ID K1W3C2_TRIAC Unreviewed; 440 AA.
AC K1W3C2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=sphingolipid 4-desaturase {ECO:0000256|ARBA:ARBA00012021};
DE EC=1.14.19.17 {ECO:0000256|ARBA:ARBA00012021};
GN ORFNames=A1Q2_02307 {ECO:0000313|EMBL:EKD03388.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD03388.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD03388.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD03388.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000256|ARBA:ARBA00006146}.
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:EKD03388.1}.
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DR EMBL; AMBO01000254; EKD03388.1; -; Genomic_DNA.
DR AlphaFoldDB; K1W3C2; -.
DR STRING; 1220162.K1W3C2; -.
DR eggNOG; KOG2987; Eukaryota.
DR HOGENOM; CLU_032156_0_1_1; -.
DR InParanoid; K1W3C2; -.
DR OMA; FEWVYND; -.
DR OrthoDB; 5485164at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR InterPro; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR PANTHER; PTHR12879; SPHINGOLIPID DELTA 4 DESATURASE/C-4 HYDROXYLASE PROTEIN DES2; 1.
DR PANTHER; PTHR12879:SF8; SPHINGOLIPID DELTA(4)-DESATURASE DES1; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR Pfam; PF08557; Lipid_DES; 1.
DR SMART; SM01269; Lipid_DES; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..110
FT /note="Sphingolipid delta4-desaturase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01269"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 49411 MW; C0A7496ABBCA16A0 CRC64;
MSAAVSAAAS AGATALPSPS KLKQRPRHSS PSDESVVSSG VTTELDSASA STPSTPTFAR
NDEPEPGKAA AGQGEDFLWM YTEEPHRSRR MAILKTHPEV RKLMGPTKWT AVIALSVLAL
QISLALYLRR FPTLSWQTLL TAYVVGGTAN QNTFLAIHEI THNLAFKSIK LNKALAIVVN
CAIAVPYAMA FKGYHIEHHK FLGEDGIDTD LPSRLEAVIL NNVAGKTFFA TFQLLFYALR
PGFIRSQRPT YWHFINLVTV LSFDALLVKF FGWRPVLYLL LSSFFAGSLH PCAAHFIAEH
YLLSRPDPDS VQHLALETTS YYGPLNVLTY NVGYHNEHHD FPSVPWTRLP ALRAMAPEFY
DTLPYHTSWP LVTWRFITDP KVGMWSRAKR EGRGERIDEH VWHGLYEKKG EETEDPFVEE
EEMRREMAEA VEIGYASDCE
//
