TSC10_YEAST
ID TSC10_YEAST Reviewed; 320 AA.
AC P38342; D6VQR2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=3-ketodihydrosphingosine reductase TSC10 {ECO:0000303|PubMed:9804843};
DE EC=1.1.1.102 {ECO:0000269|PubMed:9804843};
DE AltName: Full=3-dehydrosphinganine reductase {ECO:0000303|PubMed:9804843};
DE AltName: Full=KDS reductase {ECO:0000303|PubMed:9804843};
DE AltName: Full=Temperature-sensitive CSG2 suppressor protein 10 {ECO:0000303|PubMed:9804843};
GN Name=TSC10 {ECO:0000303|PubMed:9804843}; OrderedLocusNames=YBR265W;
GN ORFNames=YBR1734;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 255.
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9804843; DOI=10.1074/jbc.273.46.30688;
RA Beeler T., Bacikova D., Gable K., Hopkins L., Johnson C., Slife H.,
RA Dunn T.;
RT "The Saccharomyces cerevisiae TSC10/YBR265w gene encoding 3-ketosphinganine
RT reductase is identified in a screen for temperature-sensitive suppressors
RT of the Ca2+-sensitive csg2Delta mutant.";
RL J. Biol. Chem. 273:30688-30694(1998).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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).
CC -!- FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to
CC dihydrosphingosine (DHS). {ECO:0000269|PubMed:9804843}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH;
CC Xref=Rhea:RHEA:22640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57817, ChEBI:CHEBI:58299, ChEBI:CHEBI:58349;
CC EC=1.1.1.102; Evidence={ECO:0000269|PubMed:9804843};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:9804843}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 7700 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; X70529; CAA49930.1; -; Genomic_DNA.
DR EMBL; Z36134; CAA85228.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07382.2; -; Genomic_DNA.
DR PIR; S32966; S32966.
DR RefSeq; NP_009824.2; NM_001178613.2.
DR AlphaFoldDB; P38342; -.
DR SMR; P38342; -.
DR BioGRID; 32961; 137.
DR DIP; DIP-4781N; -.
DR IntAct; P38342; 5.
DR MINT; P38342; -.
DR STRING; 4932.YBR265W; -.
DR SwissLipids; SLP:000001843; -.
DR iPTMnet; P38342; -.
DR MaxQB; P38342; -.
DR PaxDb; P38342; -.
DR PRIDE; P38342; -.
DR EnsemblFungi; YBR265W_mRNA; YBR265W; YBR265W.
DR GeneID; 852568; -.
DR KEGG; sce:YBR265W; -.
DR SGD; S000000469; TSC10.
DR VEuPathDB; FungiDB:YBR265W; -.
DR eggNOG; KOG1210; Eukaryota.
DR GeneTree; ENSGT00940000156961; -.
DR HOGENOM; CLU_010194_3_0_1; -.
DR InParanoid; P38342; -.
DR OMA; GAHPNEP; -.
DR BioCyc; MetaCyc:YBR265W-MON; -.
DR BioCyc; YEAST:YBR265W-MON; -.
DR Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR PRO; PR:P38342; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38342; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0047560; F:3-dehydrosphinganine reductase activity; IDA:SGD.
DR GO; GO:0006666; P:3-keto-sphinganine metabolic process; IDA:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IDA:SGD.
DR CDD; cd08939; KDSR-like_SDR_c; 1.
DR InterPro; IPR045022; KDSR-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 2.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; NAD; NADP;
KW Oxidoreductase; Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..320
FT /note="3-ketodihydrosphingosine reductase TSC10"
FT /id="PRO_0000054800"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 14..18
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:P40471"
FT ACT_SITE 16
FT /note="Nucleophile; for lipase activity"
FT /evidence="ECO:0000250|UniProtKB:P40471"
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 11..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 73..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 180..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 211..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT CONFLICT 255
FT /note="D -> E (in Ref. 1; CAA49930 and 2; CAA85228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35973 MW; C5F251B4099E6242 CRC64;
MKFTLEDQVV LITGGSQGLG KEFAKKYYNE AENTKIIIVS RSEARLLDTC NEIRIEAHLR
RETTDEGQVQ HKLAAPLDLE QRLFYYPCDL SCYESVECLF NALRDLDLLP TQTLCCAGGA
VPKLFRGLSG HELNLGMDIN YKTTLNVAHQ IALAEQTKEH HLIIFSSATA LYPFVGYSQY
APAKAAIKSL VAILRQELTN FRISCVYPGN FESEGFTVEQ LTKPEITKLI EGPSDAIPCK
QACDIIAKSL ARGDDDVFTD FVGWMIMGMD LGLTAKKSRF VPLQWIFGVL SNILVVPFYM
VGCSWYIRKW FRENDGKKAN
