ID   KDSR_BOVIN              Reviewed;         331 AA.
AC   Q2KIJ5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=3-ketodihydrosphingosine reductase;
DE            Short=KDS reductase;
DE            EC=1.1.1.102;
DE   AltName: Full=3-dehydrosphinganine reductase;
DE   AltName: Full=Follicular variant translocation protein 1 homolog;
DE            Short=FVT-1;
DE   Flags: Precursor;
GN   Name=KDSR; Synonyms=FVT1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; BC112615; AAI12616.1; -; mRNA.
DR   RefSeq; NP_001039384.1; NM_001045919.1.
DR   AlphaFoldDB; Q2KIJ5; -.
DR   SMR; Q2KIJ5; -.
DR   STRING; 9913.ENSBTAP00000010155; -.
DR   PaxDb; Q2KIJ5; -.
DR   GeneID; 505558; -.
DR   KEGG; bta:505558; -.
DR   CTD; 2531; -.
DR   eggNOG; KOG1210; Eukaryota.
DR   InParanoid; Q2KIJ5; -.
DR   OrthoDB; 1210617at2759; -.
DR   BRENDA; 1.1.1.102; 908.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000009136; Unplaced.
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; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW   Proto-oncogene; Reference proteome; Signal; Sphingolipid metabolism;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..331
FT                   /note="3-ketodihydrosphingosine reductase"
FT                   /id="PRO_0000331448"
FT   TOPO_DOM        26..269
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..292
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        314..331
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000250"
FT   BINDING         36..60
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  36020 MW;  64EF1D3A3A0908D4 CRC64;
     MLLLAAASLV AFVLLLYMVS PLISPKPLAL PGAHVVVTGG SSGIGKCIAI ECYKQGAFIT
     LVARNEDKLL QAKKEIEKHS INDKQVVLCI SVDVSQDYSQ VENVIKQAQE KLGPVDMLVN
     CAGMSLSGKF EDLEVSTFER LMSINYLGSV YPSRAVIATM KERRMGRVVF VSSQAGQLGL
     FGYTAYSSSK FALRGLAEAL QMEVKPYNVY VTVAYPPDTD TPGFAKENQT KPLETRLISE
     TTSVCKPEQV AKQIVKDVQG NFNSSIGSDG YMLSSLTCGM APVTSIMEGL QQVVTMGLFR
     TIALFYLGSF DSIVRRCMMQ KAKLETVDKT A