ID A0A3Q7UM23_VULVU Unreviewed; 323 AA.
AC A0A3Q7UM23;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=sphingolipid 4-desaturase {ECO:0000256|ARBA:ARBA00012021};
DE EC=1.14.19.17 {ECO:0000256|ARBA:ARBA00012021};
GN Name=DEGS2 {ECO:0000313|RefSeq:XP_025868350.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025868350.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025868350.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025868350.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025868350.1};
RG RefSeq;
RL Submitted (NOV-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_025868350.1; XM_026012565.1.
DR AlphaFoldDB; A0A3Q7UM23; -.
DR STRING; 9627.ENSVVUP00000039884; -.
DR Ensembl; ENSVVUT00000052176; ENSVVUP00000039883; ENSVVUG00000028406.
DR KEGG; vvp:112930235; -.
DR OMA; FEWVYND; -.
DR OrthoDB; 5485164at2759; -.
DR Proteomes; UP000286640; Unplaced.
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 Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR017228};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR017228};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 5..43
FT /note="Sphingolipid delta4-desaturase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01269"
SQ SEQUENCE 323 AA; 36860 MW; B2A85E8828139120 CRC64;
MGNSAGRTDF EWVYTDQPHT QRRKEMLAKY PAIKALMRPD PRLKWTVLAL VLAQLLSCRL
ARELPWRWLL FWAYAFGGCV NHSLTLAIHD ISHNAAFGSG RAAHNRWLAV FANLPVGLPF
AASFKKYHVD HHRYLGGDGL DVDVPTRLEG RLFCTPARKL LWLALQPFFY SLRPLCVHPK
ALTRMEVLNA LVQLAADAAL FALWGLKPVV YLLASSLLGL GLHPISGHFV AEHYMFLKGH
ETYSYYGPLN WITFNVGYHV EHHDFPSIPG CNLPQVRKIA PEYYDHLPQH HSWVKVLWDF
VFEDSLGPYA RVKRVCKLAE DGL
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