ID J4DAE3_THEOR Unreviewed; 390 AA.
AC J4DAE3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Sphingomyelin synthase-like domain-containing protein {ECO:0000259|Pfam:PF14360};
GN ORFNames=TOT_040000300 {ECO:0000313|EMBL:BAM41920.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41920.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM41920.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM41920.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
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}.
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DR EMBL; AP011949; BAM41920.1; -; Genomic_DNA.
DR RefSeq; XP_009692221.1; XM_009693926.1.
DR AlphaFoldDB; J4DAE3; -.
DR EnsemblProtists; BAM41920; BAM41920; TOT_040000300.
DR GeneID; 20716376; -.
DR KEGG; tot:TOT_040000300; -.
DR VEuPathDB; PiroplasmaDB:TOT_040000300; -.
DR eggNOG; ENOG502QWZH; Eukaryota.
DR OrthoDB; 5635266at2759; -.
DR Proteomes; UP000003786; Chromosome 4.
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:SF65; PHOSPHATIDYLINOSITOL:CERAMIDE INOSITOLPHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR21290; SPHINGOMYELIN SYNTHETASE; 1.
DR Pfam; PF14360; PAP2_C; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..266
FT /note="Sphingomyelin synthase-like"
FT /evidence="ECO:0000259|Pfam:PF14360"
SQ SEQUENCE 390 AA; 45493 MW; 2D05EDB9A9E06837 CRC64;
MLKAEVYSAK LTGSGKSSDS TKGFDDMNLL YKYDGEVSLE REVVEALNEG RKLIYGCLFR
MLILIPTFLL FYTFYRGMVF LIDVYFHDHT LERFLDRLHE NIDDRHLPFI NRMSDGLFYA
FVVVLMLRFI LFYPVLFNVQ VLLRFAYIYV FTYLLRGLAV IFTTIPSPYP YCVPLRISDK
WWKTYATMMF GEEGKLDCTG LLFSGRAFIM FLGLIILGQN SGPLFTMLMT LYALVTAVMI
VATKFHYTVD VMFSLLFAGS FYYFYYSRID SFGVYFLNKI NSAKHKEEED LKMSKLESSA
VTRGFAELEQ LPKLISVGHK LKSLQPLVYG SSNISDGVFK EYKSMVYFFG IKECDDLLSL
YRGTKSFNFS YWKRLRLKLR RRKLQSSILD
//
