ID   A0A0N4ZDC5_PARTI        Unreviewed;      1050 AA.
AC   A0A0N4ZDC5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Sphingomyelin phosphodiesterase {ECO:0000313|WBParaSite:PTRK_0000557000.1};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000557000.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000557000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) +
CC         phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639,
CC         ChEBI:CHEBI:295975; EC=3.1.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00023999};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254;
CC         Evidence={ECO:0000256|ARBA:ARBA00023999};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the acid sphingomyelinase family.
CC       {ECO:0000256|ARBA:ARBA00008234}.
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DR   AlphaFoldDB; A0A0N4ZDC5; -.
DR   STRING; 131310.A0A0N4ZDC5; -.
DR   WBParaSite; PTRK_0000557000.1; PTRK_0000557000.1; PTRK_0000557000.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IEA:UniProt.
DR   CDD; cd00842; MPP_ASMase; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR045473; ASM_C.
DR   InterPro; IPR041805; ASMase/PPN1_MPP.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR011001; Saposin-like.
DR   InterPro; IPR008139; SaposinB_dom.
DR   PANTHER; PTHR10340; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR10340:SF34; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR   Pfam; PF19272; ASMase_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SMART; SM00741; SapB; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF47862; Saposin; 1.
DR   PROSITE; PS50015; SAP_B; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          517..600
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   COILED          259..286
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1050 AA;  121448 MW;  B1D6CEA204965CBB CRC64;
     MTLEDVCSQN IISKRILSNI DSLDDITNFM TTTYPLCNYL NTTPIKKTFS IPSNTFTITY
     EFFAQSYQYN WDNTTISYNG ERLSIGELYR YLLSKPKEYF EHINNIKIGV YGTHQYIEMS
     ILESFFECMA TFIDEIFELY PNAYSLNFDG NDFIVGFISQ HLRSKKIRKM KGLRLGPLID
     YCKEKPDVCH EMVNGLSNLE EMDIFINDPE LNYKGDYMKG LVPLLNHLSK KKNNKLSISG
     RREAEEMHVF KEFIELTLIN KLNVSLERLG SNNETLLNEF NNLNSDFSRF PASNITSLDI
     KISTVHILGL LFKSLPIFLN LKILNLDLKK SLLDEILNVT SGNIHNGNFN CEQFKEIPNV
     EKFCLKFQVD EKVEDYMERY ERLFPIMNDL TKEVLLNLND KIKILILESI PDLSQEMGNI
     LIRNCPNITD LILAPLNTID PRFIENMKNL NFLHLKHIFN LNIPKEIKII IVSHKKDSLS
     KELGDATTDD ANSYFQTQFN RTFKLPKLFD TQNDASNSLN CVACKLTMGS VIEMSRNNTP
     LSDIETYILN RCDEVKTQIH EICIGMAKSF TDEGVFVLKR TNYTADQICG AFIADCKSAD
     DPLNDMWKFD VPNGKPIVKG WPKVNKPQST LRVLHLTDIH IDLQYVVGSE ADCMTGDSND
     RMVCCREYSE VKNKTIKIPA GYWGSPHTCD IPYRTFINAM EHISKHDKFD YIIITGDFES
     HDMWEYTKSK TMSNVMNVSA VIESYFPNTP IYQATGNHEG VPMDAMGPHA MPEYSTRGPQ
     WLYNTFAQAW KRDLPPSTAT NIKYRASYSI KPFKGLKIIS LNTVYCSKNN FYNYLNQSDP
     DDTMAWLVNE LLESEKDNEK VHIISHIPPG STYCLKGWSF NFYDIVYRFE DTIGALIYGH
     VHKDYFQVYY ENGDINSRPY HVNYVAPSLT TFSNSNPAYR VYTVDGNYEG SSFTIIESET
     YYANLTETSE TKPPEWKLEY KLKEEYGMND LSPESFHNVT VKFEHDLELF DKYYLYYNRN
     YRSCKATCRM NAICALRSAR SYDKSNFCNE
//