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Protein

Sphingolipid delta(4)-desaturase/C4-monooxygenase DES2

Gene

Degs2

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

Functioni

Bifunctional enzyme which acts as both a sphingolipid delta(4)-desaturase and a sphingolipid C4-monooxygenase.By similarity

Catalytic activityi

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

Pathwayi: sphingolipid biosynthesis

This protein is involved in the pathway sphingolipid biosynthesis, which is part of Membrane lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway sphingolipid biosynthesis and in Membrane lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-RNO-1660661. Sphingolipid de novo biosynthesis.
SABIO-RKQ564G3.
UniPathwayiUPA00786.

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingolipid delta(4)-desaturase/C4-monooxygenase DES2 (EC:1.14.18.5, EC:1.14.19.17)
Alternative name(s):
Degenerative spermatocyte homolog 2
Sphingolipid 4-desaturase
Sphingolipid C4-monooxygenase
Gene namesi
Name:Degs2Imported
Synonyms:Des2Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi1305023. Degs2.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei41 – 61HelicalSequence analysisAdd BLAST21
Transmembranei68 – 88HelicalSequence analysisAdd BLAST21
Transmembranei200 – 220HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00003128182 – 323Sphingolipid delta(4)-desaturase/C4-monooxygenase DES21 PublicationAdd BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PaxDbiQ564G3.
PRIDEiQ564G3.

Expressioni

Gene expression databases

BgeeiENSRNOG00000011716.
GenevisibleiQ564G3. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015855.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni95 – 99Required for C4-hydroxylase activityBy similarity5

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.
InParanoidiQ564G3.
KOiK04712.
OMAiWFFCTPA.
OrthoDBiEOG091G09NW.
PhylomeDBiQ564G3.
TreeFamiTF313582.

Family and domain databases

InterProiIPR011388. DES1/DES2.
IPR031195. Des2.
IPR005804. FA_desaturase_dom.
IPR013866. Sphingolipid_d4-desaturase_N.
[Graphical view]
PANTHERiPTHR12879:SF1. PTHR12879:SF1. 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.

Q564G3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNSAARSDF EWVYSDQPHT QRRKEMLAKY PSIKALMRPD PNIKWTVLGM
60 70 80 90 100
VLVQVLACWL VRGLSWRWLL FWAYAFGGCI NHSLTLAIHD ISHNTAFGTR
110 120 130 140 150
CASRNRWFAV FANLPIGLPY ATSFKKYHVD HHRYLGGDGL DVDIPTDFEG
160 170 180 190 200
WFFCTPARKL LWLVLQPFFY SLRPLYVNPK AVTRMEILNA LVQLAFNVTI
210 220 230 240 250
FALWGIKAIV YLLASSLLGL GLHPISGHFV AEHYMFLKGH ETYSYYGPLN
260 270 280 290 300
WITFNVGYHV EHHDFPSIPG CYLPLVRMIA PEYYDHLPQH HSWVKVLWDF
310 320
VFEDSLGPYS RVKRKCKLAK DQL
Length:323
Mass (Da):37,441
Last modified:May 10, 2005 - v1
Checksum:iFCB8061A3CDB7683
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938082 mRNA. Translation: CAI79417.1.
BC098701 mRNA. Translation: AAH98701.1.
RefSeqiNP_001017457.1. NM_001017457.2.
UniGeneiRn.166717.

Genome annotation databases

EnsembliENSRNOT00000015855; ENSRNOP00000015855; ENSRNOG00000011716.
GeneIDi314438.
KEGGirno:314438.
UCSCiRGD:1305023. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938082 mRNA. Translation: CAI79417.1.
BC098701 mRNA. Translation: AAH98701.1.
RefSeqiNP_001017457.1. NM_001017457.2.
UniGeneiRn.166717.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015855.

Proteomic databases

PaxDbiQ564G3.
PRIDEiQ564G3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015855; ENSRNOP00000015855; ENSRNOG00000011716.
GeneIDi314438.
KEGGirno:314438.
UCSCiRGD:1305023. rat.

Organism-specific databases

CTDi123099.
RGDi1305023. Degs2.

Phylogenomic databases

eggNOGiKOG2987. Eukaryota.
ENOG410XQVT. LUCA.
GeneTreeiENSGT00390000013448.
HOGENOMiHOG000188299.
HOVERGENiHBG052775.
InParanoidiQ564G3.
KOiK04712.
OMAiWFFCTPA.
OrthoDBiEOG091G09NW.
PhylomeDBiQ564G3.
TreeFamiTF313582.

Enzyme and pathway databases

UniPathwayiUPA00786.
ReactomeiR-RNO-1660661. Sphingolipid de novo biosynthesis.
SABIO-RKQ564G3.

Miscellaneous databases

PROiQ564G3.

Gene expression databases

BgeeiENSRNOG00000011716.
GenevisibleiQ564G3. RN.

Family and domain databases

InterProiIPR011388. DES1/DES2.
IPR031195. Des2.
IPR005804. FA_desaturase_dom.
IPR013866. Sphingolipid_d4-desaturase_N.
[Graphical view]
PANTHERiPTHR12879:SF1. PTHR12879:SF1. 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 nameiDEGS2_RAT
AccessioniPrimary (citable) accession number: Q564G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: May 10, 2005
Last modified: November 30, 2016
This is version 89 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.