ID R0LL24_ANAPL Unreviewed; 365 AA.
AC R0LL24;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 2 {ECO:0000313|EMBL:EOB01153.1};
DE SubName: Full=Sphingomyelin synthase 2 {ECO:0000313|Ensembl:ENSAPLP00020025562.1};
DE Flags: Fragment;
GN Name=SGMS2 {ECO:0000313|Ensembl:ENSAPLP00020025562.1};
GN ORFNames=Anapl_04779 {ECO:0000313|EMBL:EOB01153.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB01153.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|EMBL:EOB01153.1}
RP NUCLEOTIDE SEQUENCE.
RA Li N.;
RT "The genome sequence and transcriptome of duck provide insight into the
RT interaction host.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
RN [3] {ECO:0000313|Ensembl:ENSAPLP00020025562.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; KB743113; EOB01153.1; -; Genomic_DNA.
DR RefSeq; XP_005019881.1; XM_005019824.2.
DR RefSeq; XP_005019882.1; XM_005019825.2.
DR RefSeq; XP_005019883.1; XM_005019826.2.
DR RefSeq; XP_005019884.1; XM_005019827.2.
DR RefSeq; XP_012955327.1; XM_013099873.1.
DR RefSeq; XP_012955329.1; XM_013099875.1.
DR RefSeq; XP_012955330.1; XM_013099876.1.
DR Ensembl; ENSAPLT00020027558.1; ENSAPLP00020025562.1; ENSAPLG00020017548.1.
DR GeneID; 101791169; -.
DR KEGG; apla:101791169; -.
DR CTD; 166929; -.
DR OrthoDB; 1343173at2759; -.
DR Proteomes; UP000296049; Unassembled WGS sequence.
DR Proteomes; UP000694400; 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 CDD; cd01610; PAP2_like; 1.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290:SF24; PHOSPHATIDYLCHOLINE:CERAMIDE CHOLINEPHOSPHOTRANSFERASE 2; 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:UP000296049};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EOB01153.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 221..293
FT /note="Sphingomyelin synthase-like"
FT /evidence="ECO:0000259|Pfam:PF14360"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 365
FT /evidence="ECO:0000313|EMBL:EOB01153.1"
SQ SEQUENCE 365 AA; 42348 MW; 967C1E430C67579D CRC64;
MNTIETAKLE EHMEGQNNDA SNGYTRPTLS VSEENKNGNS KPKGLSNGLR KTAKKYPDYI
QIAMPAETRN KFPLEWWKTG IAFVYALFNL ILTTVMITVV HERVPPKELS PPLPDKFFDY
VDRVKWAFSV SEINGMILVG LWIFQWLFLR YKSIVGRRFF FIIGTLYLYR CITMYVTTLP
VPGMHFQCAP KLNGDSQAKL QRILRLISGG GLSITGSHIL CGDFLFSGHT VVLTLIYLFI
KEYSPRHFWW YHLICWLMSA AGIICILVAH EHYTVDVVIA YYITTRLFWW YHSMANEKTL
KVSSQTNFLS RAWWYPIFYF FEKNVQGSVP CSFSWPISWP PSCFKSSCKK YSRVQKMGED
NEKST
//