DEGS2_RAT
ID DEGS2_RAT Reviewed; 323 AA.
AC Q564G3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Sphingolipid delta(4)-desaturase/C4-monooxygenase DES2;
DE EC=1.14.18.5;
DE EC=1.14.19.17;
DE AltName: Full=Degenerative spermatocyte homolog 2;
DE AltName: Full=Sphingolipid 4-desaturase;
DE AltName: Full=Sphingolipid C4-monooxygenase;
GN Name=Degs2 {ECO:0000312|EMBL:AAH98701.1};
GN Synonyms=Des2 {ECO:0000312|EMBL:CAI79417.1};
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], AND MYRISTOYLATION AT GLY-2.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:CAI79417.1};
RC TISSUE=Liver {ECO:0000269|PubMed:17716801};
RX PubMed=17716801; DOI=10.1016/j.biochi.2007.07.001;
RA Beauchamp E., Goenaga D., Le Bloc'h J., Catheline D., Legrand P., Rioux V.;
RT "Myristic acid increases the activity of dihydroceramide delta4-desaturase
RT 1 through its N-terminal myristoylation.";
RL Biochimie 89:1553-1561(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus {ECO:0000312|EMBL:AAH98701.1};
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: Bifunctional enzyme which acts as both a sphingolipid
CC delta(4)-desaturase and a sphingolipid C4-monooxygenase.
CC {ECO:0000250|UniProtKB:Q8R2F2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dihydroceramide + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a
CC phytoceramide + 2 Fe(III)-[cytochrome b5] + H2O;
CC Xref=Rhea:RHEA:55808, 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:139048,
CC ChEBI:CHEBI:139051; EC=1.14.18.5;
CC Evidence={ECO:0000250|UniProtKB:Q8R2F2};
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:Q8R2F2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N-octanoylsphinganine + O2
CC = 2 Fe(III)-[cytochrome b5] + H2O + N-octanoyl-4-hydroxysphinganine;
CC Xref=Rhea:RHEA:43116, 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:82841,
CC ChEBI:CHEBI:82842; Evidence={ECO:0000250|UniProtKB:Q6QHC5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43117;
CC Evidence={ECO:0000250|UniProtKB:Q6QHC5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = an N-acyl-(4R)-4-hydroxysphinganine + 2 Fe(III)-[cytochrome b5] +
CC H2O; Xref=Rhea:RHEA:46364, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488,
CC ChEBI:CHEBI:31998; EC=1.14.18.5;
CC Evidence={ECO:0000250|UniProtKB:Q6QHC5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46365;
CC Evidence={ECO:0000250|UniProtKB:Q6QHC5};
CC -!- PATHWAY: Membrane lipid metabolism; sphingolipid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8R2F2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8R2F2}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ938082; CAI79417.1; -; mRNA.
DR EMBL; BC098701; AAH98701.1; -; mRNA.
DR RefSeq; NP_001017457.1; NM_001017457.2.
DR AlphaFoldDB; Q564G3; -.
DR STRING; 10116.ENSRNOP00000015855; -.
DR iPTMnet; Q564G3; -.
DR PaxDb; Q564G3; -.
DR Ensembl; ENSRNOT00000015855; ENSRNOP00000015855; ENSRNOG00000011716.
DR GeneID; 314438; -.
DR KEGG; rno:314438; -.
DR UCSC; RGD:1305023; rat.
DR CTD; 123099; -.
DR RGD; 1305023; Degs2.
DR eggNOG; KOG2987; Eukaryota.
DR GeneTree; ENSGT00390000013448; -.
DR HOGENOM; CLU_032156_0_0_1; -.
DR InParanoid; Q564G3; -.
DR OMA; FTYIHLL; -.
DR OrthoDB; 1255438at2759; -.
DR PhylomeDB; Q564G3; -.
DR TreeFam; TF313582; -.
DR BRENDA; 1.14.19.17; 5301.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR SABIO-RK; Q564G3; -.
DR UniPathway; UPA00786; -.
DR PRO; PR:Q564G3; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000011716; Expressed in duodenum and 18 other tissues.
DR Genevisible; Q564G3; 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:0042284; F:sphingolipid delta-4 desaturase activity; ISO:RGD.
DR GO; GO:0000170; F:sphingosine hydroxylase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006667; P:sphinganine metabolic process; ISO:RGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; ISO:RGD.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR InterPro; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Lipoprotein;
KW Membrane; Myristate; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17716801"
FT CHAIN 2..323
FT /note="Sphingolipid delta(4)-desaturase/C4-monooxygenase
FT DES2"
FT /evidence="ECO:0000269|PubMed:17716801"
FT /id="PRO_0000312818"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 95..99
FT /note="Required for C4-hydroxylase activity"
FT /evidence="ECO:0000250|UniProtKB:Q8R2F2"
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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:17716801"
SQ SEQUENCE 323 AA; 37441 MW; FCB8061A3CDB7683 CRC64;
MGNSAARSDF EWVYSDQPHT QRRKEMLAKY PSIKALMRPD PNIKWTVLGM VLVQVLACWL
VRGLSWRWLL FWAYAFGGCI NHSLTLAIHD ISHNTAFGTR CASRNRWFAV FANLPIGLPY
ATSFKKYHVD HHRYLGGDGL DVDIPTDFEG WFFCTPARKL LWLVLQPFFY SLRPLYVNPK
AVTRMEILNA LVQLAFNVTI FALWGIKAIV YLLASSLLGL GLHPISGHFV AEHYMFLKGH
ETYSYYGPLN WITFNVGYHV EHHDFPSIPG CYLPLVRMIA PEYYDHLPQH HSWVKVLWDF
VFEDSLGPYS RVKRKCKLAK DQL
