ID A0A1U8DIA0_ALLSI Unreviewed; 287 AA.
AC A0A1U8DIA0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Sphingolipid delta(4)-desaturase DES1 {ECO:0000256|ARBA:ARBA00023815};
DE AltName: Full=Degenerative spermatocyte homolog 1 {ECO:0000256|ARBA:ARBA00032761};
DE AltName: Full=Dihydroceramide desaturase-1 {ECO:0000256|ARBA:ARBA00030408};
DE AltName: Full=Retinol isomerase {ECO:0000256|ARBA:ARBA00030541};
GN Name=DEGS1 {ECO:0000313|RefSeq:XP_014380036.2};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014380036.2};
RN [1] {ECO:0000313|RefSeq:XP_014380036.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55356,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:45479;
CC Evidence={ECO:0000256|ARBA:ARBA00023728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55357;
CC Evidence={ECO:0000256|ARBA:ARBA00023728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55360,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:78272;
CC Evidence={ECO:0000256|ARBA:ARBA00023689};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55361;
CC Evidence={ECO:0000256|ARBA:ARBA00023689};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol = 11-cis-retinol; Xref=Rhea:RHEA:19141,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:17336;
CC Evidence={ECO:0000256|ARBA:ARBA00023720};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19142;
CC Evidence={ECO:0000256|ARBA:ARBA00023720};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19143;
CC Evidence={ECO:0000256|ARBA:ARBA00023720};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55352,
CC ChEBI:CHEBI:17336, ChEBI:CHEBI:45479;
CC Evidence={ECO:0000256|ARBA:ARBA00023714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55353;
CC Evidence={ECO:0000256|ARBA:ARBA00023714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55348,
CC ChEBI:CHEBI:17336, ChEBI:CHEBI:78272;
CC Evidence={ECO:0000256|ARBA:ARBA00023675};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55349;
CC Evidence={ECO:0000256|ARBA:ARBA00023675};
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:0000256|ARBA:ARBA00029284};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46545;
CC Evidence={ECO:0000256|ARBA:ARBA00029284};
CC -!- SUBUNIT: Interacts with RLBP1; the interaction increases synthesis of
CC chromophore-precursors by DEGS1. {ECO:0000256|ARBA:ARBA00023795}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|PIRNR:PIRNR017228}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000256|PIRNR:PIRNR017228}.
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DR RefSeq; XP_014380036.2; XM_014524550.2.
DR AlphaFoldDB; A0A1U8DIA0; -.
DR STRING; 38654.A0A1U8DIA0; -.
DR KEGG; asn:102374259; -.
DR eggNOG; KOG2987; Eukaryota.
DR InParanoid; A0A1U8DIA0; -.
DR OrthoDB; 5485164at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR InterPro; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
DR PANTHER; PTHR12879; SPHINGOLIPID DELTA 4 DESATURASE/C-4 HYDROXYLASE PROTEIN DES2; 1.
DR PANTHER; PTHR12879:SF2; SPHINGOLIPID DELTA(4)-DESATURASE DES1; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR017228};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR017228};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..253
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 287 AA; 33641 MW; F453E5C21B0FB1AB CRC64;
MKPDRHLIWV VVLMVLAQLI AFYLVKDLDW KWVIFWAYVF GSCISHSMTL AIHEISHNSA
FGNCKAMWNR WFGIFANLPL GLPYSISFKR YHMDHHRYLG GDGIDVDIPT DFEGWLFCTR
FRKFIWIVLQ PLFYAIRPLC INPKPISRLE IINLLAQLSF DVVIYYFWGI KSVCYMLAGS
VLGLGLHPIS GHFIAEHYMF LKGHETYSYY GPLNLLTFNV GYHNEHHDFP NIPGKSLPLV
KKIAAEYYDN LPQYNSWIKV LYDFVMDDTI SPYSRMKRHL KGDVKQE
//
