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Q04519

- ASM_MOUSE

UniProt

Q04519 - ASM_MOUSE

Protein

Sphingomyelin phosphodiesterase

Gene

Smpd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Converts sphingomyelin to ceramide. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol.

    Catalytic activityi

    Sphingomyelin + H2O = N-acylsphingosine + phosphocholine.

    GO - Molecular functioni

    1. hydrolase activity, acting on glycosyl bonds Source: UniProtKB-KW
    2. sphingomyelin phosphodiesterase activity Source: UniProtKB-EC

    GO - Biological processi

    1. ceramide biosynthetic process Source: Ensembl
    2. negative regulation of MAP kinase activity Source: Ensembl
    3. positive regulation of apoptotic process Source: Ensembl
    4. positive regulation of protein dephosphorylation Source: Ensembl
    5. response to cocaine Source: Ensembl
    6. response to drug Source: Ensembl
    7. sphingomyelin catabolic process Source: InterPro
    8. termination of signal transduction Source: Ensembl

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_199008. Glycosphingolipid metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sphingomyelin phosphodiesterase (EC:3.1.4.12)
    Alternative name(s):
    Acid sphingomyelinase
    Short name:
    aSMase
    Gene namesi
    Name:Smpd1
    Synonyms:Asm
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:98325. Smpd1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: Ensembl
    2. lamellar body Source: Ensembl
    3. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4444Sequence AnalysisAdd
    BLAST
    Chaini45 – 627583Sphingomyelin phosphodiesterasePRO_0000002324Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi84 – 841N-linked (GlcNAc...)PROSITE-ProRule annotation
    Disulfide bondi87 ↔ 163PROSITE-ProRule annotation
    Disulfide bondi90 ↔ 155PROSITE-ProRule annotation
    Disulfide bondi118 ↔ 129PROSITE-ProRule annotation
    Glycosylationi173 – 1731N-linked (GlcNAc...)PROSITE-ProRule annotation
    Disulfide bondi219 ↔ 224PROSITE-ProRule annotation
    Disulfide bondi225 ↔ 248PROSITE-ProRule annotation
    Glycosylationi333 – 3331N-linked (GlcNAc...)PROSITE-ProRule annotation
    Disulfide bondi383 ↔ 429PROSITE-ProRule annotation
    Glycosylationi393 – 3931N-linked (GlcNAc...)PROSITE-ProRule annotation
    Glycosylationi518 – 5181N-linked (GlcNAc...)PROSITE-ProRule annotation
    Disulfide bondi582 ↔ 586PROSITE-ProRule annotation
    Disulfide bondi592 ↔ 605PROSITE-ProRule annotation
    Glycosylationi611 – 6111N-linked (GlcNAc...)PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ04519.
    PRIDEiQ04519.

    PTM databases

    PhosphoSiteiQ04519.

    Expressioni

    Gene expression databases

    BgeeiQ04519.
    CleanExiMM_SMPD1.
    GenevestigatoriQ04519.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    MINTiMINT-1604473.

    Structurei

    3D structure databases

    ProteinModelPortaliQ04519.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini83 – 16785Saposin B-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the acid sphingomyelinase family.Curated
    Contains 1 saposin B-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG303902.
    GeneTreeiENSGT00530000063095.
    HOGENOMiHOG000008599.
    HOVERGENiHBG004288.
    InParanoidiQ04519.
    KOiK12350.
    OMAiADPLCCR.
    OrthoDBiEOG79PJP3.
    PhylomeDBiQ04519.
    TreeFamiTF313674.

    Family and domain databases

    Gene3Di1.10.225.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR011001. Saposin-like.
    IPR008139. SaposinB.
    IPR011160. Sphingomy_PDE.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000948. Sphingomy_PDE. 1 hit.
    SMARTiSM00741. SapB. 1 hit.
    [Graphical view]
    SUPFAMiSSF47862. SSF47862. 1 hit.
    SSF56300. SSF56300. 1 hit.
    PROSITEiPS50015. SAP_B. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q04519-1 [UniParc]FASTAAdd to Basket

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    MPHHRASSGQ DHLRAGWEQR LERSLPAPRV GLLWMGLGLA LVLALFDSTV    50
    LWVPARAYPL PSEGHSVKFS AIAPPLQSAF GWQNLTCPAC KVLFTALNHG 100
    LKKEPNVARV GSVAIKICKM LNIAPLDVCQ SAVHLFEDDV VEVWTRSVLS 150
    PSEACGLLLG SSCGHWDIFS TWNISLPSVP KPPPKPPSPP APGAPVSRVL 200
    FLTDLHWDHE YLEGTDPYCA DPLCCRRGSG WPPNSQKGAG FWGEYSKCDL 250
    PLRTLESLLK GLGPAGPFEM VYWTGDIPAH DVWQQSRQDQ LRALTTITDL 300
    VRKFLGPVPV YPAVGNHEST PVNGFPPPFI KGNQSSQWLY EAMAKAWEPW 350
    LPADALHTLR IGGFYALTPR PGLRLISLNM NFCSRENFWL LINSTDPAGQ 400
    LQWLVEELQA AENRGDKVHI IGHIPPGHCL KSWSWNYYKI IARYENTLAG 450
    QFFGHTHVDE FEIFYDEETL SRPLAVAFLA PSATTFINLN PGYRVYQIDG 500
    NYPGSSHVVL DHETYILNLT QANAAGGTPS WKRLYRARET YGLPDAMPAS 550
    WHNLVYRMRD DEQLFQTFWF LYHKGHPPSE PCGTPCRLAT LCAQLSARAD 600
    SPALCRHLMP NGSLPDANRL WSRPLLC 627
    Length:627
    Mass (Da):69,927
    Last modified:February 1, 1996 - v2
    Checksum:i0FFC7EA74EE71E91
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481S → T in AAH11304. (PubMed:15489334)Curated
    Sequence conflicti450 – 4501G → S in AAH11304. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z14252 mRNA. Translation: CAA78619.1.
    Z14132 Genomic DNA. Translation: CAA78506.1.
    AK088147 mRNA. Translation: BAC40171.1.
    AK145534 mRNA. Translation: BAE26489.1.
    AK145702 mRNA. Translation: BAE26598.1.
    AK164167 mRNA. Translation: BAE37659.1.
    BC011304 mRNA. Translation: AAH11304.1.
    CCDSiCCDS21653.1.
    PIRiA58720. S27393.
    RefSeqiNP_035551.1. NM_011421.2.
    UniGeneiMm.4628.

    Genome annotation databases

    EnsembliENSMUST00000046983; ENSMUSP00000042187; ENSMUSG00000037049.
    GeneIDi20597.
    KEGGimmu:20597.
    UCSCiuc009iyf.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z14252 mRNA. Translation: CAA78619.1 .
    Z14132 Genomic DNA. Translation: CAA78506.1 .
    AK088147 mRNA. Translation: BAC40171.1 .
    AK145534 mRNA. Translation: BAE26489.1 .
    AK145702 mRNA. Translation: BAE26598.1 .
    AK164167 mRNA. Translation: BAE37659.1 .
    BC011304 mRNA. Translation: AAH11304.1 .
    CCDSi CCDS21653.1.
    PIRi A58720. S27393.
    RefSeqi NP_035551.1. NM_011421.2.
    UniGenei Mm.4628.

    3D structure databases

    ProteinModelPortali Q04519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1604473.

    PTM databases

    PhosphoSitei Q04519.

    Proteomic databases

    PaxDbi Q04519.
    PRIDEi Q04519.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000046983 ; ENSMUSP00000042187 ; ENSMUSG00000037049 .
    GeneIDi 20597.
    KEGGi mmu:20597.
    UCSCi uc009iyf.2. mouse.

    Organism-specific databases

    CTDi 6609.
    MGIi MGI:98325. Smpd1.

    Phylogenomic databases

    eggNOGi NOG303902.
    GeneTreei ENSGT00530000063095.
    HOGENOMi HOG000008599.
    HOVERGENi HBG004288.
    InParanoidi Q04519.
    KOi K12350.
    OMAi ADPLCCR.
    OrthoDBi EOG79PJP3.
    PhylomeDBi Q04519.
    TreeFami TF313674.

    Enzyme and pathway databases

    Reactomei REACT_199008. Glycosphingolipid metabolism.

    Miscellaneous databases

    ChiTaRSi SMPD1. mouse.
    NextBioi 298915.
    PROi Q04519.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q04519.
    CleanExi MM_SMPD1.
    Genevestigatori Q04519.

    Family and domain databases

    Gene3Di 1.10.225.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR011001. Saposin-like.
    IPR008139. SaposinB.
    IPR011160. Sphingomy_PDE.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000948. Sphingomy_PDE. 1 hit.
    SMARTi SM00741. SapB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47862. SSF47862. 1 hit.
    SSF56300. SSF56300. 1 hit.
    PROSITEi PS50015. SAP_B. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the acid sphingomyelinase of the mouse and the organization and complete nucleotide sequence of the gene."
      Newrzella D., Stoffel W.
      Biol. Chem. Hoppe-Seyler 373:1233-1238(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    2. Hofmann K.
      Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 224-225 AND 384.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Hippocampus and Thymus.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

    Entry informationi

    Entry nameiASM_MOUSE
    AccessioniPrimary (citable) accession number: Q04519
    Secondary accession number(s): Q3UL52
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are two types of sphingomyelinases: ASM (acid), and NSM (neutral).

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3