TC10A_ARATH
ID TC10A_ARATH Reviewed; 326 AA.
AC Q0WRJ2; Q9M7S9;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=3-dehydrosphinganine reductase TSC10A;
DE EC=1.1.1.102;
DE AltName: Full=3-ketodihydrosphingosine reductase;
DE Short=KDS reductase;
DE AltName: Full=3-ketosphinganine reductase;
GN Name=TSC10A; OrderedLocusNames=At3g06060; ORFNames=F24F17.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, STEREOSPECIFICITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21421810; DOI=10.1105/tpc.110.079095;
RA Chao D.Y., Gable K., Chen M., Baxter I., Dietrich C.R., Cahoon E.B.,
RA Guerinot M.L., Lahner B., Lu S., Markham J.E., Morrissey J., Han G.,
RA Gupta S.D., Harmon J.M., Jaworski J.G., Dunn T.M., Salt D.E.;
RT "Sphingolipids in the root play an important role in regulating the leaf
RT ionome in Arabidopsis thaliana.";
RL Plant Cell 23:1061-1081(2011).
CC -!- FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to
CC dihydrosphingosine (DHS). Required for sphingolipid biosynthesis. In
CC plants, sphingolipids seems to play a critical role in mineral ion
CC homeostasis, most likely through their involvement in the ion transport
CC functionalities of membrane systems in the root. Lacks
CC stereospecificity and can also produce L-threo-DHS in addition to D-
CC erythro-DHS. {ECO:0000269|PubMed:21421810}.
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:21421810};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:21421810}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:21421810}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:21421810}.
CC -!- DISRUPTION PHENOTYPE: High frequency of tricotyledons and altered
CC flower morphology. The double mutants tsc10a and tsc10b are not viable.
CC {ECO:0000269|PubMed:21421810}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF66134.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAO24564.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC068073; AAF66134.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74338.1; -; Genomic_DNA.
DR EMBL; BT003132; AAO24564.1; ALT_SEQ; mRNA.
DR EMBL; AK228314; BAF00257.1; -; mRNA.
DR RefSeq; NP_187257.2; NM_111481.3.
DR AlphaFoldDB; Q0WRJ2; -.
DR SMR; Q0WRJ2; -.
DR STRING; 3702.AT3G06060.1; -.
DR iPTMnet; Q0WRJ2; -.
DR PaxDb; Q0WRJ2; -.
DR PRIDE; Q0WRJ2; -.
DR ProteomicsDB; 234206; -.
DR EnsemblPlants; AT3G06060.1; AT3G06060.1; AT3G06060.
DR GeneID; 819779; -.
DR Gramene; AT3G06060.1; AT3G06060.1; AT3G06060.
DR KEGG; ath:AT3G06060; -.
DR Araport; AT3G06060; -.
DR TAIR; locus:2080379; AT3G06060.
DR eggNOG; KOG1210; Eukaryota.
DR HOGENOM; CLU_010194_3_2_1; -.
DR InParanoid; Q0WRJ2; -.
DR BioCyc; MetaCyc:AT3G06060-MON; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q0WRJ2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WRJ2; baseline and differential.
DR Genevisible; Q0WRJ2; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047560; F:3-dehydrosphinganine reductase activity; IDA:TAIR.
DR GO; GO:0006666; P:3-keto-sphinganine metabolic process; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:TAIR.
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 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 Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..326
FT /note="3-dehydrosphinganine reductase TSC10A"
FT /id="PRO_0000430305"
FT TOPO_DOM 1..7
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..288
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT ACT_SITE 192
FT /evidence="ECO:0000250"
FT BINDING 45..56
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 326 AA; 34980 MW; 56455EB893A0FBC8 CRC64;
MAAISPLFLL FLIPIIPLSL LAILALIVRP RPIKIPIKSR HAFITGGSSG IGLALAHRAA
SEGARVSILA RSGSKLEEAK KSIQLATGVE VATFSADVRD YDAVSKAIDE SGPIDVLIVN
QGVFTAKELV KHSPEDVKFT IDVNLVGSFN VIKAALPAMK ARKDRGPASI SLVSSQAGQV
GVYGYAAYSA SKFGLQGLAQ ALQQEVISDD IHVTLIFPPD TNTPGFEEEQ KSRPEVTAII
AASSGSMETE EVAKKAMDGI KAGNFTVSCN FEGFLLSLAT TGMSPQRSFW LAFLEVITAG
PIRLIALFFQ WDWYKAIEKW SKTKTK
