ID DES1L_ARATH Reviewed; 332 AA.
AC Q9ZPH4;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=Sphingolipid delta(4)-desaturase DES1-like;
DE EC=1.14.19.17 {ECO:0000305|PubMed:18978071};
GN OrderedLocusNames=At4g04930; ORFNames=T1J1.1;
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 [MRNA].
RA Destefano-Beltran L.J.C., Casas-Mollano A., Ciavatta V., Cairney J.;
RT "Isolation of an Arabidopsis thaliana cDNA clone encoding a novel
RT transmembrane protein homologous to a Drosophila protein required for the
RT initiation of meiosis in spermatogenesis.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18978071; DOI=10.1104/pp.108.129411;
RA Michaelson L.V., Zauner S., Markham J.E., Haslam R.P., Desikan R.,
RA Mugford S., Albrecht S., Warnecke D., Sperling P., Heinz E., Napier J.A.;
RT "Functional characterization of a higher plant sphingolipid Delta4-
RT desaturase: defining the role of sphingosine and sphingosine-1-phosphate in
RT Arabidopsis.";
RL Plant Physiol. 149:487-498(2009).
CC -!- FUNCTION: Sphingolipid-delta-4-desaturase required for the biosynthesis
CC of delta-4-unsaturated sphingolipids and derivatives. May be required
CC for the biosynthesis of glucosylceramides.
CC {ECO:0000269|PubMed:18978071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46544, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488,
CC ChEBI:CHEBI:52639; EC=1.14.19.17;
CC Evidence={ECO:0000305|PubMed:18978071};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in flowers.
CC {ECO:0000269|PubMed:18978071}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18978071}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000305}.
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DR EMBL; AF220201; AAF27915.1; -; mRNA.
DR EMBL; AF128393; AAD17340.1; -; Genomic_DNA.
DR EMBL; AL161502; CAB81035.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82444.1; -; Genomic_DNA.
DR EMBL; AK221700; BAD95415.1; -; mRNA.
DR PIR; A85062; A85062.
DR RefSeq; NP_192402.1; NM_116731.4.
DR AlphaFoldDB; Q9ZPH4; -.
DR STRING; 3702.Q9ZPH4; -.
DR iPTMnet; Q9ZPH4; -.
DR PaxDb; 3702-AT4G04930-1; -.
DR ProteomicsDB; 224078; -.
DR EnsemblPlants; AT4G04930.1; AT4G04930.1; AT4G04930.
DR GeneID; 825832; -.
DR Gramene; AT4G04930.1; AT4G04930.1; AT4G04930.
DR KEGG; ath:AT4G04930; -.
DR Araport; AT4G04930; -.
DR TAIR; AT4G04930; DES-1-LIKE.
DR eggNOG; KOG2987; Eukaryota.
DR HOGENOM; CLU_032156_0_0_1; -.
DR InParanoid; Q9ZPH4; -.
DR OMA; FEWVYND; -.
DR OrthoDB; 5485164at2759; -.
DR PhylomeDB; Q9ZPH4; -.
DR BioCyc; ARA:AT4G04930-MONOMER; -.
DR BioCyc; MetaCyc:AT4G04930-MONOMER; -.
DR PRO; PR:Q9ZPH4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZPH4; baseline and differential.
DR Genevisible; Q9ZPH4; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IMP:TAIR.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:TAIR.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR InterPro; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR PANTHER; PTHR12879; SPHINGOLIPID DELTA 4 DESATURASE/C-4 HYDROXYLASE PROTEIN DES2; 1.
DR PANTHER; PTHR12879:SF8; SPHINGOLIPID DELTA(4)-DESATURASE DES1; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR Pfam; PF08557; Lipid_DES; 1.
DR PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1.
DR SMART; SM01269; Lipid_DES; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Oxidoreductase;
KW Reference proteome; Sphingolipid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..332
FT /note="Sphingolipid delta(4)-desaturase DES1-like"
FT /id="PRO_0000430303"
FT TRANSMEM 55..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 103..107
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 140..144
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 271..275
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 38507 MW; 51EB3145EA0E8FF8 CRC64;
MGKGGREKIS SNEEEREGVM ATDFFWSYTD EPHASRRRQI LSCYPQIRQL FGPDPWAFLK
ITLVVILQLS TAAILHNSGW LKILSIAYFF GSFLNHNLFL AIHELSHNLA FSTPVYNRCL
GIFANLPIGV PMSVTFQKYH LEHHRFQGVD GIDMDVPTYT EAHLVTNIFA KTIWVFLQLF
FYALRPIFIK PKPPGYWEFI NFLIQIVLDV SVVLFFGWRS FAYLILSTFV GGGMHPMAGH
FISEHYVFNP NQETYSYYGP LNLLTWSVGY HNEHHDFPRI PGNKLHLVKE IAGEYYEGLE
SYKSWSQVIY MYIMDTTVGP YSRMKRKLSK SD
//
