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Database: UniProt
Entry: B7Q6K4_IXOSC
LinkDB: B7Q6K4_IXOSC
Original site: B7Q6K4_IXOSC 
ID   B7Q6K4_IXOSC            Unreviewed;       340 AA.
AC   B7Q6K4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Stearoyl-CoA desaturase, putative {ECO:0000313|EMBL:EEC14476.1, ECO:0000313|EnsemblMetazoa:ISCW021567-PA};
DE            EC=1.14.19.1 {ECO:0000313|EMBL:EEC14476.1};
DE   Flags: Fragment;
GN   ORFNames=IscW_ISCW021567 {ECO:0000313|EMBL:EEC14476.1};
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1] {ECO:0000313|EMBL:EEC14476.1, ECO:0000313|Proteomes:UP000001555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC   {ECO:0000313|EMBL:EEC14476.1};
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ISCW021567-PA}
RP   IDENTIFICATION.
RC   STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW021567-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|RuleBase:RU000581};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC       metal ions. {ECO:0000256|RuleBase:RU000581}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00009295, ECO:0000256|RuleBase:RU000581}.
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DR   EMBL; ABJB010946766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS868232; EEC14476.1; -; Genomic_DNA.
DR   RefSeq; XP_002411987.1; XM_002411942.1.
DR   AlphaFoldDB; B7Q6K4; -.
DR   STRING; 6945.B7Q6K4; -.
DR   PaxDb; 6945-B7Q6K4; -.
DR   EnsemblMetazoa; ISCW021567-RA; ISCW021567-PA; ISCW021567.
DR   KEGG; isc:IscW_ISCW021567; -.
DR   VEuPathDB; VectorBase:ISCI021567; -.
DR   VEuPathDB; VectorBase:ISCP_002345; -.
DR   VEuPathDB; VectorBase:ISCW021567; -.
DR   HOGENOM; CLU_027359_0_2_1; -.
DR   InParanoid; B7Q6K4; -.
DR   OMA; WVWRNIL; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR   GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IBA:GO_Central.
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; ACYL-COA DESATURASE; 1.
DR   PANTHER; PTHR11351:SF31; DESATURASE 1, ISOFORM A-RELATED; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PRINTS; PR00075; FACDDSATRASE.
DR   PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU000581};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU000581};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU000581};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000581};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000581};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        53..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          76..283
FT                   /note="Fatty acid desaturase"
FT                   /evidence="ECO:0000259|Pfam:PF00487"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EEC14476.1"
SQ   SEQUENCE   340 AA;  39933 MW;  A5265342CE948E37 CRC64;
     AHLDGKMLTI VPKEDDRIFP QIINSHSPAV SKPVSKEAEQ LQRFKTEIVW RNVAIFAILH
     SMALYGMYVA LYQAMWKTWI FAYFWGTFAG LGVTAGAHRL WSHRAYRARF PLRMALMVFN
     CMACQNDLYE WTRDHRVHHK FSETHADPHN VNRGFFFAHM GWLMCKKHPD VMRKGKAVDC
     SDLLRDPVIR FQKKYYVPLT TFFCFYLPAV LPHYMFGETY WNAFFVSTML RYVFSLNFTW
     LVNSAAHLWG CRPYDKHISP AENRFVSWAA IGEGFHNYHH TFPWDYSTSE LGWKLNFTTM
     FIDCMAAIGL AYDLKTVPKE VIEKRKTRTG DGSYDHLHLH
//
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