DEGS1_DROME
ID DEGS1_DROME Reviewed; 321 AA.
AC Q94515;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Sphingolipid delta(4)-desaturase DES1 {ECO:0000303|PubMed:11937514};
DE EC=1.14.19.17 {ECO:0000269|PubMed:11937514};
DE AltName: Full=Degenerative spermatocyte homolog 1 {ECO:0000303|PubMed:11937514, ECO:0000303|PubMed:9003299};
DE Short=DES-1 {ECO:0000303|PubMed:11937514, ECO:0000303|PubMed:9003299};
DE AltName: Full=Dihydroceramide desaturase-1 {ECO:0000303|PubMed:11937514};
GN Name=ifc {ECO:0000312|FlyBase:FBgn0001941};
GN ORFNames=CG9078 {ECO:0000312|FlyBase:FBgn0001941};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL28744.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28744.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Farfan D., Frise E., George R., Gonzalez M.,
RA Guarin H., Li P., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.,
RA Paragas V., Park S., Phouanenavong S., Wan K., Yu C., Lewis S.E.,
RA Rubin G.M., Celniker S.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAM12535.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11937514; DOI=10.1074/jbc.m202947200;
RA Ternes P., Franke S., Zaehringer U., Sperling P., Heinz E.;
RT "Identification and characterization of a sphingolipid delta 4-desaturase
RT family.";
RL J. Biol. Chem. 277:25512-25518(2002).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=9003299; DOI=10.1007/s004380050308;
RA Endo K., Akiyama T., Kobayashi S., Okada M.;
RT "Degenerative spermatocyte, a novel gene encoding a transmembrane protein
RT required for the initiation of meiosis in Drosophila spermatogenesis.";
RL Mol. Gen. Genet. 253:157-165(1996).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9819060; DOI=10.1007/s004380050861;
RA Basu J., Li Z.;
RT "The Des-1 protein, required for central spindle assembly and cytokinesis,
RT is associated with mitochondria along the meiotic spindle apparatus and
RT with the contractile ring during male meiosis in Drosophila melanogaster.";
RL Mol. Gen. Genet. 259:664-673(1998).
CC -!- FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts
CC sphinganine-containing sphingolipids (such as N-acylsphinganines or
CC dihydroceramides) into sphingolipids containing the delta-4-desaturated
CC sphingoid base (E)-sphing-4-enine (such as N-acylsphing-4-enines or
CC ceramides), which are required for many different functions (structural
CC functions as well as signaling) (PubMed:11937514). Required to initiate
CC spermatid differentiation among other signals (PubMed:9003299).
CC Required for central spindle assembly and cytokinesis during male
CC meiosis, may act as part of an anchoring mechanism that links membrane-
CC bounded cellular compartments to components of the cytoskeleton
CC (PubMed:9819060). {ECO:0000269|PubMed:11937514,
CC ECO:0000269|PubMed:9003299, ECO:0000269|PubMed:9819060}.
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:0000269|PubMed:11937514};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46545;
CC Evidence={ECO:0000269|PubMed:11937514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyleicosasphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+)
CC + O2 = an N-acyleicosasphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:55800, 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:71984,
CC ChEBI:CHEBI:71986; Evidence={ECO:0000269|PubMed:11937514};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55801;
CC Evidence={ECO:0000269|PubMed:11937514};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000305|PubMed:11937514}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Membrane; Multi-pass membrane protein
CC {ECO:0000305|PubMed:9819060}. Mitochondrion
CC {ECO:0000269|PubMed:9819060}.
CC -!- TISSUE SPECIFICITY: Testes. {ECO:0000269|PubMed:9003299,
CC ECO:0000269|PubMed:9819060}.
CC -!- DISRUPTION PHENOTYPE: Primary spermatocytes become mature in size but
CC degenerate without initiating meiotic chromosome condensation in their
CC nuclei. The mutation does not affect female fertility but leads to
CC semi-lethality both in males and females during embryonic stages
CC (PubMed:9003299). Homozigous mutant spermatids show a misshapen
CC Nebenkern, which varies in size and is associated with multiple nuclei
CC (PubMed:9819060). {ECO:0000269|PubMed:9003299,
CC ECO:0000269|PubMed:9819060}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000305}.
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DR EMBL; AE014134; AAF52318.1; -; Genomic_DNA.
DR EMBL; X94180; CAA63889.1; -; Genomic_DNA.
DR EMBL; AY061196; AAL28744.1; -; mRNA.
DR EMBL; AF466379; AAM12535.1; -; mRNA.
DR RefSeq; NP_476594.1; NM_057246.5.
DR AlphaFoldDB; Q94515; -.
DR STRING; 7227.FBpp0078810; -.
DR SwissLipids; SLP:000000169; -.
DR PaxDb; Q94515; -.
DR PRIDE; Q94515; -.
DR DNASU; 33836; -.
DR EnsemblMetazoa; FBtr0079179; FBpp0078810; FBgn0001941.
DR GeneID; 33836; -.
DR KEGG; dme:Dmel_CG9078; -.
DR UCSC; CG9078-RA; d. melanogaster.
DR CTD; 33836; -.
DR FlyBase; FBgn0001941; ifc.
DR VEuPathDB; VectorBase:FBgn0001941; -.
DR eggNOG; KOG2987; Eukaryota.
DR GeneTree; ENSGT00390000013448; -.
DR HOGENOM; CLU_032156_0_0_1; -.
DR InParanoid; Q94515; -.
DR OMA; FTYIHLL; -.
DR OrthoDB; 1255438at2759; -.
DR PhylomeDB; Q94515; -.
DR BRENDA; 1.14.19.17; 1994.
DR Reactome; R-DME-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 33836; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33836; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001941; Expressed in oviduct (Drosophila) and 46 other tissues.
DR ExpressionAtlas; Q94515; baseline and differential.
DR GO; GO:0070938; C:contractile ring; IDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
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:0005770; C:late endosome; IMP:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0016006; C:Nebenkern; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IDA:FlyBase.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:1904503; P:negative regulation of lipophagy; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; TAS:FlyBase.
DR GO; GO:0007053; P:spindle assembly involved in male meiosis; IMP:FlyBase.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR InterPro; IPR031196; DES1.
DR InterPro; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR PANTHER; PTHR12879:SF2; PTHR12879:SF2; 1.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Mitochondrion;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..321
FT /note="Sphingolipid delta(4)-desaturase DES1"
FT /id="PRO_0000453621"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 321 AA; 37213 MW; B8DB13961BF5F38E CRC64;
MGQKVSRTDF EWVYTEEPHA SRRKIILEKY PQIKKLFGHD PNFKWVAGAM VLTQILALFV
VKDLSWSWLI VAAYCFGGII NHSLMLAVHE ISHNLAFGHS RPMHNRILGF ICNLPIGLPM
SISFKKYHLE HHRYQGDEAI DTDIPTLLEA RLFDTTFGKF LWVCLQPFFY IFRPLIINPK
PPTRLEIINT VVQLTFNALI VYFLGWKPLA YLLIGSILAM GLHPVAGHFI SEHYMFAKGF
ETYSYYGPLN WITFNVGYHN EHHDFPAVPG SRLPEVKRIA KEFYDTMPQH TSWTRVLYDF
IMDPAVGPYA RVKRRQRGLA S
