ATH1_YEAST
ID ATH1_YEAST Reviewed; 1211 AA.
AC P48016; D6W436;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Periplasmic acid trehalase ATH1;
DE EC=3.2.1.28 {ECO:0000269|PubMed:8764988, ECO:0000305|PubMed:19703229, ECO:0000305|PubMed:7502577};
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
GN Name=ATH1; OrderedLocusNames=YPR026W; ORFNames=YP9367.06;
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] OF 130-1211, FUNCTION, CATALYTIC
RP ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=MW303-1B;
RX PubMed=7502577; DOI=10.1002/yea.320111103;
RA Destruelle M., Holzer H., Klionsky D.J.;
RT "Isolation and characterization of a novel yeast gene, ATH1, that is
RT required for vacuolar acid trehalase activity.";
RL Yeast 11:1015-1025(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 368-381 AND 385-396, FUNCTION, CATALYTIC ACTIVITY, AND
RP GLYCOSYLATION.
RX PubMed=8764988; DOI=10.1016/0014-5793(96)00751-x;
RA Alizadeh P., Klionsky D.J.;
RT "Purification and biochemical characterization of the ATH1 gene product,
RT vacuolar acid trehalase, from Saccharomyces cerevisiae.";
RL FEBS Lett. 391:273-278(1996).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8647289; DOI=10.1016/0014-5793(96)00450-4;
RA Nwaka S., Mechler B., Holzer H.;
RT "Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on
RT trehalose.";
RL FEBS Lett. 386:235-238(1996).
RN [6]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, UBIQUITINATION, AND MUTAGENESIS OF
RP LYS-2; LYS-27; LYS-37 AND 49-ASN--TYR-68.
RX PubMed=17475771; DOI=10.1091/mbc.e06-11-0995;
RA Huang J., Reggiori F., Klionsky D.J.;
RT "The transmembrane domain of acid trehalase mediates ubiquitin-independent
RT multivesicular body pathway sorting.";
RL Mol. Biol. Cell 18:2511-2524(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 1-MET--THR-100 AND 47-LEU--LEU-69.
RX PubMed=19703229; DOI=10.1111/j.1742-4658.2009.07227.x;
RA He S., Bystricky K., Leon S., Francois J.M., Parrou J.L.;
RT "The Saccharomyces cerevisiae vacuolar acid trehalase is targeted at the
RT cell surface for its physiological function.";
RL FEBS J. 276:5432-5446(2009).
CC -!- FUNCTION: Periplasmic acid trehalase that catalyzes hydrolysis of the
CC disaccharide trehalose and required for growth on trehalose as carbon
CC source (PubMed:7502577, PubMed:8647289, PubMed:19703229,
CC PubMed:8764988). Growth on trehalose is strictly respiratory (By
CC similarity). {ECO:0000250|UniProtKB:N1P212,
CC ECO:0000269|PubMed:19703229, ECO:0000269|PubMed:7502577,
CC ECO:0000269|PubMed:8647289, ECO:0000269|PubMed:8764988}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC Evidence={ECO:0000269|PubMed:8764988, ECO:0000305|PubMed:19703229,
CC ECO:0000305|PubMed:7502577};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17475771}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:17475771}. Vacuole
CC lumen {ECO:0000269|PubMed:17475771, ECO:0000269|PubMed:19703229}.
CC Periplasm {ECO:0000250|UniProtKB:N1P212}. Note=May exist in the
CC periplasm either as a membrane-bound or as a free protein (By
CC similarity). Vacuolar localization is dependent on the multivesicular
CC body (MVB) sorting pathway (PubMed:17475771). Vacuolar localization
CC appears to be associated with its degradation (PubMed:19703229).
CC {ECO:0000250|UniProtKB:N1P212, ECO:0000269|PubMed:17475771,
CC ECO:0000269|PubMed:19703229}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17475771,
CC ECO:0000269|PubMed:19703229, ECO:0000269|PubMed:8764988}.
CC -!- PTM: Ubiquitinated in the N-terminal region; ubiquitination is not
CC required for vacuolar targeting. {ECO:0000269|PubMed:17475771}.
CC -!- DISRUPTION PHENOTYPE: Abolishes cellular acid trehalase activity
CC (PubMed:7502577, PubMed:19703229). Abolishes growth on trehalose carbon
CC source (PubMed:8647289). {ECO:0000269|PubMed:19703229,
CC ECO:0000269|PubMed:7502577, ECO:0000269|PubMed:8647289}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
CC -!- CAUTION: The functional relevance of vacuolar localization is disputed.
CC {ECO:0000305|PubMed:17475771, ECO:0000305|PubMed:19703229}.
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DR EMBL; X84156; CAA58961.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89280.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95022.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11452.1; -; Genomic_DNA.
DR PIR; S54500; S54500.
DR RefSeq; NP_015351.1; NM_001184123.1.
DR AlphaFoldDB; P48016; -.
DR SMR; P48016; -.
DR BioGRID; 36203; 41.
DR IntAct; P48016; 1.
DR STRING; 4932.YPR026W; -.
DR ChEMBL; CHEMBL2366477; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR iPTMnet; P48016; -.
DR MaxQB; P48016; -.
DR PaxDb; P48016; -.
DR PRIDE; P48016; -.
DR EnsemblFungi; YPR026W_mRNA; YPR026W; YPR026W.
DR GeneID; 856137; -.
DR KEGG; sce:YPR026W; -.
DR SGD; S000006230; ATH1.
DR VEuPathDB; FungiDB:YPR026W; -.
DR eggNOG; KOG4125; Eukaryota.
DR GeneTree; ENSGT00390000006297; -.
DR HOGENOM; CLU_006285_4_0_1; -.
DR InParanoid; P48016; -.
DR OMA; VDYEYHI; -.
DR BioCyc; MetaCyc:YPR026W-MON; -.
DR BioCyc; YEAST:YPR026W-MON; -.
DR BRENDA; 3.2.1.28; 984.
DR PRO; PR:P48016; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P48016; protein.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0030287; C:cell wall-bounded periplasmic space; IDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IMP:SGD.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0015976; P:carbon utilization; IMP:UniProtKB.
DR GO; GO:0005993; P:trehalose catabolic process; IDA:SGD.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Periplasm; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Vacuole.
FT CHAIN 1..1211
FT /note="Periplasmic acid trehalase ATH1"
FT /id="PRO_0000012110"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:19703229"
FT TOPO_DOM 68..1211
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT REGION 70..131
FT /note="Required for cell surface targeting"
FT /evidence="ECO:0000305|PubMed:19703229"
FT ACT_SITE 644
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 513..514
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 711..712
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 972
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 990
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1031
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1064
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 1..100
FT /note="Missing: Abolishes cell surface localization.
FT Abolishes acid trehalase activity."
FT /evidence="ECO:0000269|PubMed:19703229"
FT MUTAGEN 2
FT /note="K->R: Abolishes its ubiquitination; when associated
FT with R-27 and R-37. Normal protein targeting to vacuolar
FT lumen; when associated with R-27 and R-37."
FT /evidence="ECO:0000269|PubMed:17475771"
FT MUTAGEN 27
FT /note="K->R: Abolishes its ubiquitination; when associated
FT with R-27 and R-37. Normal protein targeting to vacuolar
FT lumen; when associated with R-2 and R-37."
FT /evidence="ECO:0000269|PubMed:17475771"
FT MUTAGEN 37
FT /note="K->R: Abolishes its ubiquitination; when associated
FT with R-27 and R-37. Normal protein targeting to vacuolar
FT lumen; when associated with R-2 and R-27."
FT /evidence="ECO:0000269|PubMed:17475771"
FT MUTAGEN 47..69
FT /note="Missing: Abnormal protein expression."
FT /evidence="ECO:0000269|PubMed:19703229"
FT MUTAGEN 49..68
FT /note="NSILLLMMLFLLAIFVTALY->VAILLLMMLFLLAIFVVALF: Protein
FT mislocalized to the vacuolar membrane in a small proportion
FT of cells."
FT /evidence="ECO:0000269|PubMed:17475771"
FT CONFLICT 1168..1211
FT /note="LQVGDKGNTDWRKTRYIVVAVQGVYDDYDDDNKGATIKEIVLND -> FAGG
FT (in Ref. 1; CAA58961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1211 AA; 136921 MW; 34AEC44B0B648DEC CRC64;
MKRIRSLWFN AEASYSNLNN SPSLRNKNST GNNSRSKNYR SFSRFDLINS ILLLMMLFLL
AIFVTALYLT KSSRLTYSHA SRAALFNPLG VISPSLGNHT LNYDPEARES SKKLYELLSD
FNTAYYDDEN MILGSNLFSK NTYSRQPYVA NGYIGSRIPN IGFGYALDTL NFYTDAPGAL
NNGWPLRNHR FAGAFVSDFY CLQPKLNSTN FPELDDVGYS TVISSIPQWT NLQFSLVNDS
KWFNPQNVTL DDVTNYSQNL SMKDGIVTTE LDWLNSQIHV KSEIWAHRHI HPLGVVSLEI
SLNTDHLPSD FDSLDVNIWD ILDFNTSHRT VLHSTGTDEK NNAVFMIVQP DNVPSSNCAI
YSTCTVKYEN STNPINSSES FEEKDVSSNI YNVILTEDQP KIIVHKYVGI MSTEFNKNKE
QQDNTNIGLA KMIALNSKGN YEKLLSSHKR AWYDLYNDAF IEIPSDSLLE MTARSSLFHL
LANTRDYNVS SDRGLPVGVS GLSSDSYGGM VFWDADIWME PALLPFFPNV AQNMNNYRNA
THSQAKLNAE KYGYPGAIYP WTSGKYANCT STGPCVDYEY HINVDVAMAS FSIYLNGHEG
IDDEYLRYTT WPIIKNAAQF FTAYVKYNSS LGLYETYNLT DPDEFANHIN NGAFTNAGIK
TLLKWATDIG NHLGEVVDPK WSEISKDIYI PRSSSNITLE YSGMNSSVEI KQADVTLMVY
PLGYINDESI LNNAIKDLYY YSERQSASGP AMTYPVFVAA AAGLLNHGSS SQSYLYKSVL
PYLRAPFAQF SEQSDDNFLT NGLTQPAFPF LTANGGFLQS ILFGLTGIRY SYEVDPDTKK
INRLLRFNPI ELPLLPGGIA IRNFKYMNQV LDIIIDDHNG TIVHKSGDVP IHIKIPNRSL
IHDQDINFYN GSENERKPNL ERRDVDRVGD PMRMDRYGTY YLLKPKQELT VQLFKPGLNA
RNNIAENKQI TNLTAGVPGD VAFSALDGNN YTHWQPLDKI HRAKLLIDLG EYNEKEITKG
MILWGQRPAK NISISILPHS EKVENLFANV TEIMQNSGND QLLNETIGQL LDNAGIPVEN
VIDFDGIEQE DDESLDDVQA LLHWKKEDLA KLIEQIPRLN FLKRKFVKIL DNVPVSPSEP
YYEASRNQSL IEILPSNRTT FTIDYDKLQV GDKGNTDWRK TRYIVVAVQG VYDDYDDDNK
GATIKEIVLN D
