DEGS1_MICFO
ID DEGS1_MICFO Reviewed; 323 AA.
AC Q6UQ04;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Sphingolipid delta(4)-desaturase DES1 {ECO:0000305};
DE EC=1.14.19.17 {ECO:0000250|UniProtKB:O15121};
DE AltName: Full=Degenerative spermatocyte homolog 1;
DE AltName: Full=Dihydroceramide desaturase-1;
DE AltName: Full=Retinol isomerase;
DE EC=5.2.1.- {ECO:0000250|UniProtKB:Q5F3C1};
GN Name=DEGS1; Synonyms=DES1;
OS Microtus fortis (Reed vole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Arvicolinae; Microtus.
OX NCBI_TaxID=100897;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RA Hu W.-X., Qing Z.-Q., Xu B.;
RT "The cloning of fatty acid desaturase from Microtus fortis bone marrow cDNA
RT library.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts D-
CC erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine) (By
CC similarity). Catalyzes the equilibrium isomerization of retinols (By
CC similarity). {ECO:0000250|UniProtKB:O09005,
CC ECO:0000250|UniProtKB:Q5F3C1}.
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:0000250|UniProtKB:O15121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46545;
CC Evidence={ECO:0000250|UniProtKB:O15121};
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:0000250|UniProtKB:O09005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19142;
CC Evidence={ECO:0000250|UniProtKB:O09005};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19143;
CC Evidence={ECO:0000250|UniProtKB:O09005};
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:0000250|UniProtKB:Q5F3C1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55349;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
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:0000250|UniProtKB:Q5F3C1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55353;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
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:0000250|UniProtKB:Q5F3C1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55357;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
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:0000250|UniProtKB:Q5F3C1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55361;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
CC -!- SUBUNIT: Interacts with RLBP1; the interaction increases synthesis of
CC chromophore-precursors by DEGS1. {ECO:0000250|UniProtKB:Q5F3C1}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:O15121}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O15121}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O15121}.
CC -!- PTM: Myristoylation can target the enzyme to the mitochondria leading
CC to an increase in ceramide levels. {ECO:0000250|UniProtKB:O15121}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000305}.
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DR EMBL; AY364471; AAQ63465.1; -; mRNA.
DR AlphaFoldDB; Q6UQ04; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016859; F:cis-trans isomerase activity; ISS:UniProtKB.
DR GO; GO:0050251; F:retinol isomerase activity; ISS:UniProtKB.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043217; P:myelin maintenance; ISS:UniProtKB.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR InterPro; IPR031196; DES1.
DR InterPro; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR PANTHER; PTHR12879:SF2; PTHR12879:SF2; 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.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Isomerase; Lipid biosynthesis; Lipid metabolism; Lipoprotein; Membrane;
KW Mitochondrion; Myristate; Oxidoreductase; Phosphoprotein; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15121"
FT CHAIN 2..323
FT /note="Sphingolipid delta(4)-desaturase DES1"
FT /id="PRO_0000312728"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 89..93
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 128..132
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 259..263
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15121"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:O15121"
SQ SEQUENCE 323 AA; 38066 MW; 393E9D86BA128426 CRC64;
MGSRVSREEF EWVYTDQPHT DRRREILAKY PEIKSLMKPD PNLIWIITAM FLVQLISLYL
VKDLDWKWVI FWSYVFGSCL NHSMTLAIHE ISHNFPFGHH KAVWNRWFGI FANLPIGVPY
SVSFKRYHMD HHRYLGADGI DVDIPTDFEG WFFCTTFRKL VWVILQPLFY ALRPLFINPK
PITYLEIINT VTQIILDIIV YYVFGIKSLV YMLAASLLGL GLHPISGHFI AEHYMFLKGH
ETYSYYGPLN LLTFNVGYHN EHHDFPNVPG KNLPLVRKIA AEYYDKLPQY NSWIKVLYDF
VMDDTISPYS RMKRPPKGSE NLD
