ID A0A2G5VQX2_9PELO Unreviewed; 437 AA.
AC A0A2G5VQX2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=sphingomyelin phosphodiesterase {ECO:0000256|ARBA:ARBA00012369};
DE EC=3.1.4.12 {ECO:0000256|ARBA:ARBA00012369};
GN Name=Cni-T27F6.6 {ECO:0000313|EMBL:PIC54183.1};
GN Synonyms=Cnig_chr_I.g3542 {ECO:0000313|EMBL:PIC54183.1};
GN ORFNames=B9Z55_003542 {ECO:0000313|EMBL:PIC54183.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC54183.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC {ECO:0000256|ARBA:ARBA00006335}.
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:PIC54183.1}.
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DR EMBL; PDUG01000001; PIC54183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VQX2; -.
DR STRING; 1611254.A0A2G5VQX2; -.
DR Proteomes; UP000230233; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0043603; P:amide metabolic process; IEA:UniProt.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR038772; Sph/SMPD2-like.
DR PANTHER; PTHR16320:SF1; ENDONUCLEASE_EXONUCLEASE_PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G01540); 1.
DR PANTHER; PTHR16320; SPHINGOMYELINASE FAMILY MEMBER; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 369..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..321
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
SQ SEQUENCE 437 AA; 49929 MW; 965EE12ABDED404B CRC64;
MTSSNTTESE SLESGKDVEE PVIRRESFAA LRRNNVAPRQ LRVVTLNAWC LPQPWPIGST
DRVHRLQKIG EYMINEIYDI VGLQELWSYN DFVRLSEQVK DAYPYFHYFH SGFTGSGVCV
FSRHPIVSTL TSRYSLNGFA HHIHRGDWFG GKVVGLTEIE IDGDLRVNFY TTHLHAEYDR
ENDLYLPHRT AQSFELAQFV RHTARGADVV IVTGDLNMEP CDLGFRLILS HAKLFDAWRM
SHEVETTDGD DGELLKFRGI AKGGTCDRPD NCYSKKALRE KDDSKRIDYM LFKSGRCNVK
LEECEITLNQ IPGEDLNYSD HVGLRARFTI DDRFRHEKSL NTWEPNRPLL IEAIGIVAGG
ERRARTDRIF FLVLAGICLV LILGSLFFEV FPMGFAILRF ALTVIGVFFV WQGLIGLTLE
RKALKAAKQA MQQILNN
//
