ID A0A210QS86_MIZYE Unreviewed; 381 AA.
AC A0A210QS86;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acyl-CoA desaturase {ECO:0000313|EMBL:OWF51602.1};
GN ORFNames=KP79_PYT06480 {ECO:0000313|EMBL:OWF51602.1};
OS Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC Mizuhopecten.
OX NCBI_TaxID=6573 {ECO:0000313|EMBL:OWF51602.1, ECO:0000313|Proteomes:UP000242188};
RN [1] {ECO:0000313|Proteomes:UP000242188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PY_sf001 {ECO:0000313|Proteomes:UP000242188};
RX PubMed=28812685; DOI=10.1038/s41559-017-0120;
RA Wang S., Zhang J., Jiao W., Li J., Xun X., Sun Y., Guo X., Huan P.,
RA Dong B., Zhang L., Hu X., Sun X., Wang J., Zhao C., Wang Y., Wang D.,
RA Huang X., Wang R., Lv J., Li Y., Zhang Z., Liu B., Lu W., Hui Y., Liang J.,
RA Zhou Z., Hou R., Li X., Liu Y., Li H., Ning X., Lin Y., Zhao L., Xing Q.,
RA Dou J., Li Y., Mao J., Guo H., Dou H., Li T., Mu C., Jiang W., Fu Q.,
RA Fu X., Miao Y., Liu J., Yu Q., Li R., Liao H., Li X., Kong Y., Jiang Z.,
RA Chourrout D., Li R., Bao Z.;
RT "Scallop genome provides insights into evolution of bilaterian karyotype
RT and development.";
RL Nat. Ecol. Evol. 1:120-120(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWF51602.1}.
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DR EMBL; NEDP02002201; OWF51602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A210QS86; -.
DR STRING; 6573.A0A210QS86; -.
DR EnsemblMetazoa; XM_021495471.1; XP_021351146.1; LOC110448949.
DR Proteomes; UP000242188; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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:UP000242188};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..312
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 381 AA; 43483 MW; 007F45AE034DA408 CRC64;
MVSTAVPMLR RDVIRLSCIT ISFSLLVTIM AISRTQTTTL RHEKGGDVMD ENDKLGLDSA
ETFVGRDYKI NGHPWPYRAK GIILFTLLHI GAVIGVCCLH QIKLLTWIFG CVLHVFCQIS
ITAGNHRLWA HRTYKAKLPL RIVLMIGQTT TVQNDIFKWA LDHRVHHKYT DTDADPHNAK
RGFFFSHIGW LLLNKLPEFN EKSKNIDVSD LLADPVVTFQ LRYYTALCTM FGFVMPALVP
WGLWGEDFLA AFFTAGILRC VIGHHTTFLV NSAAHAWGNK PYDIRIDPGE NIAVSVLTTG
EGFHNFHHVF PQDYRTSEHG WRFNLSTAFI DTMSAIGQVT DRRYVSDDVI RRRQKRTDCK
KLVLLFSAKD LCKIHKRSKN I
//
