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Sphingolipid delta(4)-desaturase DES1 (EC 1.14.19.17) (Degenerative spermatocyte homolog 1) (Degenerative spermatocyte-like protein RDES)

 DEGS1_RAT               Reviewed;         323 AA.
Q5XIF5; Q564G4; Q91XI6;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
30-AUG-2017, entry version 100.
RecName: Full=Sphingolipid delta(4)-desaturase DES1;
EC=1.14.19.17 {ECO:0000250|UniProtKB:O15121};
AltName: Full=Degenerative spermatocyte homolog 1;
AltName: Full=Degenerative spermatocyte-like protein RDES;
Name=Degs1; Synonyms=Degs, Des1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Testis;
Tirado O.M., Selva D.M., Munell F., Reventos J.;
"A rat homolog of DEGS.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Goenaga D., Catheline D., Legrand P., Rioux V.;
"Cloning and characterization of the rat sphingolipid delta 4
desaturases DES1 and DES2.";
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts
D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine)
(By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: A dihydroceramide + 2 ferrocytochrome b5 +
O(2) + 2 H(+) = a (4E)-sphing-4-enine ceramide + 2 ferricytochrome
b5 + 2 H(2)O. {ECO:0000250|UniProtKB:O15121}.
-!- SUBCELLULAR LOCATION: Mitochondrion
{ECO:0000250|UniProtKB:O15121}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:O15121}; Multi-pass membrane protein
{ECO:0000250}. Membrane {ECO:0000250|UniProtKB:O15121}; Lipid-
anchor {ECO:0000250|UniProtKB:O15121}.
-!- PTM: Myristoylation can target the enzyme to the mitochondria
leading to an increase in ceramide levels. {ECO:0000250}.
-!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
DEGS subfamily. {ECO:0000305}.
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EMBL; AY036902; AAK64511.1; -; mRNA.
EMBL; AJ938081; CAI79416.1; -; mRNA.
EMBL; BC083727; AAH83727.1; -; mRNA.
RefSeq; NP_445775.2; NM_053323.2.
UniGene; Rn.34792; -.
SMR; Q5XIF5; -.
ELM; Q5XIF5; -.
STRING; 10116.ENSRNOP00000004319; -.
PaxDb; Q5XIF5; -.
PRIDE; Q5XIF5; -.
Ensembl; ENSRNOT00000004319; ENSRNOP00000004319; ENSRNOG00000003223.
GeneID; 58970; -.
KEGG; rno:58970; -.
UCSC; RGD:70917; rat.
CTD; 8560; -.
RGD; 70917; Degs1.
eggNOG; KOG2987; Eukaryota.
eggNOG; ENOG410XQVT; LUCA.
GeneTree; ENSGT00390000013448; -.
HOGENOM; HOG000188299; -.
HOVERGEN; HBG052775; -.
InParanoid; Q5XIF5; -.
KO; K04712; -.
OMA; QIFFYAL; -.
OrthoDB; EOG091G09NW; -.
PhylomeDB; Q5XIF5; -.
TreeFam; TF313582; -.
Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:Q5XIF5; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000003223; -.
Genevisible; Q5XIF5; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IBA:GO_Central.
GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
InterPro; IPR011388; DES1/DES2.
InterPro; IPR005804; FA_desaturase_dom.
InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
Pfam; PF00487; FA_desaturase; 1.
Pfam; PF08557; Lipid_DES; 1.
PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1.
SMART; SM01269; Lipid_DES; 1.
2: Evidence at transcript level;
Complete proteome; Endoplasmic reticulum; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
Lipoprotein; Membrane; Mitochondrion; Myristate; Oxidoreductase;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O15121}.
CHAIN 2 323 Sphingolipid delta(4)-desaturase DES1.
/FTId=PRO_0000312731.
TRANSMEM 41 61 Helical. {ECO:0000255}.
TRANSMEM 68 88 Helical. {ECO:0000255}.
TRANSMEM 104 124 Helical. {ECO:0000255}.
TRANSMEM 152 172 Helical. {ECO:0000255}.
TRANSMEM 184 204 Helical. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
MOTIF 89 93 Histidine box-1. {ECO:0000305}.
MOTIF 128 132 Histidine box-2. {ECO:0000305}.
MOTIF 259 263 Histidine box-3. {ECO:0000305}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000250|UniProtKB:O15121}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:O15121}.
CONFLICT 3 3 N -> S (in Ref. 1; AAK64511).
{ECO:0000305}.
CONFLICT 24 24 Q -> K (in Ref. 1; AAK64511).
{ECO:0000305}.
CONFLICT 41 41 P -> H (in Ref. 1; AAK64511).
{ECO:0000305}.
CONFLICT 48 49 TS -> AM (in Ref. 1; AAK64511).
{ECO:0000305}.
CONFLICT 69 70 LM -> VI (in Ref. 1; AAK64511).
{ECO:0000305}.
CONFLICT 75 75 A -> V (in Ref. 1; AAK64511).
{ECO:0000305}.
CONFLICT 103 103 M -> L (in Ref. 1; AAK64511).
{ECO:0000305}.
CONFLICT 190 190 T -> A (in Ref. 1; AAK64511).
{ECO:0000305}.
CONFLICT 322 322 Q -> H (in Ref. 2; CAI79416).
{ECO:0000305}.
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


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