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P22855 (MAN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-mannosidase

EC=3.2.1.24
Alternative name(s):
Alpha-D-mannoside mannohydrolase
Gene names
Name:AMS1
Ordered Locus Names:YGL156W
ORF Names:G1861
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1083 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades free oligosaccharides in the vacuole. Ref.7

Catalytic activity

Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Composed of isoforms with three constituent polypeptides described as [(107 kDa)-n (73 kDa)-(6-n) (31 kDa)-(6-n)], where n is 0-6. The 73 kDa and the 31 kDa polypeptides may be proteolytic derivatives of the 107 kDa polypeptide in the vacuole. Oligomerizes in the cytoplasm and retains its oligomeric form during import into the vacuole.

Subcellular location

Vacuole. Note: Localizes to the inner surface of the vacuolar membrane. Under nutrient-rich conditions, the protein is delivered to the vacuole by the cytoplasm to vacuole targeting (Cvt) pathway. Under starvation conditions, the protein is localized through autophagy. Ref.5 Ref.6

Post-translational modification

The N-terminus is blocked.

Miscellaneous

It is not specific for the 1,2-alpha-mannosidic linkage.

Present with 319 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LAP4P149043EBI-10398,EBI-2571

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 10831082Alpha-mannosidase
PRO_0000206910

Sites

Active site4111Nucleophile By similarity
Metal binding2981Zinc By similarity
Metal binding3001Zinc By similarity
Metal binding4111Zinc By similarity
Metal binding6261Zinc By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.9

Experimental info

Sequence conflict7861V → L in AAA34423. Ref.1
Sequence conflict7981V → A in AAA34423. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22855 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 624C818040FF5127

FASTA1,083124,499
        10         20         30         40         50         60 
MSSEDIIYDP QFKPVQGIYE NRLRQFIDTG GDYHDLNLPK FYDKKRISLD HDHVKVWWYQ 

        70         80         90        100        110        120 
VSFERGSSPV SPDKRPSWKS IIERDKKGEL EFREANINQP FGPSWSTTWF KVKISLPEDW 

       130        140        150        160        170        180 
VKSNEQLLFQ WDCSNEGIVI DPKTLIPVTA FSGGERTEYV LPKTSDGKHF FYIEAGNNGM 

       190        200        210        220        230        240 
FGCGAGSTIN PPDDNRFFHL RKADIVWPDL DARALYIDFW MLGDAARELP GDSWQKHQAR 

       250        260        270        280        290        300 
QLGNAVMNLF DPNDRSSVRK CRELLQREYF DSFLESSKVY EQGESQVLTN VYGIGNCHID 

       310        320        330        340        350        360 
TAWLWPFAET RRKIVRSWSS QCTLMDRFPE YKFVASQAQQ FKWLLEDHPE FFNKVLIPKI 

       370        380        390        400        410        420 
QQSQFFAVGG TWVENDTNIP SGESLARQFF FGQRFFLKHF GLKSKIFWLP DTFGYSSQMP 

       430        440        450        460        470        480 
QLCRLSGIDK FLTQKLSWNN INSFPHSTFN WAGIDGSQLL THMPPGNTYT ADSHFGDVLR 

       490        500        510        520        530        540 
TAKQNKTPEY YGSGLMLYGK GDGGGGPTEE MLQKMRRIRS MNNRNGNVIP KLQVGITVDE 

       550        560        570        580        590        600 
FYDDILKRTN QGHDLPTWSG ELYFEFHRGT YTSQAQTKKL MRLSEIKLHD LEWIAAKTSV 

       610        620        630        640        650        660 
LYPDSYKYPS KQINELWENV LLCQFHDVLP GSCIEMVYKY EAVPMLHNVV KECTSLIDKT 

       670        680        690        700        710        720 
VQFLQSQSKA DLVEMRTLTW SKPEKVSEEC SLNGSYTSSV TGYDDYIVLA NGKLKVIICK 

       730        740        750        760        770        780 
KTGVITSITD ETLGVEYLDT EHGRNKLGAN QFVIYDDKPL GWQAWDTELY SVNQYKYVTK 

       790        800        810        820        830        840 
PKKVQVSCNT KEKCAVEVIF QISEKCKIKS VISLNATAVT DAKLSKVDIS TTVENWDARN 

       850        860        870        880        890        900 
KFLKVEFPVN IRNDFASYET QFGITKRPTH YNTSWDVAKF EVCHHKFADY SEYSKGVSIL 

       910        920        930        940        950        960 
NDCKYGFSTH GNLMRLSLLR SPKAPDAHAD MGTHEIKYAI YPHRGALSSD TVKLAHEFNY 

       970        980        990       1000       1010       1020 
CFKYKLPKDI GMNFDDIISI SGDENVILSN IKRGEDDSAV KSNYSLNPRD EQSIVVRVYE 

      1030       1040       1050       1060       1070       1080 
SLGGESFASL NTTLNLKRIE KVDNLEMKVY KSLTATRDES NHAINRIPIK LRPFEIASFR 


LYF 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of AMS1, the structure gene of vacuolar alpha-mannosidase of Saccharomyces cerevisiae."
Yoshihisa T., Anraku Y.
Biochem. Biophys. Res. Commun. 163:908-915(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2, PMR1, RCK1, AMS1 and CAL1/CDC43."
James C.M., Indge K.J., Oliver S.G.
Yeast 11:1413-1419(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"A novel pathway of import of alpha-mannosidase, a marker enzyme of vacuolar membrane, in Saccharomyces cerevisiae."
Yoshihisa T., Anraku Y.
J. Biol. Chem. 265:22418-22425(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"Vacuolar localization of oligomeric alpha-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae."
Hutchins M.U., Klionsky D.J.
J. Biol. Chem. 276:20491-20498(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p)."
Chantret I., Frenoy J.-P., Moore S.E.H.
Biochem. J. 373:901-908(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29146 Genomic DNA. Translation: AAA34423.1.
Z48618 Genomic DNA. Translation: CAA88536.1.
Z72678 Genomic DNA. Translation: CAA96868.1.
BK006941 Genomic DNA. Translation: DAA07956.1.
PIRS53048. S60420.
RefSeqNP_011359.1. NM_001181021.1.

3D structure databases

ProteinModelPortalP22855.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33098. 16 interactions.
DIPDIP-5497N.
IntActP22855. 8 interactions.
MINTMINT-484580.
STRING4932.YGL156W.

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

Proteomic databases

PaxDbP22855.
PeptideAtlasP22855.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL156W; YGL156W; YGL156W.
GeneID852721.
KEGGsce:YGL156W.

Organism-specific databases

CYGDYGL156w.
SGDS000003124. AMS1.

Phylogenomic databases

eggNOGCOG0383.
GeneTreeENSGT00390000006338.
HOGENOMHOG000048425.
KOK01191.
OMAYSQRNFL.
OrthoDBEOG79SF5G.

Enzyme and pathway databases

BioCycYEAST:YGL156W-MONOMER.

Gene expression databases

GenevestigatorP22855.

Family and domain databases

Gene3D1.20.1270.50. 1 hit.
3.20.110.10. 1 hit.
InterProIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
[Graphical view]
PfamPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMSSF74650. SSF74650. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Other

NextBio972102.
PROP22855.

Entry information

Entry nameMAN1_YEAST
AccessionPrimary (citable) accession number: P22855
Secondary accession number(s): D6VTZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1996
Last modified: March 19, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries