Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01339
Entry Name
UniProt Accession
Theoretical PI
5.59
Molecular Weight
71196.96
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Sphingomyelin phosphodiesterase 3
Protein Synonyms/Alias
3.1.4.12; Neutral sphingomyelinase 2; nSMase-2; nSMase2; Neutral sphingomyelinase II;
Gene Name
Smpd3
Gene Synonyms/Alias
Created Date
30-AUG-2005
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
53
Canonical
RQRADDPCCLQLFCT
[1]
S-Palmitoylation
54
Canonical
QRADDPCCLQLFCTV
[1]
S-Palmitoylation
59
Canonical
PCCLQLFCTVLFTPV
[1]
S-Palmitoylation
395
Canonical
GVYGCHGCCNFKCLN
[1]
S-Palmitoylation
396
Canonical
VYGCHGCCNFKCLNS
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Tani M, Hannun YA. Neutral sphingomyelinase 2 is palmitoylated on multiplecysteine residues. Role of palmitoylation in subcellular localization. J BiolChem. 2007 Mar 30;282(13):10047-56. Epub 2007 Feb 1.[PMID:17272284]
Functional Description
Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Acts as a regulator of postnatal development and participates in bone and dentin mineralization. Overexpression enhances cell death, suggesting that it may be involved in apoptosis control.
Sequence Annotation
Topological domain: 1 10 Cytoplasmic.
Topological domain: 32 64 Cytoplasmic.
Topological domain: 86 655 Cytoplasmic.
Active site: 639 639 Proton acceptor.
Metal binding site: 362 362 Magnesium.
Functional site: 510 510 Important for substrate recognition.
Protein Length
655 AA.
Protein Sequence
(Canonical)
MVLYTTPFPN SCLSALHAVS WALIFPCYWL VDRLLASFIP TTYEKRQRAD DPCCLQLFCT  60
VLFTPVYLAL LVAALPFAFL GFIFWSPLQS ARRPYSYSRL EDKNPAGGAA LLSEWKGTGA  120
GKSFCFATAN VCLLPDSLAR LNNVFNTQAR AKEIGQRIRN GAARPQIKIY IDSPTNTSIS  180
AASFSSLVSP QGGDGSRAVP GSIKRTASVE YKGDGGRHPS DEAANGPASG EQADGSLEDS  240
CIVRIGGEEG GRPQEADDPA AGSQARNGAG GTPKGQTPNH NQRDGDSGSL GSPSASRESL  300
VKARAGQDSG GSGEPGANSK LLYKTSVVKK AAARRRRHPD EAFDHEVSAF FPANLDFLCL  360
QEVFDKRAAA KLKEQLHGYF EYILYDVGVY GCHGCCNFKC LNSGLFFASR YPVMDVAYHC  420
YPNGCSFDAL ASKGALFLKV QVGSTPQDQR IVGYIACTHL HAPPEDSAVR CEQLDLLQDW  480
LADFRKSTSS TSTANPEELV VFDVICGDLN FDNCSSDDKL EQQHSLFTRY KDPCRLGPGE  540
EKPWAIGTLL DTNGLYDEDV CTPDNLQKVL ESEEGRREYL AFPTSKSPGA GQKGRKDLLK  600
GNGRRIDYML HAEEGLCPDW KAEVEEFSFI TQLSGLTDHL PVAMRLMVSA GEEEA       655
FASTA
(Canonical)
>LipidDB-10090-01339|Q9JJY3
MVLYTTPFPNSCLSALHAVSWALIFPCYWLVDRLLASFIPTTYEKRQRADDPCCLQLFCT
VLFTPVYLALLVAALPFAFLGFIFWSPLQSARRPYSYSRLEDKNPAGGAALLSEWKGTGA
GKSFCFATANVCLLPDSLARLNNVFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSIS
AASFSSLVSPQGGDGSRAVPGSIKRTASVEYKGDGGRHPSDEAANGPASGEQADGSLEDS
CIVRIGGEEGGRPQEADDPAAGSQARNGAGGTPKGQTPNHNQRDGDSGSLGSPSASRESL
VKARAGQDSGGSGEPGANSKLLYKTSVVKKAAARRRRHPDEAFDHEVSAFFPANLDFLCL
QEVFDKRAAAKLKEQLHGYFEYILYDVGVYGCHGCCNFKCLNSGLFFASRYPVMDVAYHC
YPNGCSFDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPPEDSAVRCEQLDLLQDW
LADFRKSTSSTSTANPEELVVFDVICGDLNFDNCSSDDKLEQQHSLFTRYKDPCRLGPGE
EKPWAIGTLLDTNGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSPGAGQKGRKDLLK
GNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSAGEEEA
Gene Ontology
GO:0005794; C:Golgi apparatus; IDA:MGI
GO:0000137; C:Golgi cis cisterna; IDA:MGI
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004767; F:sphingomyelin phosphodiesterase activity; IDA:MGI
GO:0007049; P:cell cycle; IEA:UniProtKB-KW
GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI
GO:0030072; P:peptide hormone secretion; IMP:MGI
GO:0007165; P:signal transduction; TAS:MGI
GO:0006684; P:sphingomyelin metabolic process; IDA:MGI
Interpro
InterPro; IPR005135; Endo/exonuclease/phosphatase
Pfam
Pfam; PF03372; Exo_endo_phos;
SMART
PROSITE
PRINTS