FADS2_XENLA
ID FADS2_XENLA Reviewed; 446 AA.
AC Q6DDK2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Fatty acid desaturase 2;
DE EC=1.14.19.-;
DE AltName: Full=Delta(6) fatty acid desaturase;
DE Short=D6D;
DE Short=Delta(6) desaturase;
DE Short=Delta-6 desaturase;
GN Name=fads2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of a lipid metabolic pathway that catalyzes
CC biosynthesis of highly unsaturated fatty acids (HUFA) from precursor
CC essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-
CC 6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the first and
CC rate limiting step in this pathway which is the desaturation of LA
CC (18:2n-6) and ALA (18:3n-3) into gamma-linoleic acid (GLA) (18:3n-6)
CC and stearidonic acid (18:4n-3) respectively and other desaturation
CC steps. Highly unsaturated fatty acids (HUFA) play pivotal roles in many
CC biological functions (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; BC077556; AAH77556.1; -; mRNA.
DR EMBL; BC112948; AAI12949.1; -; mRNA.
DR RefSeq; NP_001086853.1; NM_001093384.1.
DR AlphaFoldDB; Q6DDK2; -.
DR SMR; Q6DDK2; -.
DR DNASU; 446688; -.
DR GeneID; 446688; -.
DR KEGG; xla:446688; -.
DR CTD; 446688; -.
DR Xenbase; XB-GENE-1010233; fads2.L.
DR OMA; QWWKNKH; -.
DR OrthoDB; 1060606at2759; -.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 446688; Expressed in brain and 12 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.120.10; -; 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; PTHR19353; 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; SSF55856; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..446
FT /note="Fatty acid desaturase 2"
FT /id="PRO_0000307106"
FT TOPO_DOM 1..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..307
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..97
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 182..186
FT /note="Histidine box-1"
FT /evidence="ECO:0000250"
FT MOTIF 219..223
FT /note="Histidine box-2"
FT /evidence="ECO:0000250"
FT MOTIF 384..388
FT /note="Histidine box-3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 446 AA; 52314 MW; ED634EF9C6891F36 CRC64;
MGMGGQSGEG CSSGDCVKPE AQYSWEEIQK HNLKTDKWLV IERKVYNISQ WVKRHPGGMR
IIGHYAGEDA TDAFHAFHPD KTFVRKFLKP LYIGELAENE PSQDRDKNAQ QVEDFRALRK
TAEDMRLFKS NPAFFIFYLF HILLIEFLAW CTLHYLGTGW IPAIITVLLL TISQAQAGWL
QHDFGHLSVF EKSKWNHLVH KFVIGHLKGA SANWWNHRHF QHHAKPNIFS KDPDVNMVNV
FVLGGTQPVE FGKKGIKYLP YNHQHLYFFL IGPPLLIPVY FTVQIIKTMI ARKDWVDLAW
SVSYYVRFFF TFVPFFGVLG SLALLNAVRF FESHWFVWVT QMNHLPMAIE HEKYQDWLNT
QLAATCNIEP SFFNDWFSGH LNFQIEHHLF PTMPRHNYWK IAPLVRSLCS KYNVTYEEKC
LYHGFRDVLR SLKKSGQLWL DAYLHK
