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O09005 (DEGS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sphingolipid delta(4)-desaturase DES1
EC=1.14.-.-
Alternative name(s):
Degenerative spermatocyte homolog 1
Gene names
Name:Degs1
Synonyms:Degs, Des1, Mdes
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine). Ref.2

Subcellular location

Mitochondrion. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Detected in testis. Detected in pachytene spermatocytes and round spermatids. Ref.1

Post-translational modification

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

Sequence similarities

Belongs to the fatty acid desaturase family. DEGS subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 323322Sphingolipid delta(4)-desaturase DES1
PRO_0000312729

Regions

Transmembrane41 – 6121Helical; Potential
Transmembrane68 – 8821Helical; Potential
Transmembrane104 – 12421Helical; Potential
Transmembrane152 – 17221Helical; Potential
Transmembrane184 – 20421Helical; Potential
Transmembrane209 – 22921Helical; Potential

Amino acid modifications

Modified residue3071Phosphoserine By similarity
Lipidation21N-myristoyl glycine By similarity

Experimental info

Sequence conflict2031V → A in AAM12532. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O09005 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: C1840C24E6FF29E0

FASTA32338,241
        10         20         30         40         50         60 
MGSRVSREEF EWVYTDQPHA ARRKEILAKY PEIKSLMKPD HNLIWIVAMM LLVQLASFYL 

        70         80         90        100        110        120 
VKDLDWKWVI FWSYVFGSCL NHSMTLAIHE ISHNFPFGHH KALWNRWFGM FANLSLGVPY 

       130        140        150        160        170        180 
SISFKRYHMD HHRYLGADKI DVDIPTDFEG WFFCTTFRKF VWVILQPLFY AFRPLFINPK 

       190        200        210        220        230        240 
PITYLEIINT VIQITFDIII YYVFGVKSLV YMLAATLLGL GLHPISGHFI AEHYMFLKGH 

       250        260        270        280        290        300 
ETYSYYGPLN LLTFNVGYHN EHHDFPNVPG KNLPMVRKIA SEYYDDLPHY NSWIKVLYDF 

       310        320 
VTDDTISPYS RMKRPPKGNE ILE

« Hide

References

« Hide 'large scale' references
[1]"Mdes, a mouse homolog of the Drosophila degenerative spermatocyte gene is expressed during mouse spermatogenesis."
Endo K., Matsuda Y., Kobayashi S.
Dev. Growth Differ. 39:399-403(1997) [PubMed: 9227906] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: ddY.
Tissue: Testis.
[2]"Identification and characterization of a sphingolipid delta 4-desaturase family."
Ternes P., Franke S., Zaehringer U., Sperling P., Heinz E.
J. Biol. Chem. 277:25512-25518(2002) [PubMed: 11937514] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: C57BL/6.
Tissue: Kidney.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow macrophage, Egg, Kidney, Ovary and Uterus.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y08460 mRNA. Translation: CAA69714.1.
AF466376 mRNA. Translation: AAM12532.1.
AK002617 mRNA. Translation: BAB22233.1.
AK077257 mRNA. Translation: BAC36713.1.
AK149811 mRNA. Translation: BAE29098.1.
AK163404 mRNA. Translation: BAE37337.1.
BC003751 mRNA. Translation: AAH03751.1.
IPIIPI00113731.
RefSeqNP_031879.1. NM_007853.4.
UniGeneMm.29648.

3D structure databases

ProteinModelPortalO09005.
ModBaseSearch...

Protein-protein interaction databases

STRINGO09005.

PTM databases

PhosphoSiteO09005.

Proteomic databases

PRIDEO09005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035295; ENSMUSP00000048519; ENSMUSG00000038633.
GeneID13244.
KEGGmmu:13244.
UCSCuc007dxw.1. mouse.

Organism-specific databases

CTD8560.
MGIMGI:1097711. Degs1.

Phylogenomic databases

eggNOGroNOG08918.
GeneTreeENSGT00390000013448.
HOGENOMHBG324309.
HOVERGENHBG052775.
InParanoidO09005.
OMAHNSAFGH.
OrthoDBEOG4JM7PZ.
PhylomeDBO09005.

Gene expression databases

ArrayExpressO09005.
BgeeO09005.
CleanExMM_DEGS1.
GenevestigatorO09005.

Family and domain databases

InterProIPR005804. Fatty_acid_desaturase-1.
IPR011388. Sphingolipid_d4-desaturase.
IPR013866. Sphingolipid_d4-desaturase_N.
[Graphical view]
KOK04712.
PfamPF00487. FA_desaturase. 1 hit.
PF08557. Lipid_DES. 1 hit.
[Graphical view]
PIRSFPIRSF017228. Sphnglp_dlt4_des. 1 hit.
ProtoNetSearch...

Other

NextBio283464.
SOURCESearch...

Entry information

Entry nameDEGS1_MOUSE
AccessionPrimary (citable) accession number: O09005
Secondary accession number(s): Q8R4H3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: July 1, 1997
Last modified: December 14, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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