ID   F1KXN2_ASCSU            Unreviewed;       458 AA.
AC   F1KXN2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Acid sphingomyelinase phosphodiesterase 3b {ECO:0000313|EMBL:ADY42636.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY42636.1};
RN   [1] {ECO:0000313|EMBL:ADY42636.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
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   EMBL; JI167613; ADY42636.1; -; mRNA.
DR   AlphaFoldDB; F1KXN2; -.
DR   EnsemblMetazoa; AgR003_g138_t03; AgR003_g138_t03; AgR003_g138.
DR   EnsemblMetazoa; AgR003_g138_t04; AgR003_g138_t04; AgR003_g138.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   PANTHER; PTHR10340:SF59; METALLOPHOS DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10340; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR   Pfam; PF19272; ASMase_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..458
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030168621"
FT   DOMAIN          21..276
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          290..428
FT                   /note="Sphingomyelin phosphodiesterase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19272"
SQ   SEQUENCE   458 AA;  52766 MW;  1F7F318C7F33C59C CRC64;
     MRIGQLLLLL QSVKLTLSTS VIQFTDFHLD KGYRAFGGDP KRMCHLNGQA TKNRTIGDFG
     NYNCDSPKAL VKHILTVASM TLRQPDFIIW TGDTFPHISD YSEKDVENLM YQTTLYLREA
     FPNIRVFPVF GNHDYSPSDQ LPDVDNTLYR VMFKHWVDWI GKEAMKTFRT GGYYVSDMND
     KTILLGLNTI LYYRNNHYKM SIANDPAGQF AFMRKQLDAA RDGNKTAHII AHIPPGAFEQ
     SPNVTWLKDK FNAELLQILR EYSDVIRSML FGHNHRDSFR LLKGENDSSL AALFIAPAVS
     PAQFNFPGST ANNPSFRIID YDEQWHITDI RQYYVSLPEL NKDPSTSAEF EYSFRHVYGI
     ESKYISAADI NNLIQRLKDD DRLFERYSFY NSVAASSTPF KGQWKDAHLC ALEYLDYDAY
     WSCLNQHHVT QPPPTDGISS SNVFPVLCFP IMYFILHF
//