DEGS1_CHICK
ID DEGS1_CHICK Reviewed; 323 AA.
AC Q5F3C1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sphingolipid delta(4)-desaturase DES1;
DE EC=1.14.19.17 {ECO:0000250|UniProtKB:O15121};
DE AltName: Full=Degenerative spermatocyte homolog 1;
DE AltName: Full=Dihydroceramide desaturase-1 {ECO:0000303|PubMed:23143414};
DE AltName: Full=Retinol isomerase;
DE EC=5.2.1.- {ECO:0000269|PubMed:23143414};
GN Name=DEGS1; Synonyms=DES1 {ECO:0000303|PubMed:23143414};
GN ORFNames=RCJMB04_22e12;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INTERACTION WITH RLBP1.
RX PubMed=23143414; DOI=10.1038/nchembio.1114;
RA Kaylor J.J., Yuan Q., Cook J., Sarfare S., Makshanoff J., Miu A., Kim A.,
RA Kim P., Habib S., Roybal C.N., Xu T., Nusinowitz S., Travis G.H.;
RT "Identification of DES1 as a vitamin A isomerase in Mueller glial cells of
RT the retina.";
RL Nat. Chem. Biol. 9:30-36(2013).
CC -!- FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts D-
CC erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine) (By
CC similarity). Catalyzes the equilibrium isomerization of retinols
CC (PubMed:23143414). {ECO:0000250|UniProtKB:O15121,
CC ECO:0000269|PubMed:23143414}.
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:0000250|UniProtKB:O15121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46545;
CC Evidence={ECO:0000250|UniProtKB:O15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol = 11-cis-retinol; Xref=Rhea:RHEA:19141,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:17336;
CC Evidence={ECO:0000269|PubMed:23143414};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19142;
CC Evidence={ECO:0000305|PubMed:23143414};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19143;
CC Evidence={ECO:0000305|PubMed:23143414};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55348,
CC ChEBI:CHEBI:17336, ChEBI:CHEBI:78272;
CC Evidence={ECO:0000269|PubMed:23143414};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55349;
CC Evidence={ECO:0000305|PubMed:23143414};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55352,
CC ChEBI:CHEBI:17336, ChEBI:CHEBI:45479;
CC Evidence={ECO:0000269|PubMed:23143414};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55353;
CC Evidence={ECO:0000305|PubMed:23143414};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55356,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:45479;
CC Evidence={ECO:0000269|PubMed:23143414};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55357;
CC Evidence={ECO:0000305|PubMed:23143414};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55360,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:78272;
CC Evidence={ECO:0000269|PubMed:23143414};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55361;
CC Evidence={ECO:0000305|PubMed:23143414};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.3 uM for all-trans-retinol {ECO:0000269|PubMed:23143414};
CC KM=14.8 uM for 11-cis-retinol {ECO:0000269|PubMed:23143414};
CC Vmax=4.3 pmol/min/mg enzyme toward all-trans-retinol for the
CC formation of 11-cis-retinol {ECO:0000269|PubMed:23143414};
CC Vmax=65 pmol/min/mg enzyme toward all-trans-retinol for the formation
CC of 9-cis-retinol {ECO:0000269|PubMed:23143414};
CC Vmax=1730 pmol/min/mg enzyme toward all-trans-retinol for the
CC formation of 13-cis-retinol {ECO:0000269|PubMed:23143414};
CC Vmax=129 pmol/min/mg enzyme toward 11-cis-retinol for the formation
CC of 9-cis-retinol {ECO:0000269|PubMed:23143414};
CC Vmax=768 pmol/min/mg enzyme toward 11-cis-retinol for the formation
CC of 13-cis-retinol {ECO:0000269|PubMed:23143414};
CC Vmax=1970 pmol/min/mg enzyme toward 11-cis-retinol for the formation
CC of all-trans-retinol {ECO:0000269|PubMed:23143414};
CC -!- SUBUNIT: Interacts with RLBP1; the interaction increases synthesis of
CC chromophore-precursors by DEGS1. {ECO:0000269|PubMed:23143414}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O15121}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O15121}.
CC -!- TISSUE SPECIFICITY: Expressed in retina and retinal pigment epithelium
CC by Mueller cells (at protein level). {ECO:0000269|PubMed:23143414}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ851729; CAH65363.1; -; mRNA.
DR RefSeq; NP_001012583.1; NM_001012565.1.
DR AlphaFoldDB; Q5F3C1; -.
DR DIP; DIP-61751N; -.
DR IntAct; Q5F3C1; 1.
DR STRING; 9031.ENSGALP00000015178; -.
DR SwissLipids; SLP:000001830; -.
DR PaxDb; Q5F3C1; -.
DR Ensembl; ENSGALT00000015194; ENSGALP00000015178; ENSGALG00000009330.
DR GeneID; 421327; -.
DR KEGG; gga:421327; -.
DR CTD; 8560; -.
DR VEuPathDB; HostDB:geneid_421327; -.
DR eggNOG; KOG2987; Eukaryota.
DR GeneTree; ENSGT00390000013448; -.
DR HOGENOM; CLU_032156_0_0_1; -.
DR InParanoid; Q5F3C1; -.
DR OMA; VYYVFGI; -.
DR OrthoDB; 1255438at2759; -.
DR PhylomeDB; Q5F3C1; -.
DR TreeFam; TF313582; -.
DR Reactome; R-GGA-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-GGA-433584; Sphingolipid metabolism.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR PRO; PR:Q5F3C1; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000009330; Expressed in spermatocyte and 13 other tissues.
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:0016859; F:cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0050251; F:retinol isomerase activity; IDA:UniProtKB.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043217; P:myelin maintenance; ISS:UniProtKB.
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; Fatty acid biosynthesis; Fatty acid metabolism;
KW Isomerase; Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..323
FT /note="Sphingolipid delta(4)-desaturase DES1"
FT /id="PRO_0000312732"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 89..93
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 128..132
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 259..263
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 37975 MW; EFDB8936175FB964 CRC64;
MGNTVAREDF EWVYTDQPHA DRRKEILAKH PEIKALMKPD YNLIWVVMLM VAAQLTAFYL
VRDLDWKWVV FWAYVFGSCI SHSMTLAIHE ISHNSAFGNG RAMWNRWFGI FANLPLGLPY
SISFKRYHMD HHRYLGGDGI DVDIPTNFEG WFFCTRFRKF IWIVLQPFFY AIRPLCINPK
PITRLEIINL LAQLFFDIVI YYLWGAKSIF YMLAGSVLGL GLHPISGHFI AEHYMFLKGH
ETYSYYGPLN LLTFNVGYHN EHHDFPNIPG KSLPLVKKIA AEYYDNLPQY NSWIKVLYDF
VMDDTISPYS RMKRQLKGEV KQD
