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Database: UniProt
Entry: R0LL24_ANAPL
LinkDB: R0LL24_ANAPL
Original site: R0LL24_ANAPL 
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
//
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