DEGS1_BOVIN
ID DEGS1_BOVIN Reviewed; 323 AA.
AC Q3ZBY7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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; BC103031; AAI03032.1; -; mRNA.
DR RefSeq; NP_001029461.1; NM_001034289.1.
DR AlphaFoldDB; Q3ZBY7; -.
DR STRING; 9913.ENSBTAP00000016887; -.
DR PaxDb; Q3ZBY7; -.
DR PRIDE; Q3ZBY7; -.
DR Ensembl; ENSBTAT00000016887; ENSBTAP00000016887; ENSBTAG00000012705.
DR GeneID; 507290; -.
DR KEGG; bta:507290; -.
DR CTD; 8560; -.
DR VEuPathDB; HostDB:ENSBTAG00000012705; -.
DR VGNC; VGNC:27990; DEGS1.
DR eggNOG; KOG2987; Eukaryota.
DR GeneTree; ENSGT00390000013448; -.
DR HOGENOM; CLU_032156_0_0_1; -.
DR InParanoid; Q3ZBY7; -.
DR OMA; VYYVFGI; -.
DR OrthoDB; 1255438at2759; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000012705; Expressed in oocyte and 106 other tissues.
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; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043217; P:myelin maintenance; ISS:UniProtKB.
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;
KW Reference proteome; Transmembrane; 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_0000312726"
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 209..229
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; 38070 MW; B94D0723102C041B CRC64;
MGNRVSREDF EWVYTDQPHA TRRQEILAKY PEIKSLMKPD SNLIWIVIMM VLTQFVAFYL
VKDLDWKWVL FWAYAFGSCV NHSMTLAIHE VSHNSAFGHY KAMWNRWFGI FANLPIGVPY
SVSFKRYHMD HHRYLGADGI DVDIPTDFEG WFFCTTFRKF IWVILQPLFY AFRPLFINPK
PISYLEIINT VIQITFDIVV YYVLGVKSLV YMLAASLFGL GLHPISGHFI AEHYMFLKGH
ETYSYYGPLN LLTFNVGYHN EHHDFPNIPG KSLPLVRKIA AEYYDNLPHY NSWIKVLYDF
VTDDTISPYS RMKRHLKGNE VQE
