DEGS1_RAT
ID DEGS1_RAT Reviewed; 323 AA.
AC Q5XIF5; Q564G4; Q91XI6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=Degenerative spermatocyte-like protein RDES;
DE AltName: Full=Dihydroceramide desaturase-1;
DE AltName: Full=Retinol isomerase;
DE EC=5.2.1.- {ECO:0000250|UniProtKB:Q5F3C1};
GN Name=Degs1 {ECO:0000312|RGD:70917}; Synonyms=Degs, Des1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RA Tirado O.M., Selva D.M., Munell F., Reventos J.;
RT "A rat homolog of DEGS.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Goenaga D., Catheline D., Legrand P., Rioux V.;
RT "Cloning and characterization of the rat sphingolipid delta 4 desaturases
RT DES1 and DES2.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; AY036902; AAK64511.1; -; mRNA.
DR EMBL; AJ938081; CAI79416.1; -; mRNA.
DR EMBL; BC083727; AAH83727.1; -; mRNA.
DR RefSeq; NP_445775.2; NM_053323.2.
DR AlphaFoldDB; Q5XIF5; -.
DR ELM; Q5XIF5; -.
DR STRING; 10116.ENSRNOP00000004319; -.
DR PaxDb; Q5XIF5; -.
DR Ensembl; ENSRNOT00000004319; ENSRNOP00000004319; ENSRNOG00000003223.
DR GeneID; 58970; -.
DR KEGG; rno:58970; -.
DR UCSC; RGD:70917; rat.
DR CTD; 8560; -.
DR RGD; 70917; Degs1.
DR eggNOG; KOG2987; Eukaryota.
DR GeneTree; ENSGT00390000013448; -.
DR HOGENOM; CLU_032156_0_0_1; -.
DR InParanoid; Q5XIF5; -.
DR OMA; VYYVFGI; -.
DR OrthoDB; 1255438at2759; -.
DR PhylomeDB; Q5XIF5; -.
DR TreeFam; TF313582; -.
DR BRENDA; 1.14.19.17; 5301.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q5XIF5; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003223; Expressed in esophagus and 20 other tissues.
DR Genevisible; Q5XIF5; RN.
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; ISO:RGD.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISO:RGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043217; P:myelin maintenance; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
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_0000312731"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
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 210..230
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"
FT CONFLICT 3
FT /note="N -> S (in Ref. 1; AAK64511)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="Q -> K (in Ref. 1; AAK64511)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="P -> H (in Ref. 1; AAK64511)"
FT /evidence="ECO:0000305"
FT CONFLICT 48..49
FT /note="TS -> AM (in Ref. 1; AAK64511)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..70
FT /note="LM -> VI (in Ref. 1; AAK64511)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="A -> V (in Ref. 1; AAK64511)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="M -> L (in Ref. 1; AAK64511)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="T -> A (in Ref. 1; AAK64511)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="Q -> H (in Ref. 2; CAI79416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 38055 MW; 7DAB9C8CF9091108 CRC64;
MGNRVSREEF EWVYTDQPHA ARRQEILAKY PEIKSLMKPD PNLIWIVTSM LLVQLASFYL
VKDLDWKWLM FWSYAFGSCL NHSMTLAIHE ISHNFPFGHH KAMWNRWFGM FANLSLGVPY
SISFKRYHMD HHRYLGADGI DVDIPTDFEG WFFCTTLRKL VWVILQPLFY AFRPLFINPK
PITHLEVINT VIQVTFDVLV YYVFGVKSLV YMLAASLLGL GLHPISGHFI AEHYMFLKGH
ETYSYYGPLN LLTFNVGYHN EHHDFPNVPG KNLPLVRKIA SEYYDNLPHY NSWIRVLYDF
VMDDTISPYS RMKRPPKGNE IQE
