ASM3A_RAT
ID ASM3A_RAT Reviewed; 445 AA.
AC Q641Z7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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; Synonyms=Asml3a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC082029; AAH82029.1; -; mRNA.
DR RefSeq; NP_001005539.1; NM_001005539.1.
DR AlphaFoldDB; Q641Z7; -.
DR SMR; Q641Z7; -.
DR STRING; 10116.ENSRNOP00000001081; -.
DR GlyGen; Q641Z7; 6 sites.
DR PaxDb; Q641Z7; -.
DR PRIDE; Q641Z7; -.
DR Ensembl; ENSRNOT00000001081; ENSRNOP00000001081; ENSRNOG00000000815.
DR GeneID; 294422; -.
DR KEGG; rno:294422; -.
DR UCSC; RGD:1359277; rat.
DR CTD; 10924; -.
DR RGD; 1359277; Smpdl3a.
DR eggNOG; KOG3770; Eukaryota.
DR GeneTree; ENSGT00950000183182; -.
DR HOGENOM; CLU_014743_0_0_1; -.
DR InParanoid; Q641Z7; -.
DR OMA; AIIMGHI; -.
DR OrthoDB; 1142100at2759; -.
DR PhylomeDB; Q641Z7; -.
DR TreeFam; TF313674; -.
DR PRO; PR:Q641Z7; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000815; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q641Z7; RN.
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..445
FT /note="Acid sphingomyelinase-like phosphodiesterase 3a"
FT /id="PRO_0000002330"
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 66
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 364
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 445 AA; 49896 MW; F85CDFFE1063B323 CRC64;
MALPGNFLCC LLVAWLCDPG LGVPLAPAYG APAVGQFWHV TDLHLDPTYH ITDDHTKVCA
SSKGANVSNP GPFGDVLCDS PYQLILSAFD FIKNSGQEAS FMIWTGDSPP HVPVRELSTG
SVIEVITNMT VTVQNLFPNL QVFPALGNHD YWPQDQLPIA TSKVYSAVSD LWKPWLDEEA
ISTLRKGGFY SQKVASNPDL RIISLNTNLY YGPNIMTLNK TDPANQFEWL ENTLNSSLRN
KEKVYVIAHV PVGYLPYATK TPAMRQYYNE KLVDIFRRYS SVIAGQFYGH THRDSLMVLS
DKNGNPINSV FVAPAVTPVK GVLEKETNNP GVRLFQYKPG DYTLLDMLQY YLNLTEANLK
GESNWTLEYT LTQAYGVADL QPKSLHGLAQ QLATIDSKQF LKYYHYFFVS YDSSAPCDQR
CKTLQICAIM NLDLVSYEDC LKRHL
