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Protein

Sphingolipid delta(4)-desaturase DES1

Gene

Degs1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine) (By similarity).By similarity

Catalytic activityi

A dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4E)-sphing-4-enine ceramide + 2 ferricytochrome b5 + 2 H2O.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-RNO-1660661. Sphingolipid de novo biosynthesis.
R-RNO-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingolipid delta(4)-desaturase DES1 (EC:1.14.19.17By similarity)
Alternative name(s):
Degenerative spermatocyte homolog 1
Degenerative spermatocyte-like protein RDES
Gene namesi
Name:Degs1
Synonyms:Degs, Des1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi70917. Degs1.

Subcellular locationi

  • Mitochondrion By similarity
  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  • Membrane By similarity; Lipid-anchor By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei41 – 61HelicalSequence analysisAdd BLAST21
Transmembranei68 – 88HelicalSequence analysisAdd BLAST21
Transmembranei104 – 124HelicalSequence analysisAdd BLAST21
Transmembranei152 – 172HelicalSequence analysisAdd BLAST21
Transmembranei184 – 204HelicalSequence analysisAdd BLAST21
Transmembranei210 – 230HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00003127312 – 323Sphingolipid delta(4)-desaturase DES1Add BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Modified residuei307PhosphoserineBy similarity1

Post-translational modificationi

Myristoylation can target the enzyme to the mitochondria leading to an increase in ceramide levels.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiQ5XIF5.
PRIDEiQ5XIF5.

Expressioni

Gene expression databases

BgeeiENSRNOG00000003223.
GenevisibleiQ5XIF5. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004319.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi89 – 93Histidine box-1Curated5
Motifi128 – 132Histidine box-2Curated5
Motifi259 – 263Histidine box-3Curated5

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2987. Eukaryota.
ENOG410XQVT. LUCA.
GeneTreeiENSGT00390000013448.
HOGENOMiHOG000188299.
HOVERGENiHBG052775.
InParanoidiQ5XIF5.
KOiK04712.
OMAiEFYETMP.
OrthoDBiEOG091G09NW.
PhylomeDBiQ5XIF5.
TreeFamiTF313582.

Family and domain databases

InterProiIPR031196. DES1.
IPR011388. DES1/DES2.
IPR005804. FA_desaturase_dom.
IPR013866. Sphingolipid_d4-desaturase_N.
[Graphical view]
PANTHERiPTHR12879:SF2. PTHR12879:SF2. 1 hit.
PfamiPF00487. FA_desaturase. 1 hit.
PF08557. Lipid_DES. 1 hit.
[Graphical view]
PIRSFiPIRSF017228. Sphnglp_dlt4_des. 1 hit.
SMARTiSM01269. Lipid_DES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5XIF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNRVSREEF EWVYTDQPHA ARRQEILAKY PEIKSLMKPD PNLIWIVTSM
60 70 80 90 100
LLVQLASFYL VKDLDWKWLM FWSYAFGSCL NHSMTLAIHE ISHNFPFGHH
110 120 130 140 150
KAMWNRWFGM FANLSLGVPY SISFKRYHMD HHRYLGADGI DVDIPTDFEG
160 170 180 190 200
WFFCTTLRKL VWVILQPLFY AFRPLFINPK PITHLEVINT VIQVTFDVLV
210 220 230 240 250
YYVFGVKSLV YMLAASLLGL GLHPISGHFI AEHYMFLKGH ETYSYYGPLN
260 270 280 290 300
LLTFNVGYHN EHHDFPNVPG KNLPLVRKIA SEYYDNLPHY NSWIRVLYDF
310 320
VMDDTISPYS RMKRPPKGNE IQE
Length:323
Mass (Da):38,055
Last modified:November 23, 2004 - v1
Checksum:i7DAB9C8CF9091108
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3N → S in AAK64511 (Ref. 1) Curated1
Sequence conflicti24Q → K in AAK64511 (Ref. 1) Curated1
Sequence conflicti41P → H in AAK64511 (Ref. 1) Curated1
Sequence conflicti48 – 49TS → AM in AAK64511 (Ref. 1) Curated2
Sequence conflicti69 – 70LM → VI in AAK64511 (Ref. 1) Curated2
Sequence conflicti75A → V in AAK64511 (Ref. 1) Curated1
Sequence conflicti103M → L in AAK64511 (Ref. 1) Curated1
Sequence conflicti190T → A in AAK64511 (Ref. 1) Curated1
Sequence conflicti322Q → H in CAI79416 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY036902 mRNA. Translation: AAK64511.1.
AJ938081 mRNA. Translation: CAI79416.1.
BC083727 mRNA. Translation: AAH83727.1.
RefSeqiNP_445775.2. NM_053323.2.
UniGeneiRn.34792.

Genome annotation databases

EnsembliENSRNOT00000004319; ENSRNOP00000004319; ENSRNOG00000003223.
GeneIDi58970.
KEGGirno:58970.
UCSCiRGD:70917. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY036902 mRNA. Translation: AAK64511.1.
AJ938081 mRNA. Translation: CAI79416.1.
BC083727 mRNA. Translation: AAH83727.1.
RefSeqiNP_445775.2. NM_053323.2.
UniGeneiRn.34792.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004319.

Proteomic databases

PaxDbiQ5XIF5.
PRIDEiQ5XIF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004319; ENSRNOP00000004319; ENSRNOG00000003223.
GeneIDi58970.
KEGGirno:58970.
UCSCiRGD:70917. rat.

Organism-specific databases

CTDi8560.
RGDi70917. Degs1.

Phylogenomic databases

eggNOGiKOG2987. Eukaryota.
ENOG410XQVT. LUCA.
GeneTreeiENSGT00390000013448.
HOGENOMiHOG000188299.
HOVERGENiHBG052775.
InParanoidiQ5XIF5.
KOiK04712.
OMAiEFYETMP.
OrthoDBiEOG091G09NW.
PhylomeDBiQ5XIF5.
TreeFamiTF313582.

Enzyme and pathway databases

ReactomeiR-RNO-1660661. Sphingolipid de novo biosynthesis.
R-RNO-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiQ5XIF5.

Gene expression databases

BgeeiENSRNOG00000003223.
GenevisibleiQ5XIF5. RN.

Family and domain databases

InterProiIPR031196. DES1.
IPR011388. DES1/DES2.
IPR005804. FA_desaturase_dom.
IPR013866. Sphingolipid_d4-desaturase_N.
[Graphical view]
PANTHERiPTHR12879:SF2. PTHR12879:SF2. 1 hit.
PfamiPF00487. FA_desaturase. 1 hit.
PF08557. Lipid_DES. 1 hit.
[Graphical view]
PIRSFiPIRSF017228. Sphnglp_dlt4_des. 1 hit.
SMARTiSM01269. Lipid_DES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDEGS1_RAT
AccessioniPrimary (citable) accession number: Q5XIF5
Secondary accession number(s): Q564G4, Q91XI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: November 23, 2004
Last modified: November 30, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.