ASM3A_BOVIN
ID ASM3A_BOVIN Reviewed; 450 AA.
AC Q3ZC91;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Acid sphingomyelinase-like phosphodiesterase 3a;
DE Short=ASM-like phosphodiesterase 3a;
DE EC=3.1.4.-;
DE Flags: Precursor;
GN Name=SMPDL3A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has in vitro nucleotide phosphodiesterase activity with
CC nucleoside triphosphates, such as ATP. Has in vitro activity with p-
CC nitrophenyl-TMP. Has lower activity with nucleoside diphosphates, and
CC no activity with nucleoside monophosphates. Has in vitro activity with
CC CDP-choline, giving rise to CMP and phosphocholine. Has in vitro
CC activity with CDP-ethanolamine. Does not have sphingomyelin
CC phosphodiesterase activity. {ECO:0000250|UniProtKB:Q92484}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q92484};
CC Note=Binds 2 Zn(2+) per subunit. {ECO:0000250|UniProtKB:Q92484};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q92484}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q92484}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92484}.
CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family. {ECO:0000305}.
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DR EMBL; BC102796; AAI02797.1; -; mRNA.
DR RefSeq; NP_001030191.1; NM_001035019.2.
DR AlphaFoldDB; Q3ZC91; -.
DR SMR; Q3ZC91; -.
DR STRING; 9913.ENSBTAP00000028765; -.
DR PaxDb; Q3ZC91; -.
DR PRIDE; Q3ZC91; -.
DR GeneID; 505300; -.
DR KEGG; bta:505300; -.
DR CTD; 10924; -.
DR eggNOG; KOG3770; Eukaryota.
DR InParanoid; Q3ZC91; -.
DR OrthoDB; 1142100at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; ISS:UniProtKB.
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 Pfam; PF19272; ASMase_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036767; ASM-like_PDE; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..450
FT /note="Acid sphingomyelinase-like phosphodiesterase 3a"
FT /id="PRO_0000288776"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..78
FT /evidence="ECO:0000250|UniProtKB:Q92484"
FT DISULFID 417..421
FT /evidence="ECO:0000255"
FT DISULFID 427..440
FT /evidence="ECO:0000250|UniProtKB:Q92484"
SQ SEQUENCE 450 AA; 51221 MW; 84311DE73ADEC1DF CRC64;
MARLGALVCC LLAAWHCRPG LGLPLAPAGT GPAVGQFWHV TDFHLDPTYH ITGDHTKVCA
SSKGAEASDP GPFGDVMCDS PYRLIFSALD FIKNSGQKVS FMIWTGDSPP HVPVLELSTD
KVINVTANIT TTIQRLFPNL QVFPALGNHD YWPQDQLPVV NSKVYNAVAN LWKPWLTEDA
ITTLRKGGFY TQKVSNNPKL RIISLNTNLY YGPNSVTLNQ TDPANQFEWL ENTLNISQQN
KEKVYIIAHV PVGYLPYARG ISAMRKYHNE KLIDIFRKYS DIIAGQFYGH THRDSIMVLS
DKKGKPVNSL FVAPAVTPVR SVLERLTNNP GVRLFQYDPR DYKLLDMLQY YLNLTDANLK
GESNWKLEYN LTQAYDIQDL QPKSLYKLAK QFAIQESKQF IKYYKYFFVS YDSSVICQGK
CKIFQICAIM NLDVISYTDC FRQYHMKHRL
