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Protein

Sphingomyelin phosphodiesterase 4

Gene

Smpd4

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

Functioni

Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide.By similarity

Catalytic activityi

Sphingomyelin + H2O = N-acylsphingosine + phosphocholine.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by phosphatidylserine and tumor necrosis factor (TNF). Inhibited by scyphostatin (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1660662. Glycosphingolipid metabolism.

Chemistry

SwissLipidsiSLP:000001481. [Q6ZPR5-1]

Names & Taxonomyi

Protein namesi
Recommended name:
Sphingomyelin phosphodiesterase 4 (EC:3.1.4.12)
Alternative name(s):
Neutral sphingomyelinase 3
Short name:
nSMase-3
Short name:
nSMase3
Neutral sphingomyelinase III
Gene namesi
Name:Smpd4
Synonyms:Kiaa1418
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1924876. Smpd4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei776 – 79621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: HGNC
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: HGNC
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • trans-Golgi network Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 823823Sphingomyelin phosphodiesterase 4PRO_0000273164Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301PhosphoserineBy similarity
Modified residuei245 – 2451PhosphoserineCombined sources
Modified residuei665 – 6651PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6ZPR5.
MaxQBiQ6ZPR5.
PaxDbiQ6ZPR5.
PRIDEiQ6ZPR5.

PTM databases

iPTMnetiQ6ZPR5.
PhosphoSiteiQ6ZPR5.

Expressioni

Gene expression databases

BgeeiQ6ZPR5.
CleanExiMM_SMPD4.
ExpressionAtlasiQ6ZPR5. baseline and differential.
GenevisibleiQ6ZPR5. MM.

Interactioni

Protein-protein interaction databases

BioGridi218808. 1 interaction.
IntActiQ6ZPR5. 2 interactions.
STRINGi10090.ENSMUSP00000006053.

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4396. Eukaryota.
ENOG410YYEJ. LUCA.
GeneTreeiENSGT00390000006044.
HOVERGENiHBG082060.
InParanoidiQ6ZPR5.
KOiK12353.
OMAiPASQEIW.
OrthoDBiEOG7SFHVZ.
PhylomeDBiQ6ZPR5.
TreeFamiTF324409.

Family and domain databases

InterProiIPR024129. Sphingomy_SMPD4.
[Graphical view]
PANTHERiPTHR12988. PTHR12988. 1 hit.
PfamiPF14724. mit_SMPDase. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6ZPR5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAFPHLQQPS FLLASLKADS INKPFAQRCQ DLVKVIEDFP AKELHAVFPW
60 70 80 90 100
LVESIFGSLD GVLVGWNLRC LQGRVNPVEY STAMEFLDPS GPMMKLVYKL
110 120 130 140 150
QAEDYNFDFP VSCLPGPVKA SIQENVLPDS PLYHNKVQFP PTGGLGLNLA
160 170 180 190 200
LNPFEYYMFY FALSLISQKP MSMTLHVRTS DCAYFTLVDR YLSWFLPTEG
210 220 230 240 250
SVPPPLCSSP GGSSPSPAPR TPAMPFASYG LHTSLLKRHI SHQTSVNADP
260 270 280 290 300
ASHEIWRSET LLQVFVEMWL HHYSLEMYQK MQSPHAKLEV LHYRLTVSSA
310 320 330 340 350
LHSPAQPSLQ ALHAYQESFT PTEEHVLVVR LLLKHLHAFA NSLKPDQASP
360 370 380 390 400
SAHSHATSPL EEFKRAAVPR FVQQKLYVFL QHCFGHWPLD ATFRAVLEMW
410 420 430 440 450
LSYLQPWRYA PEKQAQGSDP QPRCVSEKWA PFIQENLLMY TKLFVSFLNR
460 470 480 490 500
ALRTDLVSPK NALMVFRVAK VFAQPNLAEM IQKGEQLFLE PELIIPHRQH
510 520 530 540 550
RLFTVTTSFL SPWPPVVTDA SFKVKSHVYS LEGQDCKYTP MFGPEIRTLV
560 570 580 590 600
LRLAQLITQA KQTAKSISDQ YVESPTGRSF LSWLTFGLTD TNSCYPANDL
610 620 630 640 650
DEIGQDSIRK TDEYLEKALE YLRQIFRLSE AQLAQLTLAL GSARDENGKQ
660 670 680 690 700
QLPDCIVGEE GLILTPLGRY QIINGLRRFE IEYQGDLELQ PIRSYEITSL
710 720 730 740 750
VRALFRLSSA INRRFAGQMA ALCSRNDFLG SFCRYHLTEP ALSNRHLLSP
760 770 780 790 800
VGRRQVTNPA RGPRLSLRFL GSYRTLLLLL MAFFVASLFC IGPLSCSLLL
810 820
VLGYVLYAIA MTLLTERGKL HQL
Length:823
Mass (Da):93,276
Last modified:January 23, 2007 - v2
Checksum:i3C082D335608BA70
GO
Isoform 2 (identifier: Q6ZPR5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     288-316: Missing.

Show »
Length:794
Mass (Da):90,063
Checksum:i326A83F65CEF2603
GO
Isoform 3 (identifier: Q6ZPR5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     288-316: Missing.
     429-429: Missing.

Note: No experimental confirmation available.
Show »
Length:793
Mass (Da):89,877
Checksum:i78B7FB3C9954C1B1
GO
Isoform 4 (identifier: Q6ZPR5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     288-316: Missing.
     429-429: W → CLAPWSPYQHRGLR

Note: No experimental confirmation available.
Show »
Length:807
Mass (Da):91,543
Checksum:i2DF7496773312AFD
GO
Isoform 5 (identifier: Q6ZPR5-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.
     288-316: Missing.

Note: No experimental confirmation available.
Show »
Length:637
Mass (Da):72,493
Checksum:i188248B501580BB4
GO

Sequence cautioni

The sequence BAC98164.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71Q → P in AAH26767 (PubMed:15489334).Curated
Sequence conflicti15 – 151S → T in BAC27221 (PubMed:16141072).Curated
Sequence conflicti141 – 1411P → T in BAC27512 (PubMed:16141072).Curated
Sequence conflicti195 – 1951F → V in AAH26767 (PubMed:15489334).Curated
Sequence conflicti368 – 3681V → E in BAB31737 (PubMed:16141072).Curated
Sequence conflicti732 – 7321F → Y in BAC27221 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 157157Missing in isoform 5. 1 PublicationVSP_022484Add
BLAST
Alternative sequencei288 – 31629Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 2 PublicationsVSP_022485Add
BLAST
Alternative sequencei429 – 4291Missing in isoform 3. 1 PublicationVSP_022486
Alternative sequencei429 – 4291W → CLAPWSPYQHRGLR in isoform 4. 1 PublicationVSP_022487

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129354 mRNA. Translation: BAC98164.1. Different initiation.
AK019466 mRNA. Translation: BAB31737.1.
AK031029 mRNA. Translation: BAC27221.1.
AK031685 mRNA. Translation: BAC27512.1.
AK035892 mRNA. Translation: BAC29229.1.
AK164234 mRNA. Translation: BAE37694.1.
AK164456 mRNA. Translation: BAE37796.1.
BC026767 mRNA. Translation: AAH26767.1.
CCDSiCCDS28009.1. [Q6ZPR5-1]
CCDS49779.1. [Q6ZPR5-3]
CCDS49780.1. [Q6ZPR5-4]
CCDS49781.1. [Q6ZPR5-2]
RefSeqiNP_001158081.1. NM_001164609.1. [Q6ZPR5-4]
NP_001158082.1. NM_001164610.1. [Q6ZPR5-2]
NP_001158083.1. NM_001164611.1. [Q6ZPR5-3]
NP_084221.2. NM_029945.3. [Q6ZPR5-1]
XP_006522785.1. XM_006522722.2. [Q6ZPR5-1]
UniGeneiMm.34659.

Genome annotation databases

EnsembliENSMUST00000006053; ENSMUSP00000006053; ENSMUSG00000005899. [Q6ZPR5-1]
ENSMUST00000090159; ENSMUSP00000087620; ENSMUSG00000005899. [Q6ZPR5-4]
ENSMUST00000163476; ENSMUSP00000131867; ENSMUSG00000005899. [Q6ZPR5-2]
ENSMUST00000165363; ENSMUSP00000130720; ENSMUSG00000005899. [Q6ZPR5-3]
GeneIDi77626.
KEGGimmu:77626.
UCSCiuc007yll.2. mouse. [Q6ZPR5-1]
uc007ylm.2. mouse. [Q6ZPR5-3]
uc007yln.2. mouse. [Q6ZPR5-4]
uc007ylo.2. mouse. [Q6ZPR5-2]
uc007ylp.2. mouse. [Q6ZPR5-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129354 mRNA. Translation: BAC98164.1. Different initiation.
AK019466 mRNA. Translation: BAB31737.1.
AK031029 mRNA. Translation: BAC27221.1.
AK031685 mRNA. Translation: BAC27512.1.
AK035892 mRNA. Translation: BAC29229.1.
AK164234 mRNA. Translation: BAE37694.1.
AK164456 mRNA. Translation: BAE37796.1.
BC026767 mRNA. Translation: AAH26767.1.
CCDSiCCDS28009.1. [Q6ZPR5-1]
CCDS49779.1. [Q6ZPR5-3]
CCDS49780.1. [Q6ZPR5-4]
CCDS49781.1. [Q6ZPR5-2]
RefSeqiNP_001158081.1. NM_001164609.1. [Q6ZPR5-4]
NP_001158082.1. NM_001164610.1. [Q6ZPR5-2]
NP_001158083.1. NM_001164611.1. [Q6ZPR5-3]
NP_084221.2. NM_029945.3. [Q6ZPR5-1]
XP_006522785.1. XM_006522722.2. [Q6ZPR5-1]
UniGeneiMm.34659.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218808. 1 interaction.
IntActiQ6ZPR5. 2 interactions.
STRINGi10090.ENSMUSP00000006053.

Chemistry

SwissLipidsiSLP:000001481. [Q6ZPR5-1]

PTM databases

iPTMnetiQ6ZPR5.
PhosphoSiteiQ6ZPR5.

Proteomic databases

EPDiQ6ZPR5.
MaxQBiQ6ZPR5.
PaxDbiQ6ZPR5.
PRIDEiQ6ZPR5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006053; ENSMUSP00000006053; ENSMUSG00000005899. [Q6ZPR5-1]
ENSMUST00000090159; ENSMUSP00000087620; ENSMUSG00000005899. [Q6ZPR5-4]
ENSMUST00000163476; ENSMUSP00000131867; ENSMUSG00000005899. [Q6ZPR5-2]
ENSMUST00000165363; ENSMUSP00000130720; ENSMUSG00000005899. [Q6ZPR5-3]
GeneIDi77626.
KEGGimmu:77626.
UCSCiuc007yll.2. mouse. [Q6ZPR5-1]
uc007ylm.2. mouse. [Q6ZPR5-3]
uc007yln.2. mouse. [Q6ZPR5-4]
uc007ylo.2. mouse. [Q6ZPR5-2]
uc007ylp.2. mouse. [Q6ZPR5-5]

Organism-specific databases

CTDi55627.
MGIiMGI:1924876. Smpd4.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG4396. Eukaryota.
ENOG410YYEJ. LUCA.
GeneTreeiENSGT00390000006044.
HOVERGENiHBG082060.
InParanoidiQ6ZPR5.
KOiK12353.
OMAiPASQEIW.
OrthoDBiEOG7SFHVZ.
PhylomeDBiQ6ZPR5.
TreeFamiTF324409.

Enzyme and pathway databases

ReactomeiR-MMU-1660662. Glycosphingolipid metabolism.

Miscellaneous databases

ChiTaRSiSmpd4. mouse.
NextBioi347250.
PROiQ6ZPR5.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZPR5.
CleanExiMM_SMPD4.
ExpressionAtlasiQ6ZPR5. baseline and differential.
GenevisibleiQ6ZPR5. MM.

Family and domain databases

InterProiIPR024129. Sphingomy_SMPD4.
[Graphical view]
PANTHERiPTHR12988. PTHR12988. 1 hit.
PfamiPF14724. mit_SMPDase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryonic tail.
  2. "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] (ISOFORMS 2; 3; 4 AND 5).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Head, Testis and Thymus.
  3. "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] (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Spleen and Testis.

Entry informationi

Entry nameiNSMA3_MOUSE
AccessioniPrimary (citable) accession number: Q6ZPR5
Secondary accession number(s): Q3TPE0
, Q3TPP1, Q8CBJ5, Q8CD12, Q8CD83, Q8R0J3, Q9CX74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 84 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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.