KDSR_MOUSE
ID KDSR_MOUSE Reviewed; 332 AA.
AC Q6GV12;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=15328338; DOI=10.1074/jbc.m405915200;
RA Kihara A., Igarashi Y.;
RT "FVT-1 is a mammalian 3-ketodihydrosphingosine reductase with an active
RT site that faces the cytosolic side of the endoplasmic reticulum membrane.";
RL J. Biol. Chem. 279:49243-49250(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to
CC dihydrosphingosine (DHS). {ECO:0000269|PubMed:15328338}.
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; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AY634684; AAT57900.1; -; mRNA.
DR CCDS; CCDS15210.1; -.
DR RefSeq; NP_081810.1; NM_027534.2.
DR AlphaFoldDB; Q6GV12; -.
DR SMR; Q6GV12; -.
DR BioGRID; 214234; 1.
DR STRING; 10090.ENSMUSP00000010049; -.
DR iPTMnet; Q6GV12; -.
DR PhosphoSitePlus; Q6GV12; -.
DR EPD; Q6GV12; -.
DR PaxDb; Q6GV12; -.
DR PRIDE; Q6GV12; -.
DR ProteomicsDB; 264994; -.
DR Antibodypedia; 23084; 144 antibodies from 24 providers.
DR Ensembl; ENSMUST00000010049; ENSMUSP00000010049; ENSMUSG00000009905.
DR GeneID; 70750; -.
DR KEGG; mmu:70750; -.
DR UCSC; uc007cgy.2; mouse.
DR CTD; 2531; -.
DR MGI; MGI:1918000; Kdsr.
DR VEuPathDB; HostDB:ENSMUSG00000009905; -.
DR eggNOG; KOG1210; Eukaryota.
DR GeneTree; ENSGT00940000156961; -.
DR HOGENOM; CLU_010194_3_2_1; -.
DR InParanoid; Q6GV12; -.
DR OMA; NCAGMAI; -.
DR OrthoDB; 1210617at2759; -.
DR PhylomeDB; Q6GV12; -.
DR TreeFam; TF105430; -.
DR BRENDA; 1.1.1.102; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 70750; 23 hits in 76 CRISPR screens.
DR ChiTaRS; Kdsr; mouse.
DR PRO; PR:Q6GV12; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6GV12; protein.
DR Bgee; ENSMUSG00000009905; Expressed in decidua and 210 other tissues.
DR ExpressionAtlas; Q6GV12; baseline and differential.
DR Genevisible; Q6GV12; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006666; P:3-keto-sphinganine metabolic process; ISO:MGI.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IGI:MGI.
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 1: Evidence at protein 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..332
FT /note="3-ketodihydrosphingosine reductase"
FT /id="PRO_0000031983"
FT TOPO_DOM 26..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..293
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..332
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:0000305"
FT BINDING 36..60
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 35956 MW; FBB23BD1C3A3906D CRC64;
MLLLAAAGLV AFVLLLYMVS PLISPKPLAL PGAHVVVTGG SSGIGKCIAI ECYKQGAFIT
LVARNEDKLL QAKKDIEKHS INDKQVVLCI SVDVSQDYNQ VENVIKQAQE KLGPVDMLVN
CAGTSMSGKF EELEVSSFEK LMSINYLGSV YPSRAVITTM KERRVGRIVF VSSQAGQLGL
FGFTAYSSSK FAIRGLAEAL QMEVKPYNVY VTVAYPPDTD TPGLAEENKT KPLETRLISE
TTAICKPEQV AKQIVKDAIQ GNFNSSIGSD GYMLSSLTCG MAPVTSITEG LQQVVTMGLF
RTIALFYLGS FDNIVRRCMV QKAKPEVVDK TA
