TREA_SCHPO
ID TREA_SCHPO Reviewed; 735 AA.
AC O42893; P78922; Q9UU37;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytosolic neutral trehalase {ECO:0000305};
DE EC=3.2.1.28 {ECO:0000269|PubMed:12153582, ECO:0000305|PubMed:12943532};
DE AltName: Full=Alpha,alpha-trehalase;
DE AltName: Full=Alpha,alpha-trehalose glucohydrolase;
DE AltName: Full=Neutral trehalase {ECO:0000303|PubMed:9838130};
GN Name=ntp1 {ECO:0000303|PubMed:9838130};
GN ORFNames=SPBC660.07 {ECO:0000312|PomBase:SPBC660.07};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=9838130; DOI=10.1016/s0167-4781(98)00214-0;
RA Soto T., Fernandez J., Dominguez A., Vicente-Soler J., Cansado J.,
RA Gacto M.;
RT "Analysis of the ntp1+ gene, encoding neutral trehalase in the fission
RT yeast Schizosaccharomyces pombe.";
RL Biochim. Biophys. Acta 1443:225-229(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 172-359, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 294-735.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, INDUCTION, AND PHOSPHORYLATION.
RX PubMed=9974219; DOI=10.1006/fgbi.1998.1084;
RA Fernandez J., Soto T., Franco A., Vicente-Soler J., Cansado J., Gacto M.;
RT "Enhancement of neutral trehalase activity by oxidative stress in the
RT fission yeast Schizosaccharomyces pombe.";
RL Fungal Genet. Biol. 25:79-86(1998).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9495778; DOI=10.1128/jb.180.5.1342-1345.1998;
RA Cansado J., Soto T., Fernandez J., Vicente-Soler J., Gacto M.;
RT "Characterization of mutants devoid of neutral trehalase activity in the
RT fission yeast Schizosaccharomyces pombe: partial protection from heat shock
RT and high-salt stress.";
RL J. Bacteriol. 180:1342-1345(1998).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11094289; DOI=10.1111/j.1574-6968.2000.tb09412.x;
RA Beltran F.F., Castillo R., Vicente-Soler J., Cansado J., Gacto M.;
RT "Role for trehalase during germination of spores in the fission yeast
RT Schizosaccharomyces pombe.";
RL FEMS Microbiol. Lett. 193:117-121(2000).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH
RP TPP1 AND TPS1, AND INTERACTION WITH TPP1 AND TPS1.
RX PubMed=12153582; DOI=10.1046/j.1432-1033.2002.03082.x;
RA Soto T., Franco A., Padmanabhan S., Vicente-Soler J., Cansado J., Gacto M.;
RT "Molecular interaction of neutral trehalase with other enzymes of trehalose
RT metabolism in the fission yeast Schizosaccharomyces pombe.";
RL Eur. J. Biochem. 269:3847-3855(2002).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, IDENTIFICATION IN A
RP COMPLEX WITH TPS1, INTERACTION WITH TPS1, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ASP-97; ARG-100 AND ASP-108.
RX PubMed=12943532; DOI=10.1042/bj20030825;
RA Franco A., Soto T., Vicente-Soler J., Paredes V., Madrid M., Gacto M.,
RA Cansado J.;
RT "A role for calcium in the regulation of neutral trehalase activity in the
RT fission yeast Schizosaccharomyces pombe.";
RL Biochem. J. 376:209-217(2003).
RN [10]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH TPS1, INTERACTION WITH TPS1,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-6; SER-41; SER-51 AND SER-71.
RX PubMed=15965643; DOI=10.1007/s00203-005-0005-4;
RA Franco A., Soto T., Madrid M., Vicente-Soler J., Gacto M., Cansado J.;
RT "Functional characterization of Schizosaccharomyces pombe neutral trehalase
RT altered in phosphorylatable serine residues.";
RL Arch. Microbiol. 183:394-400(2005).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; SER-49; THR-50 AND
RP SER-51, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Hydrolyzes intracellular trehalose to glucose
CC (PubMed:12153582). The disaccharide trehalose serves as a storage
CC carbohydrate that is mobilized during nutrient stress and spore
CC germination (PubMed:11094289). Together with tps1, regulates the level
CC of trehalose as a protectant for cell integrity during heat, osmotic
CC and oxidative stresses (PubMed:9495778, PubMed:9974219,
CC PubMed:12943532, PubMed:15965643). {ECO:0000269|PubMed:11094289,
CC ECO:0000269|PubMed:12153582, ECO:0000269|PubMed:12943532,
CC ECO:0000269|PubMed:15965643, ECO:0000269|PubMed:9495778,
CC ECO:0000269|PubMed:9974219}.
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:12153582, ECO:0000305|PubMed:12943532};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12943532};
CC -!- ACTIVITY REGULATION: May be activated by phosphorylation.
CC {ECO:0000269|PubMed:9974219}.
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer (PubMed:12153582) (Probable). Homotrimer
CC (PubMed:12153582) (Probable). Oligomerization occurs only in the
CC presence of calcium (PubMed:12153582). Forms a complex composed of at
CC least tpp1, tps1 and ntp1 (PubMed:12153582, PubMed:12943532,
CC PubMed:15965643). Interacts with tpp1 (PubMed:12153582). Interacts with
CC tps1; interaction is independent of stress conditions and
CC oligomerization state (PubMed:12153582, PubMed:12943532,
CC PubMed:15965643). {ECO:0000269|PubMed:12153582,
CC ECO:0000269|PubMed:12943532, ECO:0000269|PubMed:15965643,
CC ECO:0000305|PubMed:12943532}.
CC -!- INTERACTION:
CC O42893; P78875: tpp1; NbExp=2; IntAct=EBI-26616855, EBI-26616958;
CC O42893; P40387: tps1; NbExp=3; IntAct=EBI-26616855, EBI-26616873;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: Induced by thermal stress and osmotic stress
CC (PubMed:9495778). Induced by oxidative stress (PubMed:9974219).
CC {ECO:0000269|PubMed:9495778, ECO:0000269|PubMed:9974219}.
CC -!- DISRUPTION PHENOTYPE: Increases cellular trehalase level during osmotic
CC stress and thermal stress (PubMed:12943532, PubMed:15965643). Resistant
CC to heat shock and osmotic stress (PubMed:9495778). Delays spore
CC germination (PubMed:11094289). {ECO:0000269|PubMed:11094289,
CC ECO:0000269|PubMed:12943532, ECO:0000269|PubMed:15965643,
CC ECO:0000269|PubMed:9495778}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13934.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ224339; CAA11904.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22527.1; -; Genomic_DNA.
DR EMBL; AB027837; BAA87141.1; -; Genomic_DNA.
DR EMBL; D89273; BAA13934.1; ALT_FRAME; mRNA.
DR PIR; T40619; T40619.
DR PIR; T43203; T43203.
DR RefSeq; NP_595086.1; NM_001020993.2.
DR AlphaFoldDB; O42893; -.
DR SMR; O42893; -.
DR BioGRID; 277630; 37.
DR ComplexPortal; CPX-6423; Trehalose-6-phosphate synthase/phosphatase complex.
DR IntAct; O42893; 2.
DR STRING; 4896.SPBC660.07.1; -.
DR CAZy; GH37; Glycoside Hydrolase Family 37.
DR iPTMnet; O42893; -.
DR MaxQB; O42893; -.
DR PaxDb; O42893; -.
DR PRIDE; O42893; -.
DR EnsemblFungi; SPBC660.07.1; SPBC660.07.1:pep; SPBC660.07.
DR GeneID; 2541115; -.
DR KEGG; spo:SPBC660.07; -.
DR PomBase; SPBC660.07; ntp1.
DR VEuPathDB; FungiDB:SPBC660.07; -.
DR eggNOG; KOG0602; Eukaryota.
DR HOGENOM; CLU_006451_1_1_1; -.
DR InParanoid; O42893; -.
DR OMA; GLERPNR; -.
DR PhylomeDB; O42893; -.
DR PRO; PR:O42893; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0004555; F:alpha,alpha-trehalase activity; IDA:PomBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:PomBase.
DR GO; GO:0030437; P:ascospore formation; IMP:PomBase.
DR GO; GO:0005992; P:trehalose biosynthetic process; IC:ComplexPortal.
DR GO; GO:0005993; P:trehalose catabolic process; IDA:ComplexPortal.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IC:ComplexPortal.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001661; Glyco_hydro_37.
DR InterPro; IPR018232; Glyco_hydro_37_CS.
DR InterPro; IPR011120; Trehalase_Ca-bd.
DR PANTHER; PTHR23403; PTHR23403; 1.
DR Pfam; PF01204; Trehalase; 1.
DR Pfam; PF07492; Trehalase_Ca-bi; 1.
DR PRINTS; PR00744; GLHYDRLASE37.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS00927; TREHALASE_1; 1.
DR PROSITE; PS00928; TREHALASE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Glycosidase; Hydrolase; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..735
FT /note="Cytosolic neutral trehalase"
FT /id="PRO_0000173797"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 457
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT ACT_SITE 652
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P32356"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 290..291
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 336..338
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13482"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 6
FT /note="S->A: Abolishes activation during osmotic stress and
FT thermal stress. Increases cellular trehalose level during
FT osmotic stress but not thermal stress. Does not affect
FT binding to tps1."
FT /evidence="ECO:0000269|PubMed:15965643"
FT MUTAGEN 41
FT /note="S->A: Decreases activation during osmotic stress and
FT thermal stress. Increases cellular trehalose level during
FT osmotic stress but not thermal stress. Does not affect
FT binding to tps1."
FT /evidence="ECO:0000269|PubMed:15965643"
FT MUTAGEN 51
FT /note="S->A: Abolishes activation during osmotic stress and
FT thermal stress. Increases cellular trehalose level during
FT osmotic stress but not thermal stress. Does not affect
FT binding to tps1."
FT /evidence="ECO:0000269|PubMed:15965643"
FT MUTAGEN 71
FT /note="S->A,D: Abolishes activation and increases cellular
FT trehalose level during osmotic stress and thermal stress.
FT Does not affect binding to tps1."
FT /evidence="ECO:0000269|PubMed:15965643"
FT MUTAGEN 97
FT /note="D->L: Abolishes calcium binding. Abolishes
FT activation and increases cellular trehalose level during
FT osmotic stress and thermal stress."
FT /evidence="ECO:0000269|PubMed:12943532"
FT MUTAGEN 100
FT /note="R->L: Decreases calcium binding. Decreases
FT activation and increases cellular trehalose level during
FT osmotic stress and thermal stress. Does not affect binding
FT to tps1."
FT /evidence="ECO:0000269|PubMed:12943532"
FT MUTAGEN 108
FT /note="D->L: Abolishes calcium binding. Abolishes
FT activation and increases cellular trehalose level during
FT osmotic stress and thermal stress. Does not affect binding
FT to tps1."
FT /evidence="ECO:0000269|PubMed:12943532"
SQ SEQUENCE 735 AA; 84603 MW; 73FF979534E91BD4 CRC64;
MPSKFSSKYV DTEAISNDDD NPFATAKSYY SKDTDLSTRV SAGRPRTLST SMEASAAPTI
PELKNLRRRG SLDEHKQPRK FLVDVDKTLN ALLESEDTDR NMQITIEDTG PKVVSLGSAS
SGGYRLYELR GTYQLSNLLQ ELTLAKDYGR RYILLDERRL NENPVNRLSR LIKGTFWDAL
TRRIDASVLD VICRDTKDRS GSHVNRIYVP KAEQEMYEYY VRAAKERPYL NLQVEYLPEE
ITPEWVRDVN DKPGLLALAM EKYQDDEGNT HLRGVPFVVP GGRFNELYGW DSYFESLGLL
VDDRVDLAKG MVENFIFEIT YYGKILNANR TYYLLRSQPP FLTDMALRVY ERIKNEEGSL
DFLHRAFSAT IKEYHTVWTA TPRLDPKTGL SRYRPGGLGI PPETEASHFE HLLRPYMEKY
HMTLEEFTHA YNYQQIHEPA LDEYFVHDRA VRESGHDTTY RLEKVCADLA TVDLNSLLYK
YETDISHVIL EYFDDKFVLP NGTIETSAIW DRRARARRAA MEKYLWSEAD SMWYDYNTKL
ETKSTYESAT AFWALWAGVA TPRQAAKFVD VSLPKFEVAG GIVAGTKRSL GKVGLDNPSR
QWDYPNGWSP QQILAWYGLI RYGYEEETRR LVYRWLYTIT KSFVDFNGIV VEKYDLTRPV
DPHRVEAEYG NQGVNIKGVA REGFGWVNAS YEVGLTFCNS HMRRALGACT TPDVFFAGIK
EESLPAFENL SIHKN
