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Delta(8)-fatty-acid desaturase 2 (EC 1.14.19.29) (Delta(8)-sphingolipid desaturase 2) (Sphingoid long-chain base desaturase 2) (Sphingoid LCB desaturase 2) (Sphingolipid 8-(E/Z)-desaturase 2)

 SLD2_ARATH              Reviewed;         449 AA.
Q3EBF7;
11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
08-NOV-2005, sequence version 1.
23-MAY-2018, entry version 99.
RecName: Full=Delta(8)-fatty-acid desaturase 2;
EC=1.14.19.29 {ECO:0000269|PubMed:22023480};
AltName: Full=Delta(8)-sphingolipid desaturase 2;
AltName: Full=Sphingoid long-chain base desaturase 2;
Short=Sphingoid LCB desaturase 2;
AltName: Full=Sphingolipid 8-(E/Z)-desaturase 2;
Name=SLD2; OrderedLocusNames=At2g46210; ORFNames=T3F17.14;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=22023480; DOI=10.1111/j.1365-313X.2011.04829.x;
Chen M., Markham J.E., Cahoon E.B.;
"Sphingolipid Delta8 unsaturation is important for glucosylceramide
biosynthesis and low-temperature performance in Arabidopsis.";
Plant J. 69:769-781(2012).
-!- FUNCTION: Plays a major role as delta(8)-fatty-acid desaturase
which introduces a double bond at the 8-position in the long-chain
base (LCB) of ceramides with or without a hydroxy group at the 4-
position. The enzyme produces both the 8E and 8Z isomers (in a 4:1
ratio). This structural modification contributes to the
quantitative partitioning of ceramides between the two major
sphingolipid classes, glucosylceramides and
glycosylinositolphosphoryl ceramides. Sphingolipids are important
membrane components involved in environmental stress responses,
such as resistance to chilling, and act as cell signaling
molecules. {ECO:0000269|PubMed:22023480}.
-!- CATALYTIC ACTIVITY: A (4R)-4-hydroxysphinganine ceramide + 2
ferrocytochrome b5 + O(2) + 2 H(+) = a (4R,8E)-4-hydroxysphing-8-
enine ceramide + 2 ferricytochrome b5 + 2 H(2)O.
{ECO:0000269|PubMed:22023480}.
-!- CATALYTIC ACTIVITY: A (4R)-4-hydroxysphinganine ceramide + 2
ferrocytochrome b5 + O(2) + 2 H(+) = a (4R,8Z)-4-hydroxysphing-8-
enine ceramide + 2 ferricytochrome b5 + 2 H(2)O.
{ECO:0000269|PubMed:22023480}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305|PubMed:22023480}; Multi-pass membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in flowers and siliques.
Expressed at low levels in roots, leaves and stems.
{ECO:0000269|PubMed:22023480}.
-!- DOMAIN: The histidine box domains may contain the active site
and/or be involved in metal ion binding. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but mutant plants show enhanced sensitivity to
prolonged low-temperature exposure. {ECO:0000269|PubMed:22023480}.
-!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AK228217; Type=Frameshift; Positions=16; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC005397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002685; AEC10657.1; -; Genomic_DNA.
EMBL; AK228217; -; NOT_ANNOTATED_CDS; mRNA.
RefSeq; NP_182144.1; NM_130183.4.
UniGene; At.36539; -.
ProteinModelPortal; Q3EBF7; -.
SMR; Q3EBF7; -.
STRING; 3702.AT2G46210.1; -.
PaxDb; Q3EBF7; -.
EnsemblPlants; AT2G46210.1; AT2G46210.1; AT2G46210.
GeneID; 819228; -.
Gramene; AT2G46210.1; AT2G46210.1; AT2G46210.
KEGG; ath:AT2G46210; -.
Araport; AT2G46210; -.
TAIR; locus:2062928; AT2G46210.
eggNOG; KOG4232; Eukaryota.
eggNOG; ENOG410XVSZ; LUCA.
HOGENOM; HOG000184828; -.
InParanoid; Q3EBF7; -.
KO; K21734; -.
OMA; GWHHRHY; -.
OrthoDB; EOG09360BQ0; -.
PhylomeDB; Q3EBF7; -.
Reactome; R-ATH-2046105; Linoleic acid (LA) metabolism.
Reactome; R-ATH-2046106; alpha-linolenic acid (ALA) metabolism.
PRO; PR:Q3EBF7; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q3EBF7; differential.
Genevisible; Q3EBF7; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0052631; F:sphingolipid delta-8 desaturase activity; IMP:UniProtKB.
GO; GO:0070417; P:cellular response to cold; IMP:UniProtKB.
GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:UniProtKB.
Gene3D; 3.10.120.10; -; 1.
InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
InterPro; IPR005804; FA_desaturase_dom.
InterPro; IPR012171; Fatty_acid_desaturase.
Pfam; PF00173; Cyt-b5; 1.
Pfam; PF00487; FA_desaturase; 1.
PIRSF; PIRSF015921; FA_sphinglp_des; 1.
SMART; SM01117; Cyt-b5; 1.
SUPFAM; SSF55856; SSF55856; 1.
PROSITE; PS50255; CYTOCHROME_B5_2; 1.
1: Evidence at protein level;
Complete proteome; Electron transport; Endoplasmic reticulum; Heme;
Iron; Lipid metabolism; Membrane; Metal-binding; Oxidoreductase;
Reference proteome; Sphingolipid metabolism; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 449 Delta(8)-fatty-acid desaturase 2.
/FTId=PRO_0000429374.
TRANSMEM 113 133 Helical. {ECO:0000255}.
TRANSMEM 138 158 Helical. {ECO:0000255}.
TRANSMEM 176 196 Helical. {ECO:0000255}.
TRANSMEM 255 275 Helical. {ECO:0000255}.
TRANSMEM 284 304 Helical. {ECO:0000255}.
TRANSMEM 311 331 Helical. {ECO:0000255}.
DOMAIN 7 91 Cytochrome b5 heme-binding.
{ECO:0000255|PROSITE-ProRule:PRU00279}.
MOTIF 160 164 Histidine box-1. {ECO:0000305}.
MOTIF 197 201 Histidine box-2. {ECO:0000305}.
MOTIF 374 378 Histidine box-3. {ECO:0000305}.
METAL 42 42 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00279}.
METAL 65 65 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00279}.
CONFLICT 372 372 Q -> R (in Ref. 3; AK228217).
{ECO:0000305}.
SEQUENCE 449 AA; 51498 MW; 26C0338F460C10BD CRC64;
MADQTKKRYV TSEDLKKHNK PGDLWISIQG KVYDVSDWVK SHPGGEAAIL NLAGQDVTDA
FIAYHPGTAW HHLEKLHNGY HVRDHHVSDV SRDYRRLAAE FSKRGLFDKK GHVTLYTLTC
VGVMLAAVLY GVLACTSIWA HLISAVLLGL LWIQSAYVGH DSGHYTVTST KPCNKLIQLL
SGNCLTGISI AWWKWTHNAH HIACNSLDHD PDLQHIPIFA VSTKFFNSMT SRFYGRKLTF
DPLARFLISY QHWTFYPVMC VGRINLFIQT FLLLFSKRHV PDRALNIAGI LVFWTWFPLL
VSFLPNWQER FIFVFVSFAV TAIQHVQFCL NHFAADVYTG PPNGNDWFEK QTAGTLDISC
RSFMDWFFGG LQFQLEHHLF PRLPRCHLRT VSPVVKELCK KHNLPYRSLS WWEANVWTIR
TLKNAAIQAR DATNPVLKNL LWEAVNTHG


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