MAN1_YEAST
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 03-AUG-2022, entry version 175.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 SMR; P22855; -.
DR BioGRID; 33098; 52.
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; P22855; -.
DR PRIDE; P22855; -.
DR EnsemblFungi; YGL156W_mRNA; YGL156W; YGL156W.
DR GeneID; 852721; -.
DR KEGG; sce:YGL156W; -.
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 BioCyc; MetaCyc:YGL156W-MON; -.
DR BioCyc; YEAST:YGL156W-MON; -.
DR Reactome; R-SCE-8853383; Lysosomal oligosaccharide catabolism.
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 Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 3.20.110.10; -; 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 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; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 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
