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Entry version 162 (07 Apr 2021)
Sequence version 2 (01 Feb 1996)
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Protein

Sphingomyelin phosphodiesterase

Gene

Smpd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Converts sphingomyelin to ceramide (PubMed:9660788, PubMed:8706124). Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly. However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form (By similarity).By similarity2 Publications
In the lysosomes, converts sphingomyelin to ceramide. Plays an important role in the export of cholesterol from the intraendolysosomal membranes. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol (PubMed:27435900). Modulates stress-induced apoptosis through the production of ceramide (PubMed:8706124).2 Publications
When secreted, modulates cell signaling with its ability to reorganize the plasma membrane by converting sphingomyelin to ceramide. Secreted form is increased in response to stress and inflammatory mediators such as IL1B, IFNG or TNF as well as upon infection with bacteria and viruses. Produces the release of ceramide in the outer leaflet of the plasma membrane playing a central role in host defense. Ceramide reorganizes these rafts into larger signaling platforms that are required to internalize P. aeruginosa, induce apoptosis and regulate the cytokine response in infected cells. In wounded cells, the lysosomal form is released extracellularly in the presence of Ca2+ and promotes endocytosis and plasma membrane repair.By similarity
(Microbial infection) Secretion is activated by bacteria such as P. aeruginos, this activation results in the release of ceramide in the outer leaflet of the plasma membrane which facilitates the infection.1 Publication

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit (PubMed:27435900).

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Hydrolysis of liposomal sphingomyelin is stimulated by incorporation of diacylglycerol (DAG), ceramide and free fatty acids into the liposomal membranes. Phosphatidylcholine hydrolysis is inhibited by incorporation of cholesterol, ceramide, DAG, monoacylglycerol and fatty acids.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi204Zinc 1Combined sources1 Publication1
Metal bindingi206Zinc 1; via tele nitrogenCombined sources1 Publication1
Metal bindingi276Zinc 1Combined sources1 Publication1
Metal bindingi276Zinc 2Combined sources1 Publication1
Metal bindingi316Zinc 2Combined sources1 Publication1
Metal bindingi423Zinc 2; via tele nitrogenCombined sources1 Publication1
Metal bindingi455Zinc 2; via pros nitrogenCombined sources1 Publication1
Metal bindingi457Zinc 1; via tele nitrogenCombined sources1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1660662, Glycosphingolipid metabolism

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sphingomyelin phosphodiesterase (EC:3.1.4.122 Publications)
Alternative name(s):
Acid sphingomyelinase
Short name:
ASMase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Smpd11 Publication
Synonyms:Asm1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:98325, Smpd1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Lipid droplet, Lysosome, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutants infected with Pseudomonas aeruginosa die within 7 days whereas all wild-type mice survive the infection (PubMed:12563314). Mutants are defective in radiation-induced apoptosis (PubMed:8706124).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi128V → E: Retains 20% of wild-type activity with sphingomyelin as substrate; retains 70% of wild-type activity with bis(p-nitrophenyl) phosphate as substrate. 1 Publication1
Mutagenesisi143V → R: Retains 10% of wild-type activity with sphingomyelin as substrate; retains 70% of wild-type activity with bis(p-nitrophenyl) phosphate as substrate. 1 Publication1
Mutagenesisi280H → A: Complete loss of activity. 1 Publication1
Mutagenesisi283W → N: Retains 10% of wild-type activity. 1 Publication1
Mutagenesisi317H → A: No activity with sphingomyelin as substrate; retains 70% of wild-type activity with bis(p-nitrophenyl) phosphate as substrate. 1 Publication1
Mutagenesisi321P → E: Retains 10% of wild-type activity. 1 Publication1
Mutagenesisi388F → R: Retains 10% of wild-type activity. 1 Publication1
Mutagenesisi391L → R: Retains 20% of wild-type activity with sphingomyelin as substrate; retains 50% of wild-type activity with bis(p-nitrophenyl) phosphate as substrate. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4295802

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 44Sequence analysisAdd BLAST44
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000232445 – 627Sphingomyelin phosphodiesteraseAdd BLAST583

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi84N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi87 ↔ 163PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi90 ↔ 155PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi118 ↔ 129PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi173N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
Disulfide bondi219 ↔ 224PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi225 ↔ 248PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi333N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
Disulfide bondi383 ↔ 429PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi393N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei506PhosphoserineBy similarity1
Glycosylationi518N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
Disulfide bondi582 ↔ 586PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi592 ↔ 605PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi611N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Proteolytically processed. Mature lysosomal form arises from C-terminal proteolytic processing of pro-sphingomyelin phosphodiesterase.By similarity
Both lysosomal and secreted forms are glycosylated but they show a differential pattern of glycosylation.By similarity
Phosphorylated at Ser-506 by PRKCD upon stress stimuli. Phosphorylation is required for secretion.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q04519

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q04519

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q04519

PeptideAtlas

More...
PeptideAtlasi
Q04519

PRoteomics IDEntifications database

More...
PRIDEi
Q04519

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
281814

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q04519, 6 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q04519

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q04519

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000037049, Expressed in heart and 327 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q04519, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:27435900).

Interacts with SORT1; the interaction is required for SMPD1 targeting to lysosomes (By similarity).

By similarity1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
203345, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000042187

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q04519, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1627
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q04519

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini83 – 167Saposin B-typePROSITE-ProRule annotationAdd BLAST85

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the acid sphingomyelinase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3770, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183182

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_014743_3_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q04519

Identification of Orthologs from Complete Genome Data

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OMAi
WPTEACA

Database of Orthologous Groups

More...
OrthoDBi
1142100at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q04519

TreeFam database of animal gene trees

More...
TreeFami
TF313674

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00842, MPP_ASMase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.60.21.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR041805, ASMase/PPN1_MPP
IPR004843, Calcineurin-like_PHP_ApaH
IPR029052, Metallo-depent_PP-like
IPR011001, Saposin-like
IPR008139, SaposinB_dom
IPR011160, Sphingomy_PDE

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00149, Metallophos, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000948, Sphingomy_PDE, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00741, SapB, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47862, SSF47862, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50015, SAP_B, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q04519-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPHHRASSGQ DHLRAGWEQR LERSLPAPRV GLLWMGLGLA LVLALFDSTV
60 70 80 90 100
LWVPARAYPL PSEGHSVKFS AIAPPLQSAF GWQNLTCPAC KVLFTALNHG
110 120 130 140 150
LKKEPNVARV GSVAIKICKM LNIAPLDVCQ SAVHLFEDDV VEVWTRSVLS
160 170 180 190 200
PSEACGLLLG SSCGHWDIFS TWNISLPSVP KPPPKPPSPP APGAPVSRVL
210 220 230 240 250
FLTDLHWDHE YLEGTDPYCA DPLCCRRGSG WPPNSQKGAG FWGEYSKCDL
260 270 280 290 300
PLRTLESLLK GLGPAGPFEM VYWTGDIPAH DVWQQSRQDQ LRALTTITDL
310 320 330 340 350
VRKFLGPVPV YPAVGNHEST PVNGFPPPFI KGNQSSQWLY EAMAKAWEPW
360 370 380 390 400
LPADALHTLR IGGFYALTPR PGLRLISLNM NFCSRENFWL LINSTDPAGQ
410 420 430 440 450
LQWLVEELQA AENRGDKVHI IGHIPPGHCL KSWSWNYYKI IARYENTLAG
460 470 480 490 500
QFFGHTHVDE FEIFYDEETL SRPLAVAFLA PSATTFINLN PGYRVYQIDG
510 520 530 540 550
NYPGSSHVVL DHETYILNLT QANAAGGTPS WKRLYRARET YGLPDAMPAS
560 570 580 590 600
WHNLVYRMRD DEQLFQTFWF LYHKGHPPSE PCGTPCRLAT LCAQLSARAD
610 620
SPALCRHLMP NGSLPDANRL WSRPLLC
Length:627
Mass (Da):69,927
Last modified:February 1, 1996 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0FFC7EA74EE71E91
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti48S → T in AAH11304 (PubMed:15489334).Curated1
Sequence conflicti450G → S in AAH11304 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS21653.1

Protein sequence database of the Protein Information Resource

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PIRi
A58720, S27393

NCBI Reference Sequences

More...
RefSeqi
NP_035551.1, NM_011421.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000046983; ENSMUSP00000042187; ENSMUSG00000037049

Database of genes from NCBI RefSeq genomes

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GeneIDi
20597

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:20597

UCSC genome browser

More...
UCSCi
uc009iyf.2, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FI9X-ray2.54A/B84-611[»]
5FIBX-ray2.80A/B84-611[»]
5FICX-ray2.80A/B/C/D84-611[»]
5HQNX-ray2.60A/B165-627[»]
SMRiQ04519
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi203345, 3 interactors
STRINGi10090.ENSMUSP00000042187

Chemistry databases

ChEMBLiCHEMBL4295802

PTM databases

GlyGeniQ04519, 6 sites
iPTMnetiQ04519
PhosphoSitePlusiQ04519

Proteomic databases

EPDiQ04519
MaxQBiQ04519
PaxDbiQ04519
PeptideAtlasiQ04519
PRIDEiQ04519
ProteomicsDBi281814

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
1065, 293 antibodies

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
6609
MGIiMGI:98325, Smpd1

Phylogenomic databases

eggNOGiKOG3770, Eukaryota
GeneTreeiENSGT00950000183182
HOGENOMiCLU_014743_3_1_1
InParanoidiQ04519
OMAiWPTEACA
OrthoDBi1142100at2759
PhylomeDBiQ04519
TreeFamiTF313674

Enzyme and pathway databases

ReactomeiR-MMU-1660662, Glycosphingolipid metabolism

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
20597, 5 hits in 54 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Smpd1, mouse

Protein Ontology

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PROi
PR:Q04519
RNActiQ04519, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000037049, Expressed in heart and 327 other tissues
GenevisibleiQ04519, MM

Family and domain databases

CDDicd00842, MPP_ASMase, 1 hit
Gene3Di3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR041805, ASMase/PPN1_MPP
IPR004843, Calcineurin-like_PHP_ApaH
IPR029052, Metallo-depent_PP-like
IPR011001, Saposin-like
IPR008139, SaposinB_dom
IPR011160, Sphingomy_PDE
PfamiView protein in Pfam
PF00149, Metallophos, 1 hit
PIRSFiPIRSF000948, Sphingomy_PDE, 1 hit
SMARTiView protein in SMART
SM00741, SapB, 1 hit
SUPFAMiSSF47862, SSF47862, 1 hit
PROSITEiView protein in PROSITE
PS50015, SAP_B, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiASM_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q04519
Secondary accession number(s): Q3UL52
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1996
Last modified: April 7, 2021
This is version 162 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
UniProt is an ELIXIR core data resource
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