DEGS2_BOVIN
ID DEGS2_BOVIN Reviewed; 323 AA.
AC Q0II71;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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:0000250|UniProtKB:Q8R2F2};
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 {ECO:0000312|EMBL:AAI22777.1};
RC TISSUE=Ileum {ECO:0000312|EMBL:AAI22777.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC122776; AAI22777.1; -; mRNA.
DR RefSeq; NP_001069719.1; NM_001076251.2.
DR AlphaFoldDB; Q0II71; -.
DR STRING; 9913.ENSBTAP00000012243; -.
DR PaxDb; Q0II71; -.
DR Ensembl; ENSBTAT00000012243; ENSBTAP00000012243; ENSBTAG00000009294.
DR GeneID; 540994; -.
DR KEGG; bta:540994; -.
DR CTD; 123099; -.
DR VEuPathDB; HostDB:ENSBTAG00000009294; -.
DR VGNC; VGNC:27991; DEGS2.
DR eggNOG; KOG2987; Eukaryota.
DR GeneTree; ENSGT00390000013448; -.
DR HOGENOM; CLU_032156_0_0_1; -.
DR InParanoid; Q0II71; -.
DR OMA; FTYIHLL; -.
DR OrthoDB; 1255438at2759; -.
DR TreeFam; TF313582; -.
DR Reactome; R-BTA-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00786; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000009294; Expressed in esophagus and 88 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:0042284; F:sphingolipid delta-4 desaturase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 2: Evidence at transcript 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:0000250|UniProtKB:Q564G3"
FT CHAIN 2..323
FT /note="Sphingolipid delta(4)-desaturase/C4-monooxygenase
FT DES2"
FT /evidence="ECO:0000250|UniProtKB:Q564G3"
FT /id="PRO_0000312815"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..231
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:0000250|UniProtKB:Q564G3"
SQ SEQUENCE 323 AA; 37319 MW; FEC0556150C819EB CRC64;
MGNRAGRSDF EWVYTDQPHT QRRKEMLAKY PAIKALMRPD PYLKWTVTAM VLAQLLACWL
AQGLAWRWLF FWAYAFGGCV NHSLTLAIHD ISHNTAFGTG RPSRNRWFAI FANLPVGLPY
AASFKKYHVD HHRYLGGDGL DVDVPTYFEG RLFCTPARKL LWLALQPFFY TLRPLCVHPK
AMTRMELCNT LVQLAADATI YALWGLKPMV YLLASSLLGL GLHPISGHFV AEHYMFLKGH
ETYSYYGPLN WITFNVGYHM EHHDFPSIPS CNLPLVRKIA PEYYDHLPQH HSWVKVLWDF
VFDDSLGPFA RVKRVCKLAE NRL
