ACOD_CYPCA
ID ACOD_CYPCA Reviewed; 327 AA.
AC Q92038;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Acyl-CoA desaturase;
DE EC=1.14.19.1 {ECO:0000250|UniProtKB:P13516};
DE AltName: Full=Delta(9)-desaturase;
DE Short=Delta-9 desaturase {ECO:0000303|PubMed:8629000};
DE AltName: Full=Fatty acid desaturase;
DE AltName: Full=Stearoyl-CoA desaturase;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Liver;
RX PubMed=8629000; DOI=10.1126/science.271.5250.815;
RA Tiku P.E., Gracey A.Y., Macartney A.I., Beynon R.J., Cossins A.R.;
RT "Cold-induced expression of delta 9-desaturase in carp by transcriptional
RT and posttranslational mechanisms.";
RL Science 271:815-818(1996).
RN [2]
RP SEQUENCE REVISION TO 11-25 AND C-TERMINUS.
RA Tiku P.E.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from
CC reduced cytochrome b5 to introduce the first double bond into saturated
CC fatty acyl-CoA substrates. Has high specificity and catalyzes the
CC insertion of a cis double bond at the delta-9 position into fatty acyl-
CC CoA substrates including palmitoyl-CoA and stearoyl-CoA. Contributes to
CC the biosynthesis of membrane phospholipids, cholesterol esters and
CC triglycerides. {ECO:0000250|UniProtKB:P13516}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:19721, 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:57387,
CC ChEBI:CHEBI:57394; EC=1.14.19.1;
CC Evidence={ECO:0000250|UniProtKB:P13516};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P13516};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:P13516};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O00767}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- INDUCTION: By cold. A 10-fold increase in transcript levels is observed
CC 48-60 hours after cooling. {ECO:0000269|PubMed:8629000}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; U31864; AAB03857.2; -; mRNA.
DR AlphaFoldDB; Q92038; -.
DR SMR; Q92038; -.
DR Proteomes; UP000694384; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; ISS:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; ISS:UniProtKB.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..327
FT /note="Acyl-CoA desaturase"
FT /id="PRO_0000185403"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 61..64
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 86..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 205..208
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 231..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT MOTIF 87..92
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 124..128
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 265..269
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 92
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 269
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
SQ SEQUENCE 327 AA; 37820 MW; 3E794CB408D33089 CRC64;
MPDREIKSPI WHPEPGTVED VFDHTYKEKE GPKPPTVIVW RNVILMSLLH LGALYGLFLF
PSARALTWIW FFGCLLFSAL GITAGAHRLW SHRSYKASLP LQIFLALGNS MAFQNDIYEW
SRDHRVHHKY SETDADPHNA VRGFFFSHVG WLLVRKHPDV IEKGRKLELS DLKADKVVMF
QRRFYKPSVL LMCFFVPTFV PWYVWGESLW VAYFVPALLR YALVLNATWL VNSAAHMWGN
RPYDSSINPR ENRFVTFSAI GEGFHNYHHT FPFDYATSEF GCKLNLTTCC FIDLMCFLGL
AREPKRVSRE AVLARAQRTG DGSHWSG
