The new UniProt website is here! Take me to UniProt BETA

UniProtKB - P32906 (MNS1_YEAST)

>sp|P32906|MNS1_YEAST Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MNS1 PE=1 SV=1
MKNSVGISIATIVAIIAAIYYVPWYEHFERKSPGAGEMRDRIESMFLESWRDYSKHGWGY
DVYGPIEHTSHNMPRGNQPLGWIIVDSVDTLMLMYNSSTLYKSEFEAEIQRSEHWINDVL
DFDIDAEVNVFETTIRMLGGLLSAYHLSDVLEVGNKTVYLNKAIDLGDRLALAFLSTQTG
IPYSSINLHSGQAVKNHADGGASSTAEFTTLQMEFKYLAYLTGNRTYWELVERVYEPLYK
NNDLLNTYDGLVPIYTFPDTGKFGASTIRFGSRGDSFYEYLLKQYLLTHETLYYDLYRKS
MEGMKKHLLAQSKPSSLWYIGEREQGLHGQLSPKMDHLVCFMGGLLASGSTEGLSIHEAR
RRPFFSLSLERKSDWDLAKGITDTCYQMYKQSSSGLAPEIVVFNDGNIKQDGWWRSSVGD
FFVKPLDRHNLQRPETVESIMFMYHLSHDHKYREWGAEIATSFFENTCVDCNDPKLRRFT
SLSDCITLPTKKSNNMESFWLAETLKYLYILFLDEFDLTKVVFNTEAHPFPVLDEEILKS
QSLTTGWSL

Entry version 193 (29 Sep 2021)
Sequence version 1 (01 Oct 1993)
Previous versions | rss

Add a publication Feedback

Protein

Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase

Gene

MNS1

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Involved in glycoprotein quality control as it is important for the targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man₉GlcNAc₂ to produce Man₈GlcNAc₂, but at high enzyme concentrations it further trims the carbohydrates to Man₅GlcNAc₂.

1 Publication

Miscellaneous

Present with 8260 molecules/cell in log phase SD medium.1 Publication

Catalytic activityⁱ

4
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁴-(α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A_1,2,3B_1,2,3)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
= 4
β-D-mannose
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A_1,2)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported."
  Herscovics A., Romero P.A., Tremblay L.O.
  Glycobiology 12:14G-15G(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY.
EC:
3.2.1.113
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported."
  Herscovics A., Romero P.A., Tremblay L.O.
  Glycobiology 12:14G-15G(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
4
H₂O
+
N⁴-(α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A_1,2,3B_1,2,3)
N⁴-[α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-L-Asn residue
zoom
=
4
β-D-mannose
zoom
+
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A_1,2)
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-Asn residue
zoom
3
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁴-(α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A_1,2,3B_1,3)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
= 3
β-D-mannose
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A_1,2)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported."
  Herscovics A., Romero P.A., Tremblay L.O.
  Glycobiology 12:14G-15G(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY.
EC:
3.2.1.113
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported."
  Herscovics A., Romero P.A., Tremblay L.O.
  Glycobiology 12:14G-15G(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
3
H₂O
+
N⁴-(α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A_1,2,3B_1,3)
N⁴-{α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-Asn residue
zoom
=
3
β-D-mannose
zoom
+
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A_1,2)
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-Asn residue
zoom

Cofactorⁱ

Ca²⁺1 Publication

Pathwayⁱ: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	399	Proton donorBy similarity		1
Metal bindingⁱ	525	Calcium1 Publication		1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosidase, Hydrolase
Ligand	Calcium, Metal-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:YJR131W-MONOMER
BRENDAⁱ	3.2.1.209, 984
UniPathwayⁱ	UPA00378

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	GH47, Glycoside Hydrolase Family 47

CAZyⁱ

GH47, Glycoside Hydrolase Family 47

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase (EC:3.2.1.1131 Publication) Alternative name(s): ER alpha-1,2-mannosidase Man(9)-alpha-mannosidase
Gene namesⁱ	Name:MNS1 Ordered Locus Names:YJR131W ORF Names:J2110
Organismⁱ	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifierⁱ	559292 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome X

Organism-specific databases

Saccharomyces Genome Database More...SGDⁱ	S000003892, MNS1
VEuPathDBⁱ	FungiDB:YJR131W

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 4	CytoplasmicSequence analysis	4
Transmembraneⁱ	5 – 24	Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST	20
Topological domainⁱ	25 – 354	LumenalSequence analysisAdd BLAST	330

Keywords - Cellular componentⁱ

Endoplasmic reticulum, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

No visible phenotype.1 Publication

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000210319	1 – 549	Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidaseAdd BLAST		549

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	96	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1
Glycosylationⁱ	155	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1
Glycosylationⁱ	224	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1
Disulfide bondⁱ	340 ↔ 385	Combined sources1 Publication
Disulfide bondⁱ	468 ↔ 471	Combined sources1 Publication

Keywords - PTMⁱ

Disulfide bond, Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P32906
PaxDbⁱ	P32906
PRIDEⁱ	P32906

Interactionⁱ

Subunit structureⁱ

Homodimer.

1 Publication

Protein-protein interaction databases

BioGRIDⁱ	33886, 148 interactors
Database of interacting proteins More...DIPⁱ	DIP-1441N
IntActⁱ	P32906, 6 interactors
Molecular INTeraction database More...MINTⁱ	P32906
STRINGⁱ	4932.YJR131W

Miscellaneous databases

RNActⁱ	P32906, protein

RNActⁱ

P32906, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	35 – 56	Combined sources	22
Beta strandⁱ	61 – 64	Combined sources	4
Turnⁱ	65 – 68	Combined sources	4
Beta strandⁱ	69 – 71	Combined sources	3
Helixⁱ	84 – 97	Combined sources	14
Beta strandⁱ	99 – 101	Combined sources	3
Helixⁱ	102 – 118	Combined sources	17
Beta strandⁱ	125 – 129	Combined sources	5
Helixⁱ	130 – 151	Combined sources	22
Helixⁱ	156 – 171	Combined sources	16
Helixⁱ	172 – 175	Combined sources	4
Beta strandⁱ	176 – 180	Combined sources	5
Beta strandⁱ	184 – 187	Combined sources	4
Turnⁱ	188 – 190	Combined sources	3
Helixⁱ	199 – 201	Combined sources	3
Helixⁱ	205 – 208	Combined sources	4
Helixⁱ	212 – 222	Combined sources	11
Helixⁱ	225 – 232	Combined sources	8
Helixⁱ	235 – 242	Combined sources	8
Helixⁱ	244 – 248	Combined sources	5
Beta strandⁱ	253 – 256	Combined sources	4
Turnⁱ	258 – 260	Combined sources	3
Turnⁱ	272 – 274	Combined sources	3
Helixⁱ	275 – 288	Combined sources	14
Helixⁱ	291 – 307	Combined sources	17
Beta strandⁱ	309 – 311	Combined sources	3
Turnⁱ	313 – 315	Combined sources	3
Beta strandⁱ	318 – 320	Combined sources	3
Turnⁱ	324 – 328	Combined sources	5
Beta strandⁱ	334 – 336	Combined sources	3
Helixⁱ	337 – 341	Combined sources	5
Helixⁱ	342 – 351	Combined sources	10
Helixⁱ	356 – 359	Combined sources	4
Helixⁱ	372 – 390	Combined sources	19
Beta strandⁱ	399 – 403	Combined sources	5
Beta strandⁱ	417 – 423	Combined sources	7
Helixⁱ	425 – 427	Combined sources	3
Helixⁱ	435 – 447	Combined sources	13
Helixⁱ	451 – 467	Combined sources	17
Beta strandⁱ	468 – 470	Combined sources	3
Turnⁱ	474 – 476	Combined sources	3
Beta strandⁱ	482 – 489	Combined sources	8
Helixⁱ	498 – 502	Combined sources	5
Helixⁱ	504 – 511	Combined sources	8
Beta strandⁱ	520 – 523	Combined sources	4
Beta strandⁱ	529 – 531	Combined sources	3
Helixⁱ	535 – 540	Combined sources	6

Show more details

3D structure databases

SMRⁱ	P32906
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P32906

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domainⁱ

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG2431, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000155422
HOGENOMⁱ	CLU_003818_3_0_1
InParanoidⁱ	P32906
OMAⁱ	LLDTCYQ

Family and domain databases

Gene3Dⁱ	1.50.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR012341, 6hp_glycosidase-like_sf IPR001382, Glyco_hydro_47 IPR036026, Seven-hairpin_glycosidases
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01532, Glyco_hydro_47, 1 hit
PRINTSⁱ	PR00747, GLYHDRLASE47
SUPFAMⁱ	SSF48225, SSF48225, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P32906-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKNSVGISIA TIVAIIAAIY YVPWYEHFER KSPGAGEMRD RIESMFLESW 
        60         70         80         90        100
RDYSKHGWGY DVYGPIEHTS HNMPRGNQPL GWIIVDSVDT LMLMYNSSTL 
       110        120        130        140        150
YKSEFEAEIQ RSEHWINDVL DFDIDAEVNV FETTIRMLGG LLSAYHLSDV 
       160        170        180        190        200
LEVGNKTVYL NKAIDLGDRL ALAFLSTQTG IPYSSINLHS GQAVKNHADG 
       210        220        230        240        250
GASSTAEFTT LQMEFKYLAY LTGNRTYWEL VERVYEPLYK NNDLLNTYDG 
       260        270        280        290        300
LVPIYTFPDT GKFGASTIRF GSRGDSFYEY LLKQYLLTHE TLYYDLYRKS 
       310        320        330        340        350
MEGMKKHLLA QSKPSSLWYI GEREQGLHGQ LSPKMDHLVC FMGGLLASGS 
       360        370        380        390        400
TEGLSIHEAR RRPFFSLSLE RKSDWDLAKG ITDTCYQMYK QSSSGLAPEI 
       410        420        430        440        450
VVFNDGNIKQ DGWWRSSVGD FFVKPLDRHN LQRPETVESI MFMYHLSHDH 
       460        470        480        490        500
KYREWGAEIA TSFFENTCVD CNDPKLRRFT SLSDCITLPT KKSNNMESFW 
       510        520        530        540 
LAETLKYLYI LFLDEFDLTK VVFNTEAHPF PVLDEEILKS QSLTTGWSL

Length:549

Mass (Da):63,057

Last modified:October 1, 1993 - v1

Checksum:ⁱB85FF351900A9BB2

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱ	40	D → Y.		1
Natural variantⁱ	376	D → L.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M63598 Genomic DNA Translation: AAA34799.1 Z49631 Genomic DNA Translation: CAA89662.1 BK006943 Genomic DNA Translation: DAA08915.1
PIRⁱ	A39345
NCBI Reference Sequences More...RefSeqⁱ	NP_012665.3, NM_001181789.3

Genome annotation databases

EnsemblFungiⁱ	YJR131W_mRNA; YJR131W; YJR131W
GeneIDⁱ	853595
KEGGⁱ	sce:YJR131W

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P32906	alpha-1,2-Mannosidase		YEAS8		549	UniRef100_P32906
alpha-1,2-Mannosidase		SACCK		549
alpha-1,2-Mannosidase		YEASC		549
alpha-1,2-Mannosidase		YEAS6		549
Mannosyl-oligosaccharide 1,2-alpha-mannosidase		Saccharomyces cerevisiae PE-2		549
+3

Protein	Similar proteins		Species	Score	Length	Source
P32906	alpha-1,2-Mannosidase		YEAS8		549	UniRef90_P32906
alpha-1,2-Mannosidase		SACCK		549
alpha-1,2-Mannosidase		YEASC		549
alpha-1,2-Mannosidase		YEAS6		549
Mannosyl-oligosaccharide 1,2-alpha-mannosidase		Saccharomyces cerevisiae PE-2		549
+14

Protein	Similar proteins		Species	Score	Length	Source
P32906	alpha-1,2-Mannosidase		YEAS8		549	UniRef50_P32906
alpha-1,2-Mannosidase		SACCK		549
alpha-1,2-Mannosidase		YEASC		549
alpha-1,2-Mannosidase		YEAS6		549
Mannosyl-oligosaccharide 1,2-alpha-mannosidase		Saccharomyces cerevisiae PE-2		549
+54

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M63598 Genomic DNA Translation: AAA34799.1 Z49631 Genomic DNA Translation: CAA89662.1 BK006943 Genomic DNA Translation: DAA08915.1
PIRⁱ	A39345
RefSeqⁱ	NP_012665.3, NM_001181789.3

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1DL2	X-ray	1.54	A	34-549	[»]
	1G6I	X-ray	1.59	A	1-549	[»]
SMRⁱ	P32906
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	33886, 148 interactors
DIPⁱ	DIP-1441N
IntActⁱ	P32906, 6 interactors
MINTⁱ	P32906
STRINGⁱ	4932.YJR131W

Protein family/group databases

CAZyⁱ	GH47, Glycoside Hydrolase Family 47

CAZyⁱ

GH47, Glycoside Hydrolase Family 47

Proteomic databases

MaxQBⁱ	P32906
PaxDbⁱ	P32906
PRIDEⁱ	P32906

Genome annotation databases

EnsemblFungiⁱ	YJR131W_mRNA; YJR131W; YJR131W
GeneIDⁱ	853595
KEGGⁱ	sce:YJR131W

Organism-specific databases

SGDⁱ	S000003892, MNS1
VEuPathDBⁱ	FungiDB:YJR131W

Phylogenomic databases

eggNOGⁱ	KOG2431, Eukaryota
GeneTreeⁱ	ENSGT00940000155422
HOGENOMⁱ	CLU_003818_3_0_1
InParanoidⁱ	P32906
OMAⁱ	LLDTCYQ

Enzyme and pathway databases

UniPathwayⁱ	UPA00378
BioCycⁱ	MetaCyc:YJR131W-MONOMER
BRENDAⁱ	3.2.1.209, 984

Miscellaneous databases

EvolutionaryTraceⁱ	P32906
Protein Ontology More...PROⁱ	PR:P32906
RNActⁱ	P32906, protein

Family and domain databases

Gene3Dⁱ	1.50.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR012341, 6hp_glycosidase-like_sf IPR001382, Glyco_hydro_47 IPR036026, Seven-hairpin_glycosidases
Pfamⁱ	View protein in Pfam PF01532, Glyco_hydro_47, 1 hit
PRINTSⁱ	PR00747, GLYHDRLASE47
SUPFAMⁱ	SSF48225, SSF48225, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MNS1_YEAST
Accessionⁱ	P32906Primary (citable) accession number: P32906 Secondary accession number(s): D6VWU9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
	Last sequence update:	October 1, 1993
	Last modified:	September 29, 2021
	This is version 193 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
Yeast chromosome X
Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P32906 (MNS1_YEAST)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase

MNS1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein glycosylation

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Endoplasmic reticulum

Endoplasmic reticulum

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: protein glycosylation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ