae depends on Rer1p for its localization in the endoplasmic reticulum. Eur J Cell Biol 78(7):435-40      12) Gonzalez DS, et al. (1999) Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis. J Biol Chem 274(30):21375-86        13) Tremblay LO and Herscovics A (1999) Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. Glycobiology 9(10):1073-8

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for MNS1/YJR131W

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for MNS1/YJR131W

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Candida Homologs (CGD) Candida Homologs (CandidaDB) Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]

Protein Sequence Calculations from Predicted Full length Translation N-term MKNSVGI C-term LTTGWSL Length(aa) 549 MW(Da) 63,057 pI 5.52 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.083   Codon Adaptation Index 0.144   Frequency of Optimal Codons 0.450   Hydropathicity of Protein -0.321   Aromaticity Score 0.129

10 20 30 40 50 | | | | | MKNSVGISIATIVAIIAAIYYVPWYEHFERKSPGAGEMRDRIESMFLESW RDYSKHGWGYDVYGPIEHTSHNMPRGNQPLGWIIVDSVDTLMLMYNSSTL YKSEFEAEIQRSEHWINDVLDFDIDAEVNVFETTIRMLGGLLSAYHLSDV LEVGNKTVYLNKAIDLGDRLALAFLSTQTGIPYSSINLHSGQAVKNHADG GASSTAEFTTLQMEFKYLAYLTGNRTYWELVERVYEPLYKNNDLLNTYDG LVPIYTFPDTGKFGASTIRFGSRGDSFYEYLLKQYLLTHETLYYDLYRKS MEGMKKHLLAQSKPSSLWYIGEREQGLHGQLSPKMDHLVCFMGGLLASGS TEGLSIHEARRRPFFSLSLERKSDWDLAKGITDTCYQMYKQSSSGLAPEI VVFNDGNIKQDGWWRSSVGDFFVKPLDRHNLQRPETVESIMFMYHLSHDH KYREWGAEIATSFFENTCVDCNDPKLRRFTSLSDCITLPTKKSNNMESFW LAETLKYLYILFLDEFDLTKVVFNTEAHPFPVLDEEILKSQSLTTGWSL*

Protein Structures from PDB: proteins of known structure with sequence similarity to MNS1/YJR131W, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to MNS1 Homolog Source (per PDB) Protein Alignment: MNS1 vs. Homolog External Links P-Value %Identical %Similar Alignment 1dl2 ( Chain: A) Crystal structure of class i alpha-1,2-mannosidase from saccharomyces cerevisiae at 1.54 angstrom resolution PDB_Info PDB_Structure Saccharomyces cerevisiae 9.9e-262 99 0 View alignment SCOP MMDB CATH 1g6i ( Chain: A) Crystal structure of the yeast alpha-1,2-mannosidase with bound 1-deoxymannojirimycin at 1.59 a resolution PDB_Info PDB_Structure Saccharomyces cerevisiae 9.9e-262 99 0 View alignment SCOP MMDB CATH 1fo2 ( Chain: A) Crystal structure of human class i alpha1,2-mannosidase in complex with 1-deoxymannojirimycin PDB_Info PDB_Structure Homo sapiens 1.2e-67 40 25 View alignment SCOP MMDB CATH 1fo3 ( Chain: A) Crystal structure of human class i alpha1,2-mannosidase in complex with kifunensine PDB_Info PDB_Structure Homo sapiens 1.2e-67 40 25 View alignment SCOP MMDB CATH 1fmi ( Chain: A) Crystal structure of human class i alpha1,2-mannosidase PDB_Info PDB_Structure Homo sapiens 1.2e-67 40 25 View alignment SCOP MMDB CATH 1x9d ( Chain: A) Crystal structure of human class i alpha-1,2-mannosidase in complex with thio-disaccharide substrate analogue PDB_Info PDB_Structure Homo sapiens 1.6e-67 40 25 View alignment SCOP MMDB CATH 1nxc ( Chain: A) Structure of mouse golgi alpha-1,2-mannosidase ia reveals the molecular basis for substrate specificity among class i enzymes (family 47 glycosidases) PDB_Info PDB_Structure Mus musculus 8.3e-59 36 28 View alignment SCOP MMDB CATH 1hcu ( Chain: A, D, B, C) Alpha-1,2-mannosidase from trichoderma reesei PDB_Info PDB_Structure Trichoderma reesei Chain A = 3.9e-29 29 27 View alignment SCOP MMDB CATH Chain D = 3.9e-29 29 27 View alignment Chain B = 3.9e-29 29 27 View alignment Chain C = 3.9e-29 29 27 View alignment 1kkt ( Chain: B, A) Structure of p. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the er and golgi class i enzymes PDB_Info PDB_Structure Penicillium citrinum Chain B = 1.0e-26 27 29 View alignment SCOP MMDB CATH Chain A = 1.0e-26 27 29 View alignment 1kre ( Chain: A, B) Structure of p. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the er and golgi class i enzymes PDB_Info PDB_Structure Penicillium citrinum Chain A = 1.0e-26 27 29 View alignment SCOP MMDB CATH Chain B = 1.0e-26 27 29 View alignment 1krf ( Chain: B, A) Structure of p. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the er and golgi class i enzymes PDB_Info PDB_Structure Penicillium citrinum Chain B = 1.0e-26 27 29 View alignment SCOP MMDB CATH Chain A = 1.0e-26 27 29 View alignment 2ri8 ( Chain: B, A) Penicillium citrinum alpha-1,2-mannosidase complex with glycerol PDB_Info PDB_Structure Penicillium citrinum Chain B = 6.0e-26 28 28 View alignment SCOP MMDB CATH Chain A = 6.0e-26 28 28 View alignment 2ri9 ( Chain: B, A) Penicillium citrinum alpha-1,2-mannosidase in complex with a substrate analog PDB_Info PDB_Structure Penicillium citrinum Chain B = 6.0e-26 28 28 View alignment SCOP MMDB CATH Chain A = 6.0e-26 28 28 View alignment

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
MNS1	Camirand A, et al. (1991) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Isolation and characterization of the gene encoding a specific processing alpha-mannosidase. J Biol Chem 266(23):15120-7

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YJR131W	SGD Systematic Sequence
853595	NCBI: Gene ID
NP_012665.1	NCBI: RefSeq protein version ID
NP_012665.1	NCBI: RefSeq protein version ID
6322591	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources YeastRC Localization (Seattle) YGAC Triples YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]
No community annotation available.

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
38 curated references; 0 references not yet curated
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Clerc S, et al. (2009) Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J Cell Biol 184(1):159-72	|ALG12 |ALG3 |ALG8 |ALG9 |MNL1 |PDI1 |PRC1 |ROT2 |YOS9
Mutants/Phenotypes Strains/Constructs	Quinn RP, et al. (2009) A novel role for Gtb1p in glucose trimming of N-linked glycans. Glycobiology 19(12):1408-16	|ALG8 |CWH41 |GTB1 |ROT2
Fungal Related Genes/Proteins	Deshpande N, et al. (2008) Protein glycosylation pathways in filamentous fungi. Glycobiology 18(8):626-37	|ALG1 |ALG11 |ALG12 |ALG13 |ALG14 |ALG2 |ALG3 |ALG6 |ALG7 |ALG8 |ALG9 |ANP1 |CWH41 |DIE2 |MORE
Fungal Related Genes/Proteins	Hannay K, et al. (2008) Buffering by gene duplicates: an analysis of molecular correlates and evolutionary conservation. BMC Genomics 9:609	|BUB1 |HKR1 |HLR1 |HMI1 |HOC1 |LRE1 |MAD3 |MNL1 |MSB2 |OCH1 |PIF1 |RRM3 |SET1 |SET2 |MORE
Reviews	Jigami Y (2008) Yeast glycobiology and its application. Biosci Biotechnol Biochem 72(3):637-48	|ALG1 |ALG11 |ALG12 |ALG13 |ALG14 |ALG2 |ALG3 |ALG5 |ALG6 |ALG7 |ALG8 |ALG9 |ANP1 |CWH41 |MORE
Evolution Fungal Related Genes/Proteins	Coronado JE, et al. (2007) Conserved processes and lineage-specific proteins in fungal cell wall evolution. Eukaryot Cell 6(12):2269-77	|ACF2 |AGA1 |AGA2 |ANS1 |BAR1 |BGL2 |BSC1 |CCW12 |CCW14 |CDA1 |CDA2 |CHS1 |CHS2 |CHS3 |MORE
Fungal Related Genes/Proteins	Mora-Montes HM, et al. (2007) Endoplasmic Reticulum {alpha}-Glycosidases of Candida albicans Are Required for N Glycosylation, Cell Wall Integrity, and Normal Host-Fungus Interaction. Eukaryot Cell 6(12):2184-93	|CWH41 |ROT2
Reviews	Lesage G and Bussey H (2006) Cell wall assembly in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 70(2):317-43	|ANP1 |BGL2 |BIG1 |CDA1 |CDA2 |CHS1 |CHS2 |CHS3 |CHS6 |CHS7 |CNE1 |CRH1 |CRR1 |CTS1 |MORE
Other Features Protein/Nucleic Acid Structure	Mulakala C, et al. (2006) Docking studies on glycoside hydrolase Family 47 endoplasmic reticulum alpha-(1-->2)-mannosidase I to elucidate the pathway to the substrate transition state. Carbohydr Res 341(13):2233-45
Function/Process Genetic Interactions Mutants/Phenotypes Strains/Constructs	Bhamidipati A, et al. (2005) Exploration of the Topological Requirements of ERAD Identifies Yos9p as a Lectin Sensor of Misfolded Glycoproteins in the ER Lumen. Mol Cell 19(6):741-51	|DER1 |HRD1 |MNL1 |YOS9
Function/Process Mutants/Phenotypes	Szathmary R, et al. (2005) Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell 19(6):765-75	|ALG12 |ALG3 |ALG9 |MNL1 |PRC1 |YOS9
Non-Fungal Related Genes/Proteins Protein Sequence Features Protein/Nucleic Acid Structure	Tempel W, et al. (2004) Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases. J Biol Chem 279(28):29774-86
Genetic Interactions Strains/Constructs	Tong AH, et al. (2004) Global mapping of the yeast genetic interaction network. Science 303(5659):808-13	|AAD4 |AAH1 |ABF2 |ACE2 |ADH6 |AEP2 |AFG1 |AGP1 |AHC1 |AHC2 |AIM21 |AIM22 |AIM26 |AIM29 |MORE
Reviews	Kostova Z and Wolf DH (2003) For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J 22(10):2309-17	|CDC48 |HRD3 |IRE1 |KAR2 |MNL1 |SEC61 |UBC7
Function/Process	Cipollo JF and Trimble RB (2002) The Saccharomyces cerevisiae alg12delta mutant reveals a role for the middle-arm alpha1,2Man- and upper-arm alpha1,2Manalpha1,6Man- residues of Glc3Man9GlcNAc2-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus. Glycobiology 12(11):749-62	|ALG12 |ALG9
Non-Fungal Related Genes/Proteins Reviews	Cabral CM, et al. (2001) Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem Sci 26(10):619-24
Cellular Location Protein-protein Interactions	Massaad MJ and Herscovics A (2001) Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system. J Cell Sci 114(Pt 24):4629-35	|ALG5 |OST1 |RER1 |SEC12
Fungal Related Genes/Proteins	Nakatsukasa K, et al. (2001) Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins. J Biol Chem 276(12):8635-8	|MNL1
Function/Process Mutants/Phenotypes Protein Sequence Features Strains/Constructs Substrates/Ligands/Cofactors	Romero PA, et al. (2000) Mutation of Arg(273) to Leu alters the specificity of the yeast N-glycan processing class I alpha1,2-mannosidase. J Biol Chem 275(15):11071-4
Protein/Nucleic Acid Structure Substrates/Ligands/Cofactors	Vallee F, et al. (2000) Crystal structure of a class I alpha1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control. EMBO J 19(4):581-8
Alias Non-Fungal Related Genes/Proteins	Gonzalez DS, et al. (1999) Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis. J Biol Chem 274(30):21375-86
Reviews	Herscovics A (1999) Processing glycosidases of Saccharomyces cerevisiae. Biochim Biophys Acta 1426(2):275-85	|CWH41 |ROT2
Mutants/Phenotypes Protein Physical Properties Strains/Constructs Substrates/Ligands/Cofactors	Lipari F and Herscovics A (1999) Calcium binding to the class I alpha-1,2-mannosidase from Saccharomyces cerevisiae occurs outside the EF hand motif. Biochemistry 38(3):1111-8
Cellular Location	Massaad MJ, et al. (1999) The processing alpha1,2-mannosidase of Saccharomyces cerevisiae depends on Rer1p for its localization in the endoplasmic reticulum. Eur J Cell Biol 78(7):435-40	|RER1
Non-Fungal Related Genes/Proteins	Nebenfuhr A, et al. (1999) Stop-and-go movements of plant Golgi stacks are mediated by the acto-myosin system. Plant Physiol 121(4):1127-42
Alias Non-Fungal Related Genes/Proteins	Tremblay LO and Herscovics A (1999) Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. Glycobiology 9(10):1073-8
Substrates/Ligands/Cofactors	Jakob CA, et al. (1998) Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 142(5):1223-33	|ALG12 |ALG9 |PRC1 |ROT2
Protein/Nucleic Acid Structure	Dole K, et al. (1997) Crystallization and preliminary X-ray analysis of the class 1 alpha 1,2-mannosidase from Saccharomyces cerevisiae. J Struct Biol 120(1):69-72
Non-Fungal Related Genes/Proteins	Kawar Z, et al. (1997) Isolation and characterization of an alpha 1,2-mannosidase cDNA from the lepidopteran insect cell line Sf9. Glycobiology 7(3):433-43
Cellular Location Function/Process Protein Physical Properties	Burke J, et al. (1996) The Saccharomyces cerevisiae processing alpha 1,2-mannosidase is localized in the endoplasmic reticulum, independently of known retrieval motifs. Eur J Cell Biol 70(4):298-305
Mutants/Phenotypes Strains/Constructs	Knop M, et al. (1996) N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 12(12):1229-38	|CNE1 |PRC1
Function/Process Fungal Related Genes/Proteins Mutants/Phenotypes Protein Physical Properties Protein Sequence Features Strains/Constructs	Lipari F and Herscovics A (1996) Role of the cysteine residues in the alpha1,2-mannosidase involved in N-glycan biosynthesis in Saccharomyces cerevisiae. The conserved Cys340 and Cys385 residues form an essential disulfide bond. J Biol Chem 271(44):27615-22
Reviews	Herscovics A and Orlean P (1993) Glycoprotein biosynthesis in yeast. FASEB J 7(6):540-50	|ALG1 |ALG2 |ALG3 |ALG5 |ALG6 |ALG7 |ALG8 |ANP1 |CWH41 |DPM1 |GDA1 |GFA1 |KRE2 |MNN1 |MORE
Function/Process Mutants/Phenotypes Protein Physical Properties Protein Processing/Modification/Regulation RNA Levels and Processing Strains/Constructs	Puccia R, et al. (1993) Disruption of the processing alpha-mannosidase gene does not prevent outer chain synthesis in Saccharomyces cerevisiae. Biochem J 290 ( Pt 1)():21-6
Function/Process Protein Physical Properties Protein Processing/Modification/Regulation	Grondin B and Herscovics A (1992) Topology of ER processing alpha-mannosidase of Saccharomyces cerevisiae. Glycobiology 2(4):369-72
DNA/RNA Sequence Features Function/Process Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Processing/Modification/Regulation Protein Sequence Features RNA Levels and Processing Strains/Constructs	Camirand A, et al. (1991) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Isolation and characterization of the gene encoding a specific processing alpha-mannosidase. J Biol Chem 266(23):15120-7
Alias Cellular Location Function/Process Protein Physical Properties Regulation of Substrates/Ligands/Cofactors	Jelinek-Kelly S and Herscovics A (1988) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the alpha-mannosidase which removes one specific mannose residue from Man9GlcNAc. J Biol Chem 263(29):14757-63
Function/Process Protein Physical Properties Substrates/Ligands/Cofactors Techniques and Reagents	Saunier B, et al. (1982) Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases. J Biol Chem 257(23):14155-61	|CWH41 |ROT2

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