ID A0A3P9A8F3_ESOLU Unreviewed; 322 AA.
AC A0A3P9A8F3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=sphingolipid 4-desaturase {ECO:0000256|ARBA:ARBA00012021};
DE EC=1.14.19.17 {ECO:0000256|ARBA:ARBA00012021};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000036992.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000036992.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000036992.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|PIRNR:PIRNR017228}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000256|ARBA:ARBA00006146,
CC ECO:0000256|PIRNR:PIRNR017228}.
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DR RefSeq; XP_010877793.1; XM_010879491.3.
DR AlphaFoldDB; A0A3P9A8F3; -.
DR STRING; 8010.ENSELUP00000036992; -.
DR Ensembl; ENSELUT00000026103.2; ENSELUP00000036992.1; ENSELUG00000016468.2.
DR GeneID; 105015975; -.
DR KEGG; els:105015975; -.
DR GeneTree; ENSGT00390000013448; -.
DR InParanoid; A0A3P9A8F3; -.
DR OMA; FEWVYND; -.
DR OrthoDB; 5485164at2759; -.
DR Proteomes; UP000265140; LG15.
DR Bgee; ENSELUG00000016468; Expressed in pharyngeal gill and 8 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR InterPro; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR PANTHER; PTHR12879; SPHINGOLIPID DELTA 4 DESATURASE/C-4 HYDROXYLASE PROTEIN DES2; 1.
DR PANTHER; PTHR12879:SF21; SPHINGOLIPID DELTA(4)-DESATURASE_C4-MONOOXYGENASE DES2; 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 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR017228};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR017228};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..43
FT /note="Sphingolipid delta4-desaturase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01269"
SQ SEQUENCE 322 AA; 37312 MW; 5229FCC597FED621 CRC64;
MGKTGGRVDF EWVYNDQPHT SRRKEILAKY PEIKALMGPD PQLKWVVTAM VLTQLLACYM
VQDLPWKWVF FWAYGFGGCI NHSLTLAIHD ISHNVAFGNK LARLNRWFAM WANLPIGLPY
SASFKKYHID HHRYLGGDGL DVDIPTDVEG WFFCTPLRKV AWLFLQPLFY ALRPLVVNPK
PISRLEVVNA AVQFAADSII FYLWGLKPIV YLIAGSILCM GLHPISGHFI AEHYMFLKGH
ETYSYYGSLN MITFNVGYHM EHHDFPSIPG SRLPQVKKIA AEYYDFLPQH TSWNQVLWDF
VFDDCIGPYA RIKREYKLVK QE
//
