ID   MAN1_YEAST              Reviewed;        1083 AA.
AC   P22855; D6VTZ5;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Alpha-mannosidase;
DE            EC=3.2.1.24;
DE   AltName: Full=Alpha-D-mannoside mannohydrolase;
GN   Name=AMS1; OrderedLocusNames=YGL156W; ORFNames=G1861;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2675832; DOI=10.1016/0006-291x(89)92308-5;
RA   Yoshihisa T., Anraku Y.;
RT   "Nucleotide sequence of AMS1, the structure gene of vacuolar alpha-
RT   mannosidase of Saccharomyces cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 163:908-915(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8585324; DOI=10.1002/yea.320111409;
RA   James C.M., Indge K.J., Oliver S.G.;
RT   "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT   chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT   PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL   Yeast 11:1413-1419(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=2266133; DOI=10.1016/s0021-9258(18)45721-3;
RA   Yoshihisa T., Anraku Y.;
RT   "A novel pathway of import of alpha-mannosidase, a marker enzyme of
RT   vacuolar membrane, in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 265:22418-22425(1990).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11264288; DOI=10.1074/jbc.m101150200;
RA   Hutchins M.U., Klionsky D.J.;
RT   "Vacuolar localization of oligomeric alpha-mannosidase requires the
RT   cytoplasm to vacuole targeting and autophagy pathway components in
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 276:20491-20498(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=12723970; DOI=10.1042/bj20030384;
RA   Chantret I., Frenoy J.-P., Moore S.E.H.;
RT   "Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles
RT   for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p).";
RL   Biochem. J. 373:901-908(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Degrades free oligosaccharides in the vacuole.
CC       {ECO:0000269|PubMed:12723970}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC         in alpha-D-mannosides.; EC=3.2.1.24;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Composed of isoforms with three constituent polypeptides
CC       described as [(107 kDa)-n (73 kDa)-(6-n) (31 kDa)-(6-n)], where n is 0-
CC       6. The 73 kDa and the 31 kDa polypeptides may be proteolytic
CC       derivatives of the 107 kDa polypeptide in the vacuole. Oligomerizes in
CC       the cytoplasm and retains its oligomeric form during import into the
CC       vacuole.
CC   -!- INTERACTION:
CC       P22855; Q12292: ATG34; NbExp=3; IntAct=EBI-10398, EBI-36362;
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:11264288,
CC       ECO:0000269|PubMed:2266133}. Note=Localizes to the inner surface of the
CC       vacuolar membrane. Under nutrient-rich conditions, the protein is
CC       delivered to the vacuole by the cytoplasm to vacuole targeting (Cvt)
CC       pathway. Under starvation conditions, the protein is localized through
CC       autophagy.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: It is not specific for the 1,2-alpha-mannosidic linkage.
CC   -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR   EMBL; M29146; AAA34423.1; -; Genomic_DNA.
DR   EMBL; Z48618; CAA88536.1; -; Genomic_DNA.
DR   EMBL; Z72678; CAA96868.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07956.1; -; Genomic_DNA.
DR   PIR; S60420; S53048.
DR   RefSeq; NP_011359.1; NM_001181021.1.
DR   PDB; 5JM0; EM; 6.30 A; A=1-1070.
DR   PDBsum; 5JM0; -.
DR   AlphaFoldDB; P22855; -.
DR   EMDB; EMD-8166; -.
DR   SMR; P22855; -.
DR   BioGRID; 33098; 55.
DR   DIP; DIP-5497N; -.
DR   IntAct; P22855; 7.
DR   MINT; P22855; -.
DR   STRING; 4932.YGL156W; -.
DR   CAZy; GH38; Glycoside Hydrolase Family 38.
DR   iPTMnet; P22855; -.
DR   MaxQB; P22855; -.
DR   PaxDb; 4932-YGL156W; -.
DR   PeptideAtlas; P22855; -.
DR   EnsemblFungi; YGL156W_mRNA; YGL156W; YGL156W.
DR   GeneID; 852721; -.
DR   KEGG; sce:YGL156W; -.
DR   AGR; SGD:S000003124; -.
DR   SGD; S000003124; AMS1.
DR   VEuPathDB; FungiDB:YGL156W; -.
DR   eggNOG; KOG4342; Eukaryota.
DR   GeneTree; ENSGT01030000234638; -.
DR   HOGENOM; CLU_003442_0_1_1; -.
DR   InParanoid; P22855; -.
DR   OMA; GQYWDAW; -.
DR   OrthoDB; 2786490at2759; -.
DR   BioCyc; MetaCyc:YGL156W-MONOMER; -.
DR   BioCyc; YEAST:YGL156W-MONOMER; -.
DR   Reactome; R-SCE-8853383; Lysosomal oligosaccharide catabolism.
DR   BioGRID-ORCS; 852721; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P22855; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P22855; Protein.
DR   GO; GO:0034270; C:Cvt complex; IDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IDA:SGD.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019309; P:mannose catabolic process; IMP:SGD.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IMP:SGD.
DR   CDD; cd10812; GH38N_AMII_ScAms1_like; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR041147; GH38_C.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR011682; Glyco_hydro_38_C.
DR   InterPro; IPR015341; Glyco_hydro_38_cen.
DR   InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR   InterPro; IPR000602; Glyco_hydro_38_N.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR   PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF17677; Glyco_hydro38C2; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Glycosidase; Hydrolase; Metal-binding;
KW   Reference proteome; Vacuole; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..1083
FT                   /note="Alpha-mannosidase"
FT                   /id="PRO_0000206910"
FT   ACT_SITE        411
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         411
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         626
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CONFLICT        786
FT                   /note="V -> L (in Ref. 1; AAA34423)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        798
FT                   /note="V -> A (in Ref. 1; AAA34423)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1083 AA;  124499 MW;  624C818040FF5127 CRC64;
     MSSEDIIYDP QFKPVQGIYE NRLRQFIDTG GDYHDLNLPK FYDKKRISLD HDHVKVWWYQ
     VSFERGSSPV SPDKRPSWKS IIERDKKGEL EFREANINQP FGPSWSTTWF KVKISLPEDW
     VKSNEQLLFQ WDCSNEGIVI DPKTLIPVTA FSGGERTEYV LPKTSDGKHF FYIEAGNNGM
     FGCGAGSTIN PPDDNRFFHL RKADIVWPDL DARALYIDFW MLGDAARELP GDSWQKHQAR
     QLGNAVMNLF DPNDRSSVRK CRELLQREYF DSFLESSKVY EQGESQVLTN VYGIGNCHID
     TAWLWPFAET RRKIVRSWSS QCTLMDRFPE YKFVASQAQQ FKWLLEDHPE FFNKVLIPKI
     QQSQFFAVGG TWVENDTNIP SGESLARQFF FGQRFFLKHF GLKSKIFWLP DTFGYSSQMP
     QLCRLSGIDK FLTQKLSWNN INSFPHSTFN WAGIDGSQLL THMPPGNTYT ADSHFGDVLR
     TAKQNKTPEY YGSGLMLYGK GDGGGGPTEE MLQKMRRIRS MNNRNGNVIP KLQVGITVDE
     FYDDILKRTN QGHDLPTWSG ELYFEFHRGT YTSQAQTKKL MRLSEIKLHD LEWIAAKTSV
     LYPDSYKYPS KQINELWENV LLCQFHDVLP GSCIEMVYKY EAVPMLHNVV KECTSLIDKT
     VQFLQSQSKA DLVEMRTLTW SKPEKVSEEC SLNGSYTSSV TGYDDYIVLA NGKLKVIICK
     KTGVITSITD ETLGVEYLDT EHGRNKLGAN QFVIYDDKPL GWQAWDTELY SVNQYKYVTK
     PKKVQVSCNT KEKCAVEVIF QISEKCKIKS VISLNATAVT DAKLSKVDIS TTVENWDARN
     KFLKVEFPVN IRNDFASYET QFGITKRPTH YNTSWDVAKF EVCHHKFADY SEYSKGVSIL
     NDCKYGFSTH GNLMRLSLLR SPKAPDAHAD MGTHEIKYAI YPHRGALSSD TVKLAHEFNY
     CFKYKLPKDI GMNFDDIISI SGDENVILSN IKRGEDDSAV KSNYSLNPRD EQSIVVRVYE
     SLGGESFASL NTTLNLKRIE KVDNLEMKVY KSLTATRDES NHAINRIPIK LRPFEIASFR
     LYF
//