ID A0A0V1MCF8_9BILA Unreviewed; 372 AA.
AC A0A0V1MCF8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=sphingolipid 4-desaturase {ECO:0000256|ARBA:ARBA00012021};
DE EC=1.14.19.17 {ECO:0000256|ARBA:ARBA00012021};
DE Flags: Fragment;
GN Name=ttm-5 {ECO:0000313|EMBL:KRZ69122.1};
GN ORFNames=T10_4863 {ECO:0000313|EMBL:KRZ69122.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ69122.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ69122.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ69122.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ69122.1}.
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DR EMBL; JYDO01000144; KRZ69122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MCF8; -.
DR STRING; 268474.A0A0V1MCF8; -.
DR Proteomes; UP000054843; 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 PIRSF; PIRSF017228; Sphnglp_dlt4_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:UP000054843};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..58
FT /note="Sphingolipid delta4-desaturase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01269"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ69122.1"
SQ SEQUENCE 372 AA; 43810 MW; 728161CC832163E2 CRC64;
LNSKLKKVFV ILFFKMGAKV SRNNFDWSYT EEPHATRRNL ILKKHPEIAA LFGFDQAFIY
VVTCIVITQF IFCYLLKDSD WTLIFLQSYF SGGLYNHALM LAIHEIAHNA AFGNCKPLWN
RLFGIFANFP IPLPFSVSFK KYHIEHHRYM GEELLDTDVP TLFEARLFTN SFRKLIWLFF
QPFFYAFRPL VIYHKAVSDL EILNFIVQMT VNYFVIQYFG WKSFTFLILS MILSMGIHPT
AGHFISEHYV FKPGQETYSY YGPLNLVTFN VGYHVEHHDF PSIPGVRLPL VRKIAPEYYD
HLMHHESWTW VLWKFVFDPT VGPYARIKRP ARVPLNHSAA NYFIDYVAIL KRIAKWFRLA
VYPSCPVPTE VH
//
