ID F7I7S8_CALJA Unreviewed; 457 AA.
AC F7I7S8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Acid sphingomyelinase-like phosphodiesterase {ECO:0000256|PIRNR:PIRNR036767};
GN Name=SMPDL3B {ECO:0000313|Ensembl:ENSCJAP00000017384.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000017384.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000017384.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000017384.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR036767-51};
CC Note=Binds 2 Zn(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036767-51};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family.
CC {ECO:0000256|ARBA:ARBA00008234, ECO:0000256|PIRNR:PIRNR036767}.
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DR AlphaFoldDB; F7I7S8; -.
DR STRING; 9483.ENSCJAP00000017384; -.
DR Ensembl; ENSCJAT00000018386.4; ENSCJAP00000017384.4; ENSCJAG00000009490.5.
DR eggNOG; KOG3770; Eukaryota.
DR GeneTree; ENSGT00950000183182; -.
DR InParanoid; F7I7S8; -.
DR OMA; DSPWHLI; -.
DR OrthoDB; 205363at2759; -.
DR TreeFam; TF313674; -.
DR Proteomes; UP000008225; Chromosome 7.
DR Bgee; ENSCJAG00000009490; Expressed in kidney and 5 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006685; P:sphingomyelin catabolic process; IEA:InterPro.
DR CDD; cd00842; MPP_ASMase; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR017064; ASM-like_Pdiesterase_prd.
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:SF25; ACID SPHINGOMYELINASE-LIKE PHOSPHODIESTERASE 3B; 1.
DR PANTHER; PTHR10340; SPHINGOMYELIN PHOSPHODIESTERASE; 1.
DR Pfam; PF19272; ASMase_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036767; ASM-like_PDE; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036767};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR036767};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036767};
KW Signal {ECO:0000256|PIRNR:PIRNR036767};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR036767}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|PIRNR:PIRNR036767"
FT CHAIN 19..457
FT /note="Acid sphingomyelinase-like phosphodiesterase"
FT /evidence="ECO:0000256|PIRNR:PIRNR036767"
FT /id="PRO_5035350915"
FT DOMAIN 22..280
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 293..430
FT /note="Sphingomyelin phosphodiesterase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19272"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036767-51"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036767-51"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036767-51"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036767-51"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036767-51"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036767-51"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR036767-51"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036767-51"
SQ SEQUENCE 457 AA; 50964 MW; 8C126FB6FBD80459 CRC64;
MRLLTWLIFL AYFGGAGAEP GKFWHIADLH LDPDYKVSKD PFQVCPSAGS QPVPNAGPWG
DYLCDSPWAL INSSIYAMKE INPEPDFILW TGDNTPHVPD KKLGEAAVLE IVERLTKLIR
EVFPDTNVYA ALGNHDFHPK NQFPVGSNKI YNQIAELWKP WLSNESIALF KKGAFYSEKL
PGPSRSGRIV VLNTNLYYTS NALTADMADP GQQFQWLEDV LTNASKAGDM VYIVGHVPPG
FFEKTENKAW FWKGFNEKYL KVVRKHHRVI AGQFFGHHHT DSFRMLYDDA GAPISAMFIT
PGVTPWKTTL PGVVNGANNP AIRVFEYDQA TLSLKDMVTY FVNLSQANAL GKPRWELEYR
LTEAFGVPDA SARSMEAVLD HIAGDQGALQ RYYAYNSVSY DAGICDEACS TQHVCAMRQV
DFNAYTACLY ASGADPMPQF LLLLLLAALL VLCTLAL
//
