ID A0A2U3XFZ0_LEPWE Unreviewed; 440 AA.
AC A0A2U3XFZ0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acyl-CoA (8-3)-desaturase isoform X1 {ECO:0000313|RefSeq:XP_006730389.1};
GN Name=FADS1 {ECO:0000313|RefSeq:XP_006730389.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006730389.1};
RN [1] {ECO:0000313|RefSeq:XP_006730389.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006730389.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005105}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}.
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DR RefSeq; XP_006730389.1; XM_006730326.2.
DR AlphaFoldDB; A0A2U3XFZ0; -.
DR STRING; 9713.A0A2U3XFZ0; -.
DR GeneID; 102739160; -.
DR KEGG; lww:102739160; -.
DR CTD; 3992; -.
DR OrthoDB; 294339at2759; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000245341; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03506; Delta6-FADS-like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353:SF57; ACYL-COA (8-3)-DESATURASE; 1.
DR PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 126..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..90
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 440 AA; 51629 MW; 9144C1A86110468F CRC64;
MDSETATQAP TQRYFTWDEV AQRSGHTAER WLVIDRKVYN ISEFCRRHPG GSRVISHYAG
QDATDPFVAF HIDKGLVRKY MNSLLIGELS PEQPSFEPTK NKELIDEFRE LRATVERMGL
MKANHVFFLL YLLHILLLDV AAWLTLWVFG TSLVPFLLCA VLLGTVQAQA GWLQHDFGHL
SVFSTSTWNH LLHHFVIGHL KGAPASWWNH MHFQHHAKPN CLGKDPDINM HPLFFALGKI
LSVELGKQKK KYMPYNHQHK YFFLIGPPAL LPLYFQWYIF YFVIQRKKWV DLAWMITFYA
RLFLTYWPFL GLKGVLGLFF LVRFLESHWF VWVTQMNHIP MRIDRDRNMD WVSIQLHATC
NVHKSAFNDW FSGHLNFQIE HHLFPTMPRH NYHKVAPLVQ SLCAKHGIEY QSKPLLAAFA
DIIYSLKESG QLWLDAYLHQ
//
