SCD2_RAT
ID SCD2_RAT Reviewed; 358 AA.
AC Q6P7B9; Q64066; Q9JMC9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Stearoyl-CoA desaturase 2 {ECO:0000303|Ref.1};
DE EC=1.14.19.1 {ECO:0000269|PubMed:20228221};
DE AltName: Full=Acyl-CoA desaturase 2;
DE AltName: Full=Delta(9)-desaturase 2;
DE Short=Delta-9 desaturase 2;
DE AltName: Full=Fatty acid desaturase 2;
GN Name=Scd2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hoshino T., Ishiguro K., Ohtsu K.;
RT "Molecular cloning and tissue expression of rat stearoyl-CoA desaturase
RT 2.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
RX PubMed=7800118; DOI=10.1007/bf00968721;
RA Baba H., Fuss B., Watson J.B., Zane L.T., Macklin W.B.;
RT "Identification of novel mRNAs expressed in oligodendrocytes.";
RL Neurochem. Res. 19:1091-1099(1994).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION BY FAT-FREE DIET.
RX PubMed=1982442; DOI=10.1093/oxfordjournals.jbchem.a123301;
RA Mihara K.;
RT "Structure and regulation of rat liver microsomal stearoyl-CoA desaturase
RT gene.";
RL J. Biochem. 108:1022-1029(1990).
RN [5]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=20228221; DOI=10.1194/jlr.m004747;
RA Green C.D., Ozguden-Akkoc C.G., Wang Y., Jump D.B., Olson L.K.;
RT "Role of fatty acid elongases in determination of de novo synthesized
RT monounsaturated fatty acid species.";
RL J. Lipid Res. 51:1871-1877(2010).
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. Catalyzes the insertion of a cis double bond
CC at the delta-9 position into fatty acyl-CoA substrates including
CC palmitoyl-CoA and stearoyl-CoA (PubMed:20228221). Gives rise to a
CC mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:20228221).
CC Contributes to the biosynthesis of membrane phospholipids, cholesterol
CC esters and triglycerides, especially during embryonic development and
CC in neonates. Important for normal permeability barrier function of the
CC skin in neonates. {ECO:0000250|UniProtKB:P13011,
CC ECO:0000269|PubMed:20228221}.
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:0000269|PubMed:20228221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19722;
CC Evidence={ECO:0000305|PubMed:20228221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 =
CC (9Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36931, 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:57379,
CC ChEBI:CHEBI:61540; Evidence={ECO:0000269|PubMed:20228221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36932;
CC Evidence={ECO:0000305|PubMed:20228221};
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:P13011}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P13011}. Microsome membrane
CC {ECO:0000250|UniProtKB:P13011}.
CC -!- TISSUE SPECIFICITY: Detected in brain and adipose tissue, and at much
CC lower levels in testis. Detected in liver when rats are kept on a fat-
CC free diet, but not when their food contains unsaturated fatty acids.
CC {ECO:0000269|PubMed:1982442}.
CC -!- INDUCTION: Up-regulated in liver in the absence of dietary unsaturated
CC fatty acids(PubMed:1982442). Expression in adipose tissue seems to be
CC constitutive (PubMed:1982442). {ECO:0000269|PubMed:1982442}.
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; AB032243; BAA92436.1; -; mRNA.
DR EMBL; BC061737; AAH61737.1; -; mRNA.
DR EMBL; S75730; AAB32826.1; -; mRNA.
DR RefSeq; NP_114029.1; NM_031841.1.
DR AlphaFoldDB; Q6P7B9; -.
DR SMR; Q6P7B9; -.
DR STRING; 10116.ENSRNOP00000067809; -.
DR SwissLipids; SLP:000000455; -.
DR iPTMnet; Q6P7B9; -.
DR PhosphoSitePlus; Q6P7B9; -.
DR jPOST; Q6P7B9; -.
DR PaxDb; Q6P7B9; -.
DR GeneID; 83792; -.
DR KEGG; rno:83792; -.
DR UCSC; RGD:621177; rat.
DR CTD; 20250; -.
DR RGD; 621177; Scd2.
DR eggNOG; KOG1600; Eukaryota.
DR InParanoid; Q6P7B9; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; Q6P7B9; -.
DR TreeFam; TF313251; -.
DR BRENDA; 1.14.19.1; 5301.
DR Reactome; R-RNO-75105; Fatty acyl-CoA biosynthesis.
DR PRO; PR:Q6P7B9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0032896; F:palmitoyl-CoA 9-desaturase activity; ISO:RGD.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IDA:RGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; TAS:RGD.
DR GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0042552; P:myelination; IEP:RGD.
DR GO; GO:0070542; P:response to fatty acid; IDA:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Microsome; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..358
FT /note="Stearoyl-CoA desaturase 2"
FT /id="PRO_0000185401"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 93..96
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 118..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 217..236
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 237..240
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TRANSMEM 241..262
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT TOPO_DOM 263..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT REGION 14..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 119..124
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 156..160
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 297..301
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
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 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 268
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 300
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 301
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT CONFLICT 76
FT /note="V -> I (in Ref. 1; BAA92436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 41013 MW; 24EAA2329011C4D9 CRC64;
MPAHILQEIS GSYSATTTIT APPSGGQQNG GEKFEKNPHH WGADVRPEIK DDLYDPSYQD
EEGPPPKLEY VWRNIVLMAL LHIGALYGIT LVPSCKVYTC LFAYLYYVIS ALGITAGAHR
LWSHRTYKAR LPLRLFLIIA NTMAFQNDVY EWARDHRAHH KFSETHADPH NSRRGFFFSH
VGWLLVRKHP AVKEKGGKLD MSDLKAEKLV MFQRRYYKPG LLLMCFILPT LVPWYCWGET
FVNSLCVSTF LRYAVVLNAT WLVNSAAHLY GYRPYDKNIS SRENILVSMG AVGEGFHNYH
HAFPYDYSAS EYRWHINFTT FFIDCMALLG LAYDRKRVSK AAVLARIKRT GEESCKSG
