TC10B_ARATH
ID TC10B_ARATH Reviewed; 331 AA.
AC F4JZN6;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=3-dehydrosphinganine reductase TSC10B;
DE EC=1.1.1.102;
DE AltName: Full=3-ketodihydrosphingosine reductase;
DE Short=KDS reductase;
DE AltName: Full=3-ketosphinganine reductase;
GN Name=TSC10B; OrderedLocusNames=At5g19200; ORFNames=T24G5;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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. Is stereospecific for
CC D-erythro-DHS production and does not produce L-threo-DHS.
CC {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 and flowers.
CC {ECO:0000269|PubMed:21421810}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but 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 ---------------------------------------------------------------------------
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; AC069326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92669.1; -; Genomic_DNA.
DR RefSeq; NP_197421.1; NM_121925.4.
DR AlphaFoldDB; F4JZN6; -.
DR SMR; F4JZN6; -.
DR STRING; 3702.AT5G19200.1; -.
DR iPTMnet; F4JZN6; -.
DR PaxDb; F4JZN6; -.
DR PRIDE; F4JZN6; -.
DR ProteomicsDB; 234165; -.
DR EnsemblPlants; AT5G19200.1; AT5G19200.1; AT5G19200.
DR GeneID; 832040; -.
DR Gramene; AT5G19200.1; AT5G19200.1; AT5G19200.
DR KEGG; ath:AT5G19200; -.
DR Araport; AT5G19200; -.
DR TAIR; locus:2182192; AT5G19200.
DR eggNOG; KOG1210; Eukaryota.
DR HOGENOM; CLU_010194_3_2_1; -.
DR InParanoid; F4JZN6; -.
DR OMA; GAHPNEP; -.
DR OrthoDB; 1210617at2759; -.
DR PhylomeDB; F4JZN6; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:F4JZN6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JZN6; baseline and differential.
DR Genevisible; F4JZN6; 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..331
FT /note="3-dehydrosphinganine reductase TSC10B"
FT /id="PRO_0000430306"
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..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..286
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..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 43..54
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; 35835 MW; ED1F3FA321B8D54E CRC64;
MAAIFSLFLF FILFIVSLLI ILSFIVRPRS VTIPIKFRHV FITGGSSGIG LALAHRAVSE
GAKVSILARS TEKLAEAKRS IQLATGVEVA TFSADVRDYD AVSKAIDESG PIDVLIVNQG
VFIGKELEKQ SPEEVKFMID VNLTGSFNVI KAALPAMKAR EGRGPASISL VSSQAGQAGI
YGYTAYSASK FGLQGLAQAL QQEVISDGIH VTLLFPPDTD TPGFEQELKK RPELTSIIAA
SSGSMKTNEV AKICFDGIKA GKFTVTCHFI GFLLSIASTG MSPQGSFWLA LTEVMFGGLI
RLASLVFQWQ WYKTIEKWSQ RNKKEVNSKL A
