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P22855

- MAN1_YEAST

UniProt

P22855 - MAN1_YEAST

Protein

Alpha-mannosidase

Gene

AMS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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 – 2981ZincBy similarity
    Metal bindingi300 – 3001ZincBy similarity
    Active sitei411 – 4111NucleophileBy similarity
    Metal bindingi411 – 4111ZincBy similarity
    Metal bindingi626 – 6261ZincBy 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

    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 2 Publications
    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.

    GO - Cellular componenti

    1. fungal-type vacuole membrane Source: SGD

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 10831082Alpha-mannosidasePRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 38 family.Curated

    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

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    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti786 – 7861V → L in AAA34423. (PubMed:2675832)Curated
    Sequence conflicti798 – 7981V → A in AAA34423. (PubMed:2675832)Curated

    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

    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: October 1, 2014
    This is version 121 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.1 Publication

    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