Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acid sphingomyelinase-like phosphodiesterase 3a

Gene

Smpdl3a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP (PubMed:26792860). Has in vitro activity with p-nitrophenyl-TMP. Has lower activity with nucleoside diphosphates, and no activity with nucleoside monophosphates. Has in vitro activity with CDP-choline, giving rise to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine. Does not have sphingomyelin phosphodiesterase activity (By similarity).By similarity1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ per subunit.1 Publication

Enzyme regulationi

Requires micromolar levels of Zn2+ for activity. Inhibited by millimolar levels of Zn2+.1 Publication

Kineticsi

  1. KM=107 µM for ATP at pH 51 Publication
  2. KM=330 µM for ATP at pH 7.51 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi42Zinc 11 Publication1
    Metal bindingi44Zinc 11 Publication1
    Metal bindingi107Zinc 11 Publication1
    Metal bindingi107Zinc 21 Publication1
    Binding sitei111Substrate1 Publication1
    Metal bindingi148Zinc 21 Publication1
    Binding sitei148Substrate1 Publication1
    Binding sitei149Substrate1 Publication1
    Metal bindingi249Zinc 21 Publication1
    Binding sitei257Substrate1 Publication1
    Metal bindingi290Zinc 21 Publication1
    Metal bindingi292Zinc 11 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acid sphingomyelinase-like phosphodiesterase 3a (EC:3.1.4.-1 Publication)
    Short name:
    ASM-like phosphodiesterase 3a
    Gene namesi
    Name:Smpdl3a
    Synonyms:Asml3a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 10

    Organism-specific databases

    MGIiMGI:1931437. Smpdl3a.

    Subcellular locationi

    GO - Cellular componenti

    • extracellular exosome Source: MGI
    • extracellular region Source: UniProtKB
    • extracellular space Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi111H → A or Q: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi149H → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi149H → Q: Nearly abolishes enzyme activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 22Sequence analysisAdd BLAST22
    ChainiPRO_000000232923 – 445Acid sphingomyelinase-like phosphodiesterase 3aAdd BLAST423

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi59 ↔ 781 Publication
    Glycosylationi66N-linked (GlcNAc...)Sequence analysis1 Publication1
    Glycosylationi128N-linked (GlcNAc...)Sequence analysis1 Publication1
    Glycosylationi219N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi235N-linked (GlcNAc...)Sequence analysis1 Publication1
    Glycosylationi353N-linked (GlcNAc...)Sequence analysis1 Publication1
    Glycosylationi364N-linked (GlcNAc...)Sequence analysis1 Publication1
    Disulfide bondi417 ↔ 421Sequence analysis
    Disulfide bondi427 ↔ 4401 Publication

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    EPDiP70158.
    MaxQBiP70158.
    PaxDbiP70158.
    PeptideAtlasiP70158.
    PRIDEiP70158.

    PTM databases

    iPTMnetiP70158.
    PhosphoSitePlusiP70158.

    Expressioni

    Tissue specificityi

    Detected in blood serum (at protein level).1 Publication

    Gene expression databases

    BgeeiENSMUSG00000019872.
    CleanExiMM_SMPDL3A.
    ExpressionAtlasiP70158. baseline and differential.
    GenevisibleiP70158. MM.

    Interactioni

    Protein-protein interaction databases

    IntActiP70158. 2 interactors.
    MINTiMINT-4088461.
    STRINGi10090.ENSMUSP00000020022.

    Structurei

    Secondary structure

    1445
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi35 – 40Combined sources6
    Helixi55 – 57Combined sources3
    Helixi60 – 62Combined sources3
    Helixi82 – 94Combined sources13
    Beta strandi100 – 104Combined sources5
    Helixi114 – 116Combined sources3
    Helixi119 – 136Combined sources18
    Beta strandi141 – 144Combined sources4
    Beta strandi150 – 153Combined sources4
    Helixi163 – 172Combined sources10
    Turni173 – 175Combined sources3
    Helixi178 – 187Combined sources10
    Beta strandi190 – 193Combined sources4
    Beta strandi200 – 204Combined sources5
    Helixi207 – 210Combined sources4
    Helixi215 – 217Combined sources3
    Helixi223 – 225Combined sources3
    Helixi226 – 239Combined sources14
    Beta strandi243 – 250Combined sources8
    Beta strandi252 – 254Combined sources3
    Beta strandi258 – 260Combined sources3
    Beta strandi262 – 264Combined sources3
    Helixi266 – 278Combined sources13
    Turni279 – 282Combined sources4
    Beta strandi283 – 288Combined sources6
    Beta strandi295 – 300Combined sources6
    Beta strandi306 – 312Combined sources7
    Beta strandi331 – 337Combined sources7
    Turni339 – 341Combined sources3
    Beta strandi344 – 351Combined sources8
    Helixi354 – 360Combined sources7
    Beta strandi366 – 370Combined sources5
    Helixi371 – 375Combined sources5
    Helixi382 – 392Combined sources11
    Helixi398 – 407Combined sources10
    Turni408 – 410Combined sources3
    Helixi419 – 430Combined sources12
    Helixi434 – 444Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5FC1X-ray1.39A23-445[»]
    5FC5X-ray1.68A23-445[»]
    5FC6X-ray1.66A23-445[»]
    5FC7X-ray1.46A23-445[»]
    5FCAX-ray1.92A/B23-445[»]
    5FCBX-ray1.55A23-445[»]
    ProteinModelPortaliP70158.
    SMRiP70158.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acid sphingomyelinase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG410KDJ7. Eukaryota.
    ENOG410XRWF. LUCA.
    GeneTreeiENSGT00530000063095.
    HOGENOMiHOG000294197.
    HOVERGENiHBG050594.
    InParanoidiP70158.
    KOiK01128.
    OMAiDLWKPWL.
    OrthoDBiEOG091G080M.
    TreeFamiTF313674.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR017064. ASM-like_Pdiesterase_prd.
    IPR004843. Calcineurin-like_PHP_ApaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036767. ASM-like_PDE. 1 hit.
    SUPFAMiSSF56300. SSF56300. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P70158-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MALLGNFLCC LLVAWLCGPG LGVPLAPADR APAVGQFWHV TDLHLDPTYH
    60 70 80 90 100
    ITDDRTKVCA SSKGANASNP GPFGDVLCDS PYQLILSAFD FIKNSGQEAS
    110 120 130 140 150
    FMIWTGDSPP HVPVPELSTG TVIKVITNMT MTVQNLFPNL QVFPALGNHD
    160 170 180 190 200
    YWPQDQLPIV TSKVYSAVAD LWKPWLGEEA ISTLKKGGFY SQKVASNPGL
    210 220 230 240 250
    RIISLNTNLY YGPNIMTLNK TDPANQFEWL ENTLNSSLWN KEKVYIIAHV
    260 270 280 290 300
    PVGYLPYATD TPAIRQYYNE KLLDIFRRYS SVIAGQFYGH THRDSLMVLS
    310 320 330 340 350
    DKNGNPLNSV FVAPAVTPVK GVLQKETNNP GVRLFQYKPG DYTLLDMVQY
    360 370 380 390 400
    YLNLTEANLK GESNWTLEYV LTQAYSVADL QPKSLYALVQ QFATKDSKQF
    410 420 430 440
    LKYYHYYFVS YDSSATCDQH CKTLQVCAIM NLDSMSYDDC LKQHL
    Length:445
    Mass (Da):49,858
    Last modified:July 27, 2011 - v2
    Checksum:i20D986E3463CB720
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y08135 mRNA. Translation: CAA69329.1.
    AK151683 mRNA. Translation: BAE30607.1.
    AK152282 mRNA. Translation: BAE31096.1.
    CH466540 Genomic DNA. Translation: EDL05124.1.
    BC139288 mRNA. Translation: AAI39289.1.
    BC139289 mRNA. Translation: AAI39290.1.
    CCDSiCCDS23857.1.
    RefSeqiNP_065586.3. NM_020561.2.
    UniGeneiMm.2379.

    Genome annotation databases

    EnsembliENSMUST00000020022; ENSMUSP00000020022; ENSMUSG00000019872.
    GeneIDi57319.
    KEGGimmu:57319.
    UCSCiuc007fcu.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y08135 mRNA. Translation: CAA69329.1.
    AK151683 mRNA. Translation: BAE30607.1.
    AK152282 mRNA. Translation: BAE31096.1.
    CH466540 Genomic DNA. Translation: EDL05124.1.
    BC139288 mRNA. Translation: AAI39289.1.
    BC139289 mRNA. Translation: AAI39290.1.
    CCDSiCCDS23857.1.
    RefSeqiNP_065586.3. NM_020561.2.
    UniGeneiMm.2379.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5FC1X-ray1.39A23-445[»]
    5FC5X-ray1.68A23-445[»]
    5FC6X-ray1.66A23-445[»]
    5FC7X-ray1.46A23-445[»]
    5FCAX-ray1.92A/B23-445[»]
    5FCBX-ray1.55A23-445[»]
    ProteinModelPortaliP70158.
    SMRiP70158.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP70158. 2 interactors.
    MINTiMINT-4088461.
    STRINGi10090.ENSMUSP00000020022.

    PTM databases

    iPTMnetiP70158.
    PhosphoSitePlusiP70158.

    Proteomic databases

    EPDiP70158.
    MaxQBiP70158.
    PaxDbiP70158.
    PeptideAtlasiP70158.
    PRIDEiP70158.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000020022; ENSMUSP00000020022; ENSMUSG00000019872.
    GeneIDi57319.
    KEGGimmu:57319.
    UCSCiuc007fcu.1. mouse.

    Organism-specific databases

    CTDi10924.
    MGIiMGI:1931437. Smpdl3a.

    Phylogenomic databases

    eggNOGiENOG410KDJ7. Eukaryota.
    ENOG410XRWF. LUCA.
    GeneTreeiENSGT00530000063095.
    HOGENOMiHOG000294197.
    HOVERGENiHBG050594.
    InParanoidiP70158.
    KOiK01128.
    OMAiDLWKPWL.
    OrthoDBiEOG091G080M.
    TreeFamiTF313674.

    Miscellaneous databases

    ChiTaRSiSmpdl3a. mouse.
    PROiP70158.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSMUSG00000019872.
    CleanExiMM_SMPDL3A.
    ExpressionAtlasiP70158. baseline and differential.
    GenevisibleiP70158. MM.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR017064. ASM-like_Pdiesterase_prd.
    IPR004843. Calcineurin-like_PHP_ApaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036767. ASM-like_PDE. 1 hit.
    SUPFAMiSSF56300. SSF56300. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiASM3A_MOUSE
    AccessioniPrimary (citable) accession number: P70158
    Secondary accession number(s): Q3U8C2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: July 27, 2011
    Last modified: November 30, 2016
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.