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P22855

- MAN1_YEAST

UniProt

P22855 - MAN1_YEAST

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Protein
Alpha-mannosidase
Gene
AMS1, YGL156W, G1861
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Degrades free oligosaccharides in the vacuole.1 Publication

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi298 – 2981Zinc By similarity
Metal bindingi300 – 3001Zinc By similarity
Active sitei411 – 4111Nucleophile By similarity
Metal bindingi411 – 4111Zinc By similarity
Metal bindingi626 – 6261Zinc By similarity

GO - Molecular functioni

  1. alpha-mannosidase activity Source: SGD
  2. carbohydrate binding Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: SGD
  2. mannose metabolic process Source: InterPro
  3. oligosaccharide catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YGL156W-MONOMER.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-mannosidase (EC:3.2.1.24)
Alternative name(s):
Alpha-D-mannoside mannohydrolase
Gene namesi
Name:AMS1
Ordered Locus Names:YGL156W
ORF Names:G1861
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL156w.
SGDiS000003124. AMS1.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. fungal-type vacuole membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10831082Alpha-mannosidase
PRO_0000206910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP22855.
PaxDbiP22855.
PeptideAtlasiP22855.

Expressioni

Gene expression databases

GenevestigatoriP22855.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
LAP4P149043EBI-10398,EBI-2571

Protein-protein interaction databases

BioGridi33098. 16 interactions.
DIPiDIP-5497N.
IntActiP22855. 8 interactions.
MINTiMINT-484580.
STRINGi4932.YGL156W.

Structurei

3D structure databases

ProteinModelPortaliP22855.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0383.
GeneTreeiENSGT00390000006338.
HOGENOMiHOG000048425.
KOiK01191.
OMAiCHMAPSE.
OrthoDBiEOG79SF5G.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. 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.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22855-1 [UniParc]FASTAAdd to Basket

« Hide

MSSEDIIYDP QFKPVQGIYE NRLRQFIDTG GDYHDLNLPK FYDKKRISLD     50
HDHVKVWWYQ VSFERGSSPV SPDKRPSWKS IIERDKKGEL EFREANINQP 100
FGPSWSTTWF KVKISLPEDW VKSNEQLLFQ WDCSNEGIVI DPKTLIPVTA 150
FSGGERTEYV LPKTSDGKHF FYIEAGNNGM FGCGAGSTIN PPDDNRFFHL 200
RKADIVWPDL DARALYIDFW MLGDAARELP GDSWQKHQAR QLGNAVMNLF 250
DPNDRSSVRK CRELLQREYF DSFLESSKVY EQGESQVLTN VYGIGNCHID 300
TAWLWPFAET RRKIVRSWSS QCTLMDRFPE YKFVASQAQQ FKWLLEDHPE 350
FFNKVLIPKI QQSQFFAVGG TWVENDTNIP SGESLARQFF FGQRFFLKHF 400
GLKSKIFWLP DTFGYSSQMP QLCRLSGIDK FLTQKLSWNN INSFPHSTFN 450
WAGIDGSQLL THMPPGNTYT ADSHFGDVLR TAKQNKTPEY YGSGLMLYGK 500
GDGGGGPTEE MLQKMRRIRS MNNRNGNVIP KLQVGITVDE FYDDILKRTN 550
QGHDLPTWSG ELYFEFHRGT YTSQAQTKKL MRLSEIKLHD LEWIAAKTSV 600
LYPDSYKYPS KQINELWENV LLCQFHDVLP GSCIEMVYKY EAVPMLHNVV 650
KECTSLIDKT VQFLQSQSKA DLVEMRTLTW SKPEKVSEEC SLNGSYTSSV 700
TGYDDYIVLA NGKLKVIICK KTGVITSITD ETLGVEYLDT EHGRNKLGAN 750
QFVIYDDKPL GWQAWDTELY SVNQYKYVTK PKKVQVSCNT KEKCAVEVIF 800
QISEKCKIKS VISLNATAVT DAKLSKVDIS TTVENWDARN KFLKVEFPVN 850
IRNDFASYET QFGITKRPTH YNTSWDVAKF EVCHHKFADY SEYSKGVSIL 900
NDCKYGFSTH GNLMRLSLLR SPKAPDAHAD MGTHEIKYAI YPHRGALSSD 950
TVKLAHEFNY CFKYKLPKDI GMNFDDIISI SGDENVILSN IKRGEDDSAV 1000
KSNYSLNPRD EQSIVVRVYE SLGGESFASL NTTLNLKRIE KVDNLEMKVY 1050
KSLTATRDES NHAINRIPIK LRPFEIASFR LYF 1083
Length:1,083
Mass (Da):124,499
Last modified:February 1, 1996 - v2
Checksum:i624C818040FF5127
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti786 – 7861V → L in AAA34423. 1 Publication
Sequence conflicti798 – 7981V → A in AAA34423. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M29146 Genomic DNA. Translation: AAA34423.1.
Z48618 Genomic DNA. Translation: CAA88536.1.
Z72678 Genomic DNA. Translation: CAA96868.1.
BK006941 Genomic DNA. Translation: DAA07956.1.
PIRiS60420. S53048.
RefSeqiNP_011359.1. NM_001181021.1.

Genome annotation databases

EnsemblFungiiYGL156W; YGL156W; YGL156W.
GeneIDi852721.
KEGGisce:YGL156W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M29146 Genomic DNA. Translation: AAA34423.1 .
Z48618 Genomic DNA. Translation: CAA88536.1 .
Z72678 Genomic DNA. Translation: CAA96868.1 .
BK006941 Genomic DNA. Translation: DAA07956.1 .
PIRi S60420. S53048.
RefSeqi NP_011359.1. NM_001181021.1.

3D structure databases

ProteinModelPortali P22855.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33098. 16 interactions.
DIPi DIP-5497N.
IntActi P22855. 8 interactions.
MINTi MINT-484580.
STRINGi 4932.YGL156W.

Protein family/group databases

CAZyi GH38. Glycoside Hydrolase Family 38.

Proteomic databases

MaxQBi P22855.
PaxDbi P22855.
PeptideAtlasi P22855.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL156W ; YGL156W ; YGL156W .
GeneIDi 852721.
KEGGi sce:YGL156W.

Organism-specific databases

CYGDi YGL156w.
SGDi S000003124. AMS1.

Phylogenomic databases

eggNOGi COG0383.
GeneTreei ENSGT00390000006338.
HOGENOMi HOG000048425.
KOi K01191.
OMAi CHMAPSE.
OrthoDBi EOG79SF5G.

Enzyme and pathway databases

BioCyci YEAST:YGL156W-MONOMER.

Miscellaneous databases

NextBioi 972102.
PROi P22855.

Gene expression databases

Genevestigatori P22855.

Family and domain databases

Gene3Di 1.20.1270.50. 1 hit.
3.20.110.10. 1 hit.
InterProi IPR011013. 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.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view ]
Pfami PF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view ]
SMARTi SM00872. Alpha-mann_mid. 1 hit.
[Graphical view ]
SUPFAMi SSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAN1_YEAST
AccessioniPrimary (citable) accession number: P22855
Secondary accession number(s): D6VTZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

It is not specific for the 1,2-alpha-mannosidic linkage.
Present with 319 molecules/cell in log phase SD medium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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