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Protein

Sphingomyelin phosphodiesterase

Gene

Smpd1

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

Functioni

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

Catalytic activityi

Sphingomyelin + H2O = N-acylsphingosine + phosphocholine.1 Publication

Cofactori

Zn2+1 PublicationNote: Zn2+ is particularly important for enzyme activity at neutral pH.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi204Zinc 1By similarity1
Metal bindingi206Zinc 1By similarity1
Metal bindingi276Zinc 1By similarity1
Metal bindingi276Zinc 2By similarity1
Metal bindingi316Zinc 2By similarity1
Metal bindingi423Zinc 2By similarity1
Metal bindingi455Zinc 2By similarity1
Metal bindingi457Zinc 1By similarity1

GO - Molecular functioni

  • acid sphingomyelin phosphodiesterase activity Source: UniProtKB
  • hydrolase activity, acting on glycosyl bonds Source: UniProtKB-KW
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1660662. Glycosphingolipid metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingomyelin phosphodiesterase (EC:3.1.4.121 Publication)
Alternative name(s):
Acid sphingomyelinase
Short name:
aSMase
Gene namesi
Name:Smpd1
Synonyms:Asm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:98325. Smpd1.

Subcellular locationi

  • Lysosome By similarity
  • Secreted 1 Publication

GO - Cellular componenti

  • endosome Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: UniProtKB
  • lamellar body Source: Ensembl
  • lysosome Source: UniProtKB
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 44Sequence analysisAdd BLAST44
ChainiPRO_000000232445 – 627Sphingomyelin phosphodiesteraseAdd BLAST583

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi84N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi87 ↔ 163PROSITE-ProRule annotation
Disulfide bondi90 ↔ 155PROSITE-ProRule annotation
Disulfide bondi118 ↔ 129PROSITE-ProRule annotation
Glycosylationi173N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi219 ↔ 224PROSITE-ProRule annotation
Disulfide bondi225 ↔ 248PROSITE-ProRule annotation
Glycosylationi333N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi383 ↔ 429PROSITE-ProRule annotation
Glycosylationi393N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi518N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi582 ↔ 586PROSITE-ProRule annotation
Disulfide bondi592 ↔ 605PROSITE-ProRule annotation
Glycosylationi611N-linked (GlcNAc...)PROSITE-ProRule annotation1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ04519.
MaxQBiQ04519.
PaxDbiQ04519.
PeptideAtlasiQ04519.
PRIDEiQ04519.

PTM databases

PhosphoSitePlusiQ04519.

Expressioni

Gene expression databases

BgeeiENSMUSG00000037049.
CleanExiMM_SMPD1.
GenevisibleiQ04519. MM.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

MINTiMINT-1604473.
STRINGi10090.ENSMUSP00000042187.

Structurei

Secondary structure

1627
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi87 – 101Combined sources15
Helixi107 – 121Combined sources15
Helixi126 – 136Combined sources11
Helixi140 – 145Combined sources6
Turni147 – 149Combined sources3
Helixi151 – 159Combined sources9
Turni161 – 163Combined sources3
Turni166 – 168Combined sources3
Beta strandi196 – 202Combined sources7
Beta strandi220 – 223Combined sources4
Beta strandi225 – 227Combined sources3
Helixi235 – 237Combined sources3
Beta strandi245 – 247Combined sources3
Helixi252 – 260Combined sources9
Helixi261 – 265Combined sources5
Beta strandi269 – 273Combined sources5
Helixi282 – 284Combined sources3
Helixi287 – 305Combined sources19
Beta strandi310 – 312Combined sources3
Beta strandi316 – 321Combined sources6
Helixi337 – 346Combined sources10
Turni347 – 350Combined sources4
Helixi353 – 362Combined sources10
Beta strandi365 – 370Combined sources6
Beta strandi373 – 377Combined sources5
Helixi380 – 383Combined sources4
Helixi388 – 391Combined sources4
Helixi397 – 399Combined sources3
Helixi400 – 414Combined sources15
Beta strandi417 – 421Combined sources5
Helixi426 – 428Combined sources3
Helixi431 – 443Combined sources13
Turni444 – 447Combined sources4
Beta strandi448 – 453Combined sources6
Beta strandi460 – 465Combined sources6
Turni467 – 469Combined sources3
Beta strandi472 – 479Combined sources8
Turni486 – 488Combined sources3
Beta strandi492 – 499Combined sources8
Beta strandi509 – 517Combined sources9
Helixi519 – 522Combined sources4
Beta strandi531 – 536Combined sources6
Helixi537 – 541Combined sources5
Helixi548 – 560Combined sources13
Helixi562 – 572Combined sources11
Turni573 – 575Combined sources3
Helixi584 – 594Combined sources11
Beta strandi598 – 600Combined sources3
Helixi602 – 605Combined sources4
Turni606 – 608Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ04519.
SMRiQ04519.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini83 – 167Saposin B-typePROSITE-ProRule annotationAdd BLAST85

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3770. Eukaryota.
ENOG410YYPB. LUCA.
GeneTreeiENSGT00530000063095.
HOGENOMiHOG000008599.
HOVERGENiHBG004288.
InParanoidiQ04519.
KOiK12350.
OMAiPAHDVWH.
OrthoDBiEOG091G03M6.
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_dom.
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

« 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
Checksum:i0FFC7EA74EE71E91
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti48S → T in AAH11304 (PubMed:15489334).Curated1
Sequence conflicti450G → S in AAH11304 (PubMed:15489334).Curated1

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.
UniGeneiMm.4628.

Genome annotation databases

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

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.
UniGeneiMm.4628.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ04519.
SMRiQ04519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1604473.
STRINGi10090.ENSMUSP00000042187.

PTM databases

PhosphoSitePlusiQ04519.

Proteomic databases

EPDiQ04519.
MaxQBiQ04519.
PaxDbiQ04519.
PeptideAtlasiQ04519.
PRIDEiQ04519.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6609.
MGIiMGI:98325. Smpd1.

Phylogenomic databases

eggNOGiKOG3770. Eukaryota.
ENOG410YYPB. LUCA.
GeneTreeiENSGT00530000063095.
HOGENOMiHOG000008599.
HOVERGENiHBG004288.
InParanoidiQ04519.
KOiK12350.
OMAiPAHDVWH.
OrthoDBiEOG091G03M6.
PhylomeDBiQ04519.
TreeFamiTF313674.

Enzyme and pathway databases

ReactomeiR-MMU-1660662. Glycosphingolipid metabolism.

Miscellaneous databases

ChiTaRSiSmpd1. mouse.
PROiQ04519.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000037049.
CleanExiMM_SMPD1.
GenevisibleiQ04519. MM.

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_dom.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 137 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

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.