SCD5_BOVIN
ID SCD5_BOVIN Reviewed; 335 AA.
AC Q2KIA4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Stearoyl-CoA desaturase 5;
DE EC=1.14.19.1 {ECO:0000250|UniProtKB:Q86SK9};
DE AltName: Full=Acyl-CoA-desaturase 4;
DE AltName: Full=Stearoyl-CoA 9-desaturase;
GN Name=SCD5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=17468887; DOI=10.1007/s11745-007-3056-2;
RA Lengi A.J., Corl B.A.;
RT "Identification and characterization of a novel bovine stearoyl-CoA
RT desaturase isoform with homology to human SCD5.";
RL Lipids 42:499-508(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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. 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. Gives rise to a mixture of 16:1 and
CC 18:1 unsaturated fatty acids. Involved in neuronal cell proliferation
CC and differentiation through down-regulation of EGFR/AKT/MAPK and Wnt
CC signaling pathways. {ECO:0000250|UniProtKB:Q86SK9}.
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:Q86SK9};
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:0000250|UniProtKB:Q86SK9};
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 -!- SUBUNIT: May self-associate and form homodimers.
CC {ECO:0000250|UniProtKB:Q86SK9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q86SK9}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:17468887}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- MISCELLANEOUS: This protein has no ortholog in rodents. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; EF014951; ABJ99757.1; -; mRNA.
DR EMBL; BC112711; AAI12712.1; -; mRNA.
DR RefSeq; NP_001070413.1; NM_001076945.1.
DR AlphaFoldDB; Q2KIA4; -.
DR SMR; Q2KIA4; -.
DR STRING; 9913.ENSBTAP00000025820; -.
DR PaxDb; Q2KIA4; -.
DR Ensembl; ENSBTAT00000025820; ENSBTAP00000025820; ENSBTAG00000022449.
DR GeneID; 617419; -.
DR KEGG; bta:617419; -.
DR CTD; 79966; -.
DR VEuPathDB; HostDB:ENSBTAG00000022449; -.
DR VGNC; VGNC:34328; SCD5.
DR eggNOG; KOG1600; Eukaryota.
DR GeneTree; ENSGT00940000162090; -.
DR HOGENOM; CLU_027359_0_0_1; -.
DR InParanoid; Q2KIA4; -.
DR OMA; CQHGPID; -.
DR OrthoDB; 971318at2759; -.
DR TreeFam; TF313251; -.
DR BRENDA; 1.14.19.1; 908.
DR Reactome; R-BTA-75105; Fatty acyl-CoA biosynthesis.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000022449; Expressed in midbrain and 98 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; ISS:UniProtKB.
DR GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; IBA:GO_Central.
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; Transmembrane; Transmembrane helix.
FT CHAIN 1..335
FT /note="Stearoyl-CoA desaturase 5"
FT /id="PRO_0000312652"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..77
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..227
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 24..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 99..104
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 136..140
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 277..281
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 104
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="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 139
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 248
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 277
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 280
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 281
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
SQ SEQUENCE 335 AA; 38215 MW; 32F8B2C60533AB31 CRC64;
MPGPAVDAEK VPFRSAKEEI RAGVGVEGSE GGGGGGGRER PGARGHRQDI VWRNVFLMSL
LHLAAVYSLV LIPKAQPLTL LWAYFCFLLT ALGVTAGAHR LWSHRSYKAK LPLRIFLAAA
NSMAFQNDIF EWSRDHRVHH KYSETDADPH NARRGFFFSH IGWLFVRKHR DVIEKGRKLD
VTDLLADPVV RFQRKYYKIT VVLMCFVVPT LVPWYIWGES LWNSYFLASI LRYTISLNVT
WLVNSVAHMY GNRPYDKHIS PRQNPLVTLG AIGEGFHNYH HTFPFDYSAS EFGLNFNPTT
WFIDFMCWLG LATDRKRATK QMIEARKART GDGSA
