ID A0A0V0TJE6_9BILA Unreviewed; 404 AA.
AC A0A0V0TJE6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE SubName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 1 {ECO:0000313|EMBL:KRX39148.1};
GN Name=sms-1 {ECO:0000313|EMBL:KRX39148.1};
GN ORFNames=T05_14570 {ECO:0000313|EMBL:KRX39148.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX39148.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX39148.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX39148.1};
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 sphingomyelin synthase family.
CC {ECO:0000256|ARBA:ARBA00005441}.
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:KRX39148.1}.
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DR EMBL; JYDJ01000242; KRX39148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TJE6; -.
DR STRING; 144512.A0A0V0TJE6; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290:SF27; PHOSPHATIDYLCHOLINE:CERAMIDE CHOLINEPHOSPHOTRANSFERASE 1; 1.
DR PANTHER; PTHR21290; SPHINGOMYELIN SYNTHETASE; 1.
DR Pfam; PF14360; PAP2_C; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRX39148.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 131..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 271..343
FT /note="Sphingomyelin synthase-like"
FT /evidence="ECO:0000259|Pfam:PF14360"
SQ SEQUENCE 404 AA; 46564 MW; 4A68F2406DF60D41 CRC64;
MSILREIDET FKNAQLCNDF YLALAEVNRR RRRRQSFRAT ATAAAGVVID LSYKQHKSRC
CCCCLRWRLF VFPLLWCMAT EDQQIMADRV KLNGHCVESD RGEETVLIEL CDNGETSSSS
IKKFPKEPKK LLLSVFLLFI AAMTNDVVLA WIHERVPETP PLPDLFFTLV PHFPNALAAS
EYLIMVSSGI MFIVCLLHRH RWILLRRVFL MLSLLYLGRC VCMLVTQVPV ADPTYFCSPK
SNNTTFGDVL LRALRLFSGA GLNIFGKHTF CGDYIFSGHT LILVMTYLVV KEYSPRRFWH
LHLLTWLVSA SGILCILLSR GHYSIDVVIA YFVTTRLFWL YHTLANSAEL KEYSVTNLMS
RECWFSLFRY MECNVAPSVP RQFEWPLSWP RCFKSASLGG SRLR
//
