ID   TSC10_NEUCR             Reviewed;         362 AA.
AC   Q7RZR2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 3.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=3-ketodihydrosphingosine reductase gsl-3;
DE            EC=1.1.1.102;
DE   AltName: Full=3-dehydrosphinganine reductase;
DE   AltName: Full=KDS reductase;
GN   Name=gsl-3; Synonyms=tsc10; ORFNames=NCU00302;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to
CC       dihydrosphingosine (DHS). {ECO:0000250}.
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;
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       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; CM002238; EAA28537.3; -; Genomic_DNA.
DR   RefSeq; XP_957773.3; XM_952680.3.
DR   AlphaFoldDB; Q7RZR2; -.
DR   SMR; Q7RZR2; -.
DR   STRING; 5141.EFNCRP00000000359; -.
DR   EnsemblFungi; EAA28537; EAA28537; NCU00302.
DR   GeneID; 3873943; -.
DR   KEGG; ncr:NCU00302; -.
DR   VEuPathDB; FungiDB:NCU00302; -.
DR   HOGENOM; CLU_010194_3_0_1; -.
DR   InParanoid; Q7RZR2; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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:0047560; F:3-dehydrosphinganine reductase activity; IBA:GO_Central.
DR   GO; GO:0006666; P:3-keto-sphinganine metabolic process; IBA:GO_Central.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
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; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW   Reference proteome; Sphingolipid metabolism; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..362
FT                   /note="3-ketodihydrosphingosine reductase gsl-3"
FT                   /id="PRO_0000054798"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        216
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000250"
FT   BINDING         55..79
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  39647 MW;  8DBEF2B625E6FC67 CRC64;
     MNHYLFSESL MEQLKTLSTS WSLPVAAVVA AIGIFATMGL FSSKNHMPVE GRTVLLTGAS
     EGMGRSAAIQ LSQKGANVIL VSRNVGRLEE ALVDVRAAAK NPSTQRFTYI SADVSEHDYA
     AAVLAEAIAW NGGRSPDIVW CVAGMSTPLL WTDDGSMAAA RRNMDVNYFG SAEMSRAILR
     EWLAPENSTG PNGEPKHLVF TASMLALFAI LGYGPYTPTK WALRGLADTL AMEVNYYPDN
     PVKVHIVYPG TIVSPGYERE NQTKPDITVE LEKDEPAESP DTVARRAIAG LEAGKYFVDV
     SFLGRLMQCG IMGGSPRNNW VLDTLMGWLI PIIYFFVLRG MNSTIVKWAR EKGHPFTHPK
     KK