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Database: UniProt
Entry: A0A261C2M2_9PELO
LinkDB: A0A261C2M2_9PELO
Original site: A0A261C2M2_9PELO 
ID   A0A261C2M2_9PELO        Unreviewed;       411 AA.
AC   A0A261C2M2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Sphingomyelin synthase-like domain-containing protein {ECO:0000259|Pfam:PF14360};
DE   Flags: Fragment;
GN   ORFNames=FL83_08975 {ECO:0000313|EMBL:OZG16809.1};
OS   Caenorhabditis latens.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG16809.1, ECO:0000313|Proteomes:UP000216463};
RN   [1] {ECO:0000313|EMBL:OZG16809.1, ECO:0000313|Proteomes:UP000216463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX534 {ECO:0000313|EMBL:OZG16809.1,
RC   ECO:0000313|Proteomes:UP000216463};
RA   Fierst J.L.;
RT   "Caenorhabditis latens genome sequence.";
RL   Submitted (JUL-2017) 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:OZG16809.1}.
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DR   EMBL; NIPN01000043; OZG16809.1; -; Genomic_DNA.
DR   STRING; 1503980.A0A261C2M2; -.
DR   Proteomes; UP000216463; 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:SF34; PHOSPHATIDYLCHOLINE:CERAMIDE CHOLINEPHOSPHOTRANSFERASE 3-RELATED; 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:UP000216463};
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        96..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        138..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          235..307
FT                   /note="Sphingomyelin synthase-like"
FT                   /evidence="ECO:0000259|Pfam:PF14360"
FT   REGION          58..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OZG16809.1"
SQ   SEQUENCE   411 AA;  46111 MW;  09F7B2B3CDE704C8 CRC64;
     MVKTVEFCEI VPRSFQYSIE TDDSLCGDEE RQHHTNINHS NGIGGGCCHH QSITSMGSVS
     KGGGGITSTV ISARGAPEDE DTESDSRRRR PQWLKCLFLG CFLLIAGISN WAVIAYTHDY
     VPRQPLPDVV FSLVGEQRWA SSLGDACVAL CIVLLGGLLV IHKHRTTVLK RVIFCAATLY
     AMRSIXLAAT QLPSGYTDNQ GRCREQVESK ASIFFGRLFE QTIRIGFQSK DQMLCGDLLF
     SGHTLVMVTC SLAVAYYLPK SIKPLQWLAH LSCFVGMICM IISRTHYTID VIIAYWLSNM
     VFRIYHAYCE LDMCMERHKS ILYSWWPCKI IDWLEEDIVP GRLDNRCSFP WSRWTHRHGS
     GGRRERGGAN HNEPVSSDSS STTCDTTTNT TTNHHQKHVS ISSSSTYPLP C
//
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