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MNL1/YHR204W 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   ChrVIII: 506319 to 508709 CDS: 506319 - 508709 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
MNL1	YHR204W	HTM1	ORF, Verified	S000001247
This name is reserved with SGD according to the Gene Naming Guidelines agreed upon by the yeast community. Gene name reserved on: 2000-11-09. Gene name expires on 2001-11-09.
Description
alpha-1,2-specific exomannosidase of the endoplasmic reticulum that generates a Man7GlcNac2 oligosaccharide signal on glycoproteins destined for ubiquitin-proteasome degradation

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 carbohydrate binding Jakob CA, et al. (2001) Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast. EMBO Rep 2(5):423-30        ISS : Inferred from Sequence or structural Similarity IMP : Inferred from Mutant Phenotype Assigned on 2002-08-20 SGD mannosyl-oligosaccharide 1,2-alpha-mannosidase activity 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 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            IMP : Inferred from Mutant Phenotype Assigned on 2010-02-05 SGD
Biological Process Annotation(s) Reference(s) Evidence Assigned By ER-associated protein catabolic process 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        IMP : Inferred from Mutant Phenotype Assigned on 2002-08-20 SGD Jakob CA, et al. (2001) Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast. EMBO Rep 2(5):423-30        IMP : Inferred from Mutant Phenotype Assigned on 2002-08-20 SGD response to unfolded protein GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0834 Assigned on 2009-05-05 UniProtKB
Cellular Component Annotation(s) Reference(s) Evidence Assigned By endoplasmic reticulum GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0256 Assigned on 2009-05-05 UniProtKB endoplasmic reticulum lumen 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-0096 Assigned on 2009-05-06 UniProtKB Sakoh-Nakatogawa M, et al. (2009) Roles of Protein-disulfide Isomerase-mediated Disulfide Bond Formation of Yeast Mnl1p in Endoplasmic Reticulum-associated Degradation. J Biol Chem 284(18):11815-25        IDA : Inferred from Direct Assay Assigned on 2009-05-01 SGD 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

Pathways [TOP] [NEXT]
No pathways available

Summary Paragraph [TOP] [NEXT]
No summary paragraph available

Basic References [TOP]

BASIC INFORMATION REFERENCES forMNL1/YHR204W for MNL1 1) Jakob CA, et al. (2001) Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast. EMBO Rep 2(5):423-30        2) 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        3) 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

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for MNL1/YHR204W

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for MNL1/YHR204W

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 MVCCLWV C-term IINLFIV Length(aa) 796 MW(Da) 91,245 pI 4.82 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.043   Codon Adaptation Index 0.137   Frequency of Optimal Codons 0.430   Hydropathicity of Protein -0.205   Aromaticity Score 0.127

10 20 30 40 50 | | | | | MVCCLWVLLALLLHLDHVACEDDAYSFTSKELKAYKQEVKELFYFGFDNY LEHGYPYDEVKPISCVPKKRNFEDPTDQGTNDILGNFTITLIDSLTTIAI LEDRPQFLKAVRLVERTFPDGNFDIDSTIQVFEITIRVIGSLLSSHLYAT DPTKAVYLGDDYDGSLLRLAQNMADRLLPAYLTSTGLPMPRRNIKRKWDV SEFPEFLETENNVAAMASPMFEFTILSYLTGDPKYEKVTRYAFDKTWSLR TGLDLLPMSFHPEKLTPYTPMTGIGASIDSLFEYALKGAILFDDSELMEV WNVAYEALKTNCKNDWFFANVMADTGHLFVPWIDSLSAFFSGLQVLAGDL DDAIANHLMFLKMWNTFGGIPERWNFSPPEFPPLSPLERSGAVALDNILP LEWYPLRPEFFESTYFLYRATKDPFYLNIGVHLLKDLKQRFKSNCGFAGF QNVITGELQDRMETFVLSETLKYLYLLFDEENELHNSASDVIFSTEAHPM WLPQEVRSNYKRNAKFNNSVYSSHLEICQKKDREQAGENTLSQRIVGFAK SIFHKGPPDEEATDPIIDYTIDTELPGTCSIKPHHVIGDEFWYSPMLSNF DRLFEIDSRFAATLIKPSHMHNYNAIELEPGFYNRWSNPQFSTCLIPPTT EIFELLFDLPGYHQLNPLMLENKTITFETFGGRSRLKIEKLQIYQIDYYG DLITASTFQDVSRKDIFSNACDAVASLYSPTYLYRVVAINGRILPRHGSV QIKKHSPVLTSNGTREEDEFKMDGIGINDHSQLMLECTPIINLFIV*

Protein Structures from PDB: proteins of known structure with sequence similarity to MNL1/YHR204W, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to MNL1 Homolog Source (per PDB) Protein Alignment: MNL1 vs. Homolog External Links P-Value %Identical %Similar Alignment 1fo2 ( Chain: A) Crystal structure of human class i alpha1,2-mannosidase in complex with 1-deoxymannojirimycin PDB_Info PDB_Structure Homo sapiens 2.8e-28 29 30 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 2.8e-28 29 30 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 3.7e-28 29 30 View alignment SCOP MMDB CATH 1fmi ( Chain: A) Crystal structure of human class i alpha1,2-mannosidase PDB_Info PDB_Structure Homo sapiens 1.3e-27 29 30 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 2.6e-27 27 32 View alignment SCOP MMDB CATH 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 2.8e-22 26 29 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 3.1e-22 26 29 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 = 3.3e-20 26 30 View alignment SCOP MMDB CATH Chain D = 3.3e-20 26 30 View alignment Chain B = 3.3e-20 26 30 View alignment Chain C = 3.3e-20 26 30 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 = 5.8e-19 25 30 View alignment SCOP MMDB CATH Chain A = 5.8e-19 25 30 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 = 5.8e-19 25 30 View alignment SCOP MMDB CATH Chain B = 5.8e-19 25 30 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 = 5.8e-19 25 30 View alignment SCOP MMDB CATH Chain A = 5.8e-19 25 30 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-19 25 30 View alignment SCOP MMDB CATH Chain A = 6.0e-19 25 30 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-19 25 30 View alignment SCOP MMDB CATH Chain A = 6.0e-19 25 30 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	Date Standardized	Reference
MNL1	2001-04-17	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

Alias Name(s)	Reference
HTM1	Jakob CA, et al. (2001) Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast. EMBO Rep 2(5):423-30

Nomenclature History Notes

Date	Note
2001-04-17	The locus YHR204W was initially reserved under the name "HTM1" but was first published under the name "MNL1"

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
YHR204W	SGD Systematic Sequence
856611	NCBI: Gene ID
NP_012074.1	NCBI: RefSeq protein version ID
NP_012074.1	NCBI: RefSeq protein version ID
6321998	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
23 curated references; 0 references not yet curated
Reviews	Yoshida Y and Tanaka K (2010) Lectin-like ERAD players in ER and cytosol. Biochim Biophys Acta 1800(2):172-180	|PNG1 |YOS9
Alias Function/Process Genetic Interactions Mutants/Phenotypes Protein Physical Properties Protein Sequence Features Protein-protein Interactions Strains/Constructs Substrates/Ligands/Cofactors	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 |MNS1 |PDI1 |PRC1 |ROT2 |YOS9
Cellular Location	Sakoh-Nakatogawa M, et al. (2009) Roles of Protein-disulfide Isomerase-mediated Disulfide Bond Formation of Yeast Mnl1p in Endoplasmic Reticulum-associated Degradation. J Biol Chem 284(18):11815-25	|PDI1
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 |MNS1 |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
Mutants/Phenotypes Strains/Constructs	Quan EM, et al. (2008) Defining the glycan destruction signal for endoplasmic reticulum-associated degradation. Mol Cell 32(6):870-7	|ALG12 |ALG9 |YOS9
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
Alias Function/Process 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 |MNS1 |YOS9
Reviews	Jones J, et al. (2005) Controlling N-linked glycan site occupancy. Biochim Biophys Acta 1726(2):121-37	|OST1 |OST2 |OST3 |OST4 |OST5 |OST6 |STT3 |SWP1 |WBP1
Alias Function/Process Genetic Interactions Mutants/Phenotypes	Kim W, et al. (2005) Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell 19(6):753-64	|CUE1 |DER1 |YOS9
Function/Process Mutants/Phenotypes Strains/Constructs	Kostova Z and Wolf DH (2005) Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation. J Cell Sci 118(Pt 7):1485-92	|CNE1 |PRC1
Mutants/Phenotypes Strains/Constructs Substrates/Ligands/Cofactors	Spear ED and Ng DT (2005) Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation. J Cell Biol 169(1):73-82	|PRC1
Alias Function/Process Genetic Interactions 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 |MNS1 |PRC1 |YOS9
Cellular Location Function/Process	Buschhorn BA, et al. (2004) A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins. FEBS Lett 577(3):422-6	|YOS9
Cross-species Expression Disease Gene Related Function/Process Genetic Interactions Mutants/Phenotypes Non-Fungal Related Genes/Proteins Strains/Constructs	Gnann A, et al. (2004) Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast. Mol Biol Cell 15(9):4125-35	|CDC48 |HRD1 |NPL4 |SSM4 |UFD1
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
Alias Cellular Location Function/Process Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Sequence Features Strains/Constructs	Vashist S and Ng DT (2004) Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J Cell Biol 165(1):41-52
Cellular Location Protein Processing/Modification/Regulation	De Groot PW, et al. (2003) Genome-wide identification of fungal GPI proteins. Yeast 20(9):781-96	|CCW14 |CWP2 |DDR2 |DFG5 |DSE2 |DSE4 |ECM33 |FIT1 |FIT2 |HOR7 |PGU1 |PLB3 |SHE10 |YAR066W |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 |MNS1 |SEC61 |UBC7
Cellular Location Mutants/Phenotypes Strains/Constructs Techniques and Reagents	Terashima H, et al. (2002) Sequence-based approach for identification of cell wall proteins in Saccharomyces cerevisiae. Curr Genet 40(5):311-6	|CWC23 |DIA3 |DSE2 |DSE4 |EAR1 |ERJ5 |GRX7 |HPF1 |PAN5 |PGU1 |PRY1 |PRY2 |SLP1 |SPC25 |MORE
Function/Process Fungal Related Genes/Proteins Mutants/Phenotypes Strains/Constructs	Jakob CA, et al. (2001) Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast. EMBO Rep 2(5):423-30	|PDR5 |SEC61 |STT3 |UBC6
Cellular Location Function/Process Fungal Related Genes/Proteins Mutants/Phenotypes Protein Sequence Features Strains/Constructs	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	|MNS1
Reviews	Hauri H, et al. (2000) Lectins and traffic in the secretory pathway. FEBS Lett 476(1-2):32-7	|PRC1 |SEC13 |SEC23 |SEC24 |SEC31

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