FAD2_SIGCA
ID FAD2_SIGCA Reviewed; 445 AA.
AC D8X2C5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Acyl-CoA Delta-4 desaturase {ECO:0000305|PubMed:20826444};
DE EC=1.14.19.44 {ECO:0000269|PubMed:20826444};
DE AltName: Full=Delta(4)/Delta(5) fatty acid desaturase {ECO:0000305|PubMed:20826444};
DE Short=D4D/D5D fatty acid desaturase {ECO:0000305|PubMed:20826444};
DE Short=Delta-4/Delta-5 fatty acid desaturase {ECO:0000305|PubMed:20826444};
DE AltName: Full=FAD2 {ECO:0000303|PubMed:20826444};
DE Short=Delta-4 desaturase;
GN Name=fad2 {ECO:0000303|PubMed:20826444};
OS Siganus canaliculatus (White-spotted spinefoot) (Chaetodon canaliculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Siganidae; Siganus.
OX NCBI_TaxID=75042;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=20826444; DOI=10.1073/pnas.1008429107;
RA Li Y., Monroig O., Zhang L., Wang S., Zheng X., Dick J.R., You C.,
RA Tocher D.R.;
RT "Vertebrate fatty acyl desaturase with Delta4 activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16840-16845(2010).
CC -!- FUNCTION: Fatty acid desaturase with bifunctional delta-4 and delta-5
CC activities. Component of a lipid metabolic pathway that catalyzes the
CC biosynthesis of polyunsaturated fatty acids (PUFA) with preference
CC toward n-3 substrates and Delta(4)function.
CC {ECO:0000269|PubMed:20826444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(II)-[cytochrome
CC b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 2
CC Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46420, Rhea:RHEA-
CC COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:73862, ChEBI:CHEBI:74265;
CC EC=1.14.19.44; Evidence={ECO:0000269|PubMed:20826444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46421;
CC Evidence={ECO:0000269|PubMed:20826444};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + 2 Fe(II)-[cytochrome
CC b5] + 2 H(+) + O2 = (4Z,7Z,10Z,13Z,16Z)-docosapentaenoyl-CoA + 2
CC Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:63648, Rhea:RHEA-
CC COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:73856, ChEBI:CHEBI:76368;
CC Evidence={ECO:0000269|PubMed:20826444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63649;
CC Evidence={ECO:0000269|PubMed:20826444};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = (4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:63652, 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:73870,
CC ChEBI:CHEBI:74298; Evidence={ECO:0000269|PubMed:20826444};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63653;
CC Evidence={ECO:0000269|PubMed:20826444};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000305|PubMed:20826444}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The protein sequence includes a number of characteristic
CC features of microsomal fatty acid desaturases including three histidine
CC boxes and an N-terminal cytochrome b5 domain containing the heme-
CC binding motif. {ECO:0000269|PubMed:20826444}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; GU594278; ADJ29913.1; -; mRNA.
DR AlphaFoldDB; D8X2C5; -.
DR SMR; D8X2C5; -.
DR SwissLipids; SLP:000000442; -.
DR UniPathway; UPA00658; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0062076; F:acyl-CoA delta5-desaturase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..445
FT /note="Acyl-CoA Delta-4 desaturase"
FT /id="PRO_0000451727"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 19..96
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
SQ SEQUENCE 445 AA; 52005 MW; 44810EFCAB70EE11 CRC64;
MGGGGQLGES GENGCKSAAG VYTWEEVQHH SNRNDQWLVI DRKVYNVTQW AKRHPGGFRV
LNHYAGEDAT EAFTAFHPDI KFVQKYMKPL LVGELAATEP SQDQDKNAAL IQDFHTLRQQ
AESEGLFQAR PLFFLLHLGH ILLLEALALL MVWHWGTGWL QTLLCAVMLA TAQSQAGWLQ
HDFGHLSVFK KSRWNHLVHK FVIGHLKGAS ANWWNHRHFQ HHAKPNIFKK DPDINMVDLF
VLGETQPVEY GIKKIKNMPY NHQHKYFFLV APPLLIPVFY NYNIMMTMIT RRDYVDLSWA
MTFYIRYMLC YVPVYGLFGS LALMMFARFL ESHWFVWVTQ MSHLPMDIDN DKRRDWLSMQ
LQATCNIEKS FFNDWFSGHL NFQIEHHLFP RMPRHNYHLV APQVQTLCEK HGIPYEVKTL
WKGMVDVVRA LKKSGDLWLD AYLHK
