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   27-MAR-2024, entry version 108.
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; 9913-ENSBTAP00000025820; -.
DR   Ensembl; ENSBTAT00000025820.6; ENSBTAP00000025820.5; ENSBTAG00000022449.5.
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; SCGESWH; -.
DR   OrthoDB; 637961at2759; -.
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 cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; ACYL-COA DESATURASE; 1.
DR   PANTHER; PTHR11351:SF99; STEAROYL-COA DESATURASE 5; 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
//