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Sphingomyelin phosphodiesterase (EC 3.1.4.12) (Acid sphingomyelinase) (aSMase)

 ASM_HUMAN               Reviewed;         629 AA.
P17405; A8K8M3; E9PKS3; P17406; Q13811; Q16837; Q16841;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
03-MAR-2009, sequence version 4.
27-SEP-2017, entry version 193.
RecName: Full=Sphingomyelin phosphodiesterase;
EC=3.1.4.12 {ECO:0000269|PubMed:15877209, ECO:0000269|PubMed:1718266, ECO:0000269|PubMed:1840600, ECO:0000269|PubMed:18815062, ECO:0000269|PubMed:26084044, ECO:0000269|PubMed:8702487};
AltName: Full=Acid sphingomyelinase {ECO:0000303|PubMed:27349982};
Short=aSMase;
Flags: Precursor;
Name=SMPD1; Synonyms=ASM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ALTERNATIVE
SPLICING, AND VARIANTS ILE-322 AND ARG-506.
PubMed=1840600;
Schuchman E.H., Suchi M., Takahashi T., Sandhoff K., Desnick R.J.;
"Human acid sphingomyelinase. Isolation, nucleotide sequence and
expression of the full-length and alternatively spliced cDNAs.";
J. Biol. Chem. 266:8531-8539(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-506.
PubMed=1292508;
Newrzella D., Stoffel W.;
"Molecular cloning of the acid sphingomyelinase of the mouse and the
organization and complete nucleotide sequence of the gene.";
Biol. Chem. Hoppe-Seyler 373:1233-1238(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-36.
PubMed=1740330; DOI=10.1016/0888-7543(92)90366-Z;
Schuchman E.H., Levran O., Pereira L.V., Desnick R.J.;
"Structural organization and complete nucleotide sequence of the gene
encoding human acid sphingomyelinase (SMPD1).";
Genomics 12:197-205(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-157.
PubMed=8407868; DOI=10.1093/oxfordjournals.jbchem.a124131;
Ida H., Rennert O.M., Eto Y., Chan W.Y.;
"Cloning of a human acid sphingomyelinase cDNA with a new mutation
that renders the enzyme inactive.";
J. Biochem. 114:15-20(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT
ARG-506.
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-629, PARTIAL PROTEIN
SEQUENCE, ALTERNATIVE SPLICING, AND VARIANTS ILE-322 AND ARG-506.
TISSUE=Fibroblast;
PubMed=2555181;
Quintern L.E., Schuchman E.H., Levran O., Suchi M., Ferlinz K.,
Reinke H., Sandhoff K., Desnick R.J.;
"Isolation of cDNA clones encoding human acid sphingomyelinase:
occurrence of alternatively processed transcripts.";
EMBO J. 8:2469-2473(1989).
[8]
CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
PubMed=8702487; DOI=10.1074/jbc.271.31.18431;
Schissel S.L., Schuchman E.H., Williams K.J., Tabas I.;
"Zn2+-stimulated sphingomyelinase is secreted by many cell types and
is a product of the acid sphingomyelinase gene.";
J. Biol. Chem. 271:18431-18436(1996).
[9]
GLYCOSYLATION AT ASN-86; ASN-175; ASN-335; ASN-395 AND ASN-520.
PubMed=9030779; DOI=10.1111/j.1432-1033.1997.511_1a.x;
Ferlinz K., Hurwitz R., Moczall H., Lansmann S., Schuchman E.H.,
Sandhoff K.;
"Functional characterization of the N-glycosylation sites of human
acid sphingomyelinase by site-directed mutagenesis.";
Eur. J. Biochem. 243:511-517(1997).
[10]
DISULFIDE BONDS, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12631268; DOI=10.1046/j.1432-1033.2003.03435.x;
Lansmann S., Schuette C.G., Bartelsen O., Hoernschemeyer J., Linke T.,
Weisgerber J., Sandhoff K.;
"Human acid sphingomyelinase.";
Eur. J. Biochem. 270:1076-1088(2003).
[11]
POLYMORPHISM.
PubMed=18088425; DOI=10.1186/1471-2350-8-79;
Dastani Z., Ruel I.L., Engert J.C., Genest J. Jr., Marcil M.;
"Sphingomyelin phosphodiesterase-1 (SMPD1) coding variants do not
contribute to low levels of high-density lipoprotein cholesterol.";
BMC Med. Genet. 8:79-79(2007).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT NPDB
ASP-357.
PubMed=27659707; DOI=10.1016/j.bbrc.2016.09.096;
Acuna M., Castro-Fernandez V., Latorre M., Castro J., Schuchman E.H.,
Guixe V., Gonzalez M., Zanlungo S.;
"Structural and functional analysis of the ASM p.Ala359Asp mutant that
causes acid sphingomyelinase deficiency.";
Biochem. Biophys. Res. Commun. 479:496-501(2016).
[13]
FUNCTION, SUBCELLULAR LOCATION, VARIANT NPDB ASP-357, AND
CHARACTERIZATION OF VARIANT NPDB ASP-357.
PubMed=25920558; DOI=10.1038/ejhg.2015.89;
Acuna M., Martinez P., Moraga C., He X., Moraga M., Hunter B.,
Nuernberg P., Gutierrez R.A., Gonzalez M., Schuchman E.H.,
Santos J.L., Miquel J.F., Mabe P., Zanlungo S.;
"Epidemiological, clinical and biochemical characterization of the
p.(Ala359Asp) SMPD1 variant causing Niemann-Pick disease type B.";
Eur. J. Hum. Genet. 24:208-213(2016).
[14]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 47-629 OF MUTANT SER-629 IN
COMPLEX WITH ZINC, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-86;
ASN-175; ASN-335; ASN-395; ASN-503 AND ASN-520, DISULFIDE BONDS, AND
SUBUNIT.
PubMed=27349982; DOI=10.1016/j.jmb.2016.06.012;
Xiong Z.J., Huang J., Poda G., Pomes R., Prive G.G.;
"Structure of human acid sphingomyelinase reveals the role of the
saposin domain in activating substrate hydrolysis.";
J. Mol. Biol. 428:3026-3042(2016).
[15]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 47-629 OF APOENZYME AND IN
COMPLEX WITH PHOSPHOCHOLINE AND ZINC, COFACTOR, AND GLYCOSYLATION AT
ASN-86; ASN-175; ASN-335; ASN-395; ASN-503 AND ASN-520.
PubMed=27725636; DOI=10.1038/ncomms13082;
Zhou Y.F., Metcalf M.C., Garman S.C., Edmunds T., Qiu H., Wei R.R.;
"Human acid sphingomyelinase structures provide insight to molecular
basis of Niemann-Pick disease.";
Nat. Commun. 7:13082-13082(2016).
[16]
VARIANT NPDA SER-577, CHARACTERIZATION OF VARIANT NPDA SER-577, AND
CATALYTIC ACTIVITY.
PubMed=1718266; DOI=10.1016/0006-291X(91)91697-B;
Ferlinz K., Hurwitz R., Sandhoff K.;
"Molecular basis of acid sphingomyelinase deficiency in a patient with
Niemann-Pick disease type A.";
Biochem. Biophys. Res. Commun. 179:1187-1191(1991).
[17]
VARIANT NPDA LEU-496.
PubMed=2023926; DOI=10.1073/pnas.88.9.3748;
Levran O., Desnick R.J., Schuchman E.H.;
"Niemann-Pick disease: a frequent missense mutation in the acid
sphingomyelinase gene of Ashkenazi Jewish type A and B patients.";
Proc. Natl. Acad. Sci. U.S.A. 88:3748-3752(1991).
[18]
VARIANT NPDB ARG-608 DEL.
PubMed=1885770; DOI=10.1172/JCI115380;
Levran O., Desnick R.J., Schuchman E.H.;
"Niemann-Pick type B disease. Identification of a single codon
deletion in the acid sphingomyelinase gene and genotype/phenotype
correlations in type A and B patients.";
J. Clin. Invest. 88:806-810(1991).
[19]
VARIANT NPDA PRO-302.
PubMed=1391960;
Levran O., Desnick R.J., Schuchman E.H.;
"Identification and expression of a common missense mutation (L302P)
in the acid sphingomyelinase gene of Ashkenazi Jewish type A Niemann-
Pick disease patients.";
Blood 80:2081-2087(1992).
[20]
VARIANT NPDB ARG-436.
PubMed=1301192; DOI=10.1002/humu.1380010111;
Takahashi T., Desnick R.J., Takada G., Schuchman E.H.;
"Identification of a missense mutation (S436R) in the acid
sphingomyelinase gene from a Japanese patient with type B Niemann-Pick
disease.";
Hum. Mutat. 1:70-71(1992).
[21]
VARIANT NPDA ILE-382, AND VARIANTS NPDB ARG-242 AND SER-383.
PubMed=1618760;
Takahashi T., Suchi M., Desnick R.J., Takada G., Schuchman E.H.;
"Identification and expression of five mutations in the human acid
sphingomyelinase gene causing types A and B Niemann-Pick disease.
Molecular evidence for genetic heterogeneity in the neuronopathic and
non-neuronopathic forms.";
J. Biol. Chem. 267:12552-12558(1992).
[22]
VARIANT NPDB GLY-391.
PubMed=8051942; DOI=10.1007/BF00735404;
Sperl W., Bart G., Vanier M.T., Christomanou H., Baldissera I.,
Steichensdorf E., Paschke E.;
"A family with visceral course of Niemann-Pick disease, macular halo
syndrome and low sphingomyelin degradation rate.";
J. Inherit. Metab. Dis. 17:93-103(1994).
[23]
VARIANT NPDA THR-389.
PubMed=8680412; DOI=10.1002/humu.1380060412;
Schuchman E.H.;
"Two new mutations in the acid sphingomyelinase gene causing type A
Niemann-pick disease: N389T and R441X.";
Hum. Mutat. 6:352-354(1995).
[24]
VARIANT NPDA CYS-446.
PubMed=8693491; DOI=10.1620/tjem.177.117;
Takahashi T., Suchi M., Sato W., Ten S.B., Sakuragawa N.,
Desnick R.J., Schuchman E.H., Takada G.;
"Identification and expression of a missense mutation (Y446C) in the
acid sphingomyelinase gene from a Japanese patient with type A
Niemann-Pick disease.";
Tohoku J. Exp. Med. 177:117-123(1995).
[25]
VARIANT NPDB GLN-246.
PubMed=8664904;
DOI=10.1002/(SICI)1098-1004(1996)7:1<65::AID-HUMU10>3.3.CO;2-8;
Ida H., Rennert O.M., Maekawa K., Eto Y.;
"Identification of three novel mutations in the acid sphingomyelinase
gene of Japanese patients with Niemann-Pick disease type A and B.";
Hum. Mutat. 7:65-67(1996).
[26]
VARIANTS NPDA LYS-292 AND PRO-341.
PubMed=9266408; DOI=10.1023/A:1005387932546;
Pavluu H., Elleder M.;
"Two novel mutations in patients with atypical phenotypes of acid
sphingomyelinase deficiency.";
J. Inherit. Metab. Dis. 20:615-616(1997).
[27]
VARIANTS NPDB VAL-49; TRP-92; PRO-137; ARG-157; PRO-196; CYS-200;
MET-225; CYS-228; ASP-232; SER-245; ARG-248; HIS-289; ALA-323;
ARG-330; ASP-357; HIS-376; LEU-376; PRO-379; VAL-413; TYR-421;
ARG-431; PRO-432; CYS-435; VAL-452; ASP-456; TRP-474; LEU-475;
LEU-480; ASN-488; SER-494; CYS-496; GLN-514; VAL-515; ARG-533;
PRO-549; ASN-576; HIS-600 AND PRO-600, AND VARIANT VAL-485.
PubMed=12369017; DOI=10.1086/345074;
Simonaro C.M., Desnick R.J., McGovern M.M., Wasserstein M.P.,
Schuchman E.H.;
"The demographics and distribution of type B Niemann-Pick disease:
novel mutations lead to new genotype/phenotype correlations.";
Am. J. Hum. Genet. 71:1413-1419(2002).
[28]
VARIANTS NPDA ARG-248; TYR-319; SER-463; LEU-475 AND HIS-537, AND
VARIANTS NPDB SER-371 AND ARG-608 DEL.
PubMed=12556236; DOI=10.1046/j.1469-1809.2003.00009.x;
Sikora J., Pavluu-Pereira H., Elleder M., Roelofs H., Wevers R.A.;
"Seven novel Acid sphingomyelinase gene mutations in Niemann-Pick type
A and B patients.";
Ann. Hum. Genet. 67:63-70(2003).
[29]
VARIANTS NPDA PRO-103; SER-245; LYS-246; HIS-313; PRO-450; LEU-475;
LEU-496; HIS-496 AND CYS-517, AND VARIANT GLN-294.
PubMed=15221801; DOI=10.1002/humu.9258;
Ricci V., Stroppiano M., Corsolini F., Di Rocco M., Parenti G.,
Regis S., Grossi S., Biancheri R., Mazzotti R., Filocamo M.;
"Screening of 25 Italian patients with Niemann-Pick A reveals fourteen
new mutations, one common and thirteen private, in SMPD1.";
Hum. Mutat. 24:105-105(2004).
[30]
VARIANTS NPDB PRO-103; PRO-225; CYS-244; THR-281; LYS-292 AND ILE-382.
PubMed=15241805; DOI=10.1002/humu.9263;
Pittis M.G., Ricci V., Guerci V.I., Marcais C., Ciana G., Dardis A.,
Gerin F., Stroppiano M., Vanier M.T., Filocamo M., Bembi B.;
"Acid sphingomyelinase: identification of nine novel mutations among
Italian Niemann Pick type B patients and characterization of in vivo
functional in-frame start codon.";
Hum. Mutat. 24:186-187(2004).
[31]
VARIANTS NPDB ALA-130 AND TYR-563, AND CHARACTERIZATION OF VARIANTS
NPDB PRO-103; ALA-130; PRO-225; CYS-244; THR-281; TYR-563; HIS-600 AND
PRO-600.
PubMed=16010684; DOI=10.1002/humu.9353;
Dardis A., Zampieri S., Filocamo M., Burlina A., Bembi B.,
Pittis M.G.;
"Functional in vitro characterization of 14 SMPD1 mutations identified
in Italian patients affected by Niemann Pick type B disease.";
Hum. Mutat. 26:164-164(2005).
[32]
VARIANTS NPDA ARG-166; LEU-184; HIS-228; VAL-241; ARG-248; GLU-251;
ALA-278; HIS-289; LYS-292; PRO-341; HIS-376; TRP-474; ARG-533 AND
SER-577, VARIANT ARG-506, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF
VARIANTS NPDA LEU-184; GLU-251; ALA-278; LYS-292; PRO-341 AND HIS-376.
PubMed=15877209; DOI=10.1007/s10545-005-5671-5;
Pavluu-Pereira H., Asfaw B., Poupctova H., Ledvinova J., Sikora J.,
Vanier M.T., Sandhoff K., Zeman J., Novotna Z., Chudoba D.,
Elleder M.;
"Acid sphingomyelinase deficiency. Phenotype variability with
prevalence of intermediate phenotype in a series of twenty-five Czech
and Slovak patients. A multi-approach study.";
J. Inherit. Metab. Dis. 28:203-227(2005).
[33]
VARIANTS NPDB ARG-166 AND ASN-176, AND VARIANT GLY-505.
PubMed=16472269; DOI=10.1111/j.1445-5994.2005.01013.x;
Muessig K., Harzer K., Mayrhofer H., Kraegeloh-Mann I., Haering H.-U.,
Machicao F.;
"Clinical findings in Niemann-Pick disease type B.";
Intern. Med. J. 36:135-136(2006).
[34]
CHARACTERIZATION OF VARIANTS NPDA PRO-302 AND LEU-496,
CHARACTERIZATION OF VARIANTS NPDB TYR-421 AND ARG-608 DEL, FUNCTION,
SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
PubMed=18815062; DOI=10.1016/j.ymgme.2008.08.004;
Jones I., He X., Katouzian F., Darroch P.I., Schuchman E.H.;
"Characterization of common SMPD1 mutations causing types A and B
Niemann-Pick disease and generation of mutation-specific mouse
models.";
Mol. Genet. Metab. 95:152-162(2008).
[35]
VARIANTS NPDB ARG-330 AND ASP-451.
PubMed=19050888; DOI=10.1007/s00277-008-0648-8;
Lan M.Y., Lin S.J., Chen Y.F., Peng C.H., Liu Y.F.;
"A novel missense mutation of the SMPD1 gene in a Taiwanese patient
with type B Niemann-Pick disease.";
Ann. Hematol. 88:695-697(2009).
[36]
VARIANTS NPDA SER-245; CYS-367; PHE-390 DEL; ARG-421; SER-467; GLU-482
AND THR-592 DEL, AND VARIANTS NPDB CYS-228; HIS-376; TRP-474; ALA-486
AND ARG-608 DEL.
PubMed=19405096; DOI=10.1002/humu.21018;
Rodriguez-Pascau L., Gort L., Schuchman E.H., Vilageliu L.,
Grinberg D., Chabas A.;
"Identification and characterization of SMPD1 mutations causing
Niemann-Pick types A and B in Spanish patients.";
Hum. Mutat. 30:1117-1122(2009).
[37]
VARIANTS NPDA ARG-209 AND HIS-251, VARIANTS NPDB MET-312; ARG-425 AND
HIS-523, CHARACTERIZATION OF VARIANTS NPDA ARG-209 AND HIS-251, AND
CHARACTERIZATION OF VARIANTS NPDB MET-312; ARG-425 AND HIS-523.
PubMed=20386867; DOI=10.2119/molmed.2010.00017;
Desnick J.P., Kim J., He X., Wasserstein M.P., Simonaro C.M.,
Schuchman E.H.;
"Identification and characterization of eight novel SMPD1 mutations
causing types A and B Niemann-Pick disease.";
Mol. Med. 16:316-321(2010).
[38]
VARIANT NPDB PRO-161.
PubMed=21621718; DOI=10.1016/S0140-6736(11)60285-7;
Meersseman W., Verschueren P., Tousseyn T., De Vos R., Cassiman D.;
"PAS-positive macrophages--not always infection.";
Lancet 377:1890-1890(2011).
[39]
VARIANT NPDB SER-520.
PubMed=22613662;
Hua R., Wu H., Cui Z., Chen J.X., Wang Z.;
"A novel SMPD1 mutation in two Chinese sibling patients with type B
Niemann-Pick disease.";
Chin. Med. J. 125:1511-1512(2012).
[40]
VARIANTS NPDA ASP-245 AND LEU-570, AND CHARACTERIZATION OF VARIANTS
NPDA ASP-245 AND LEU-570.
PubMed=23430884; DOI=10.1007/8904_2011_80;
Toth B., Erdos M., Szekely A., Ritli L., Bagossi P., Suemegi J.,
Marodi L.;
"Molecular genetic characterization of novel sphingomyelin
phosphodiesterase 1 mutations causing niemann-pick disease.";
JIMD Rep. 3:125-129(2012).
[41]
VARIANTS NPDB HIS-89; PRO-103; PRO-161; CYS-228; SER-371; PRO-549 AND
ARG-608 DEL, AND VARIANTS NPDA ARG-248; SER-463; LEU-475 AND HIS-537.
PubMed=22818240; DOI=10.1016/j.ymgme.2012.06.015;
Hollak C.E., de Sonnaville E.S., Cassiman D., Linthorst G.E.,
Groener J.E., Morava E., Wevers R.A., Mannens M., Aerts J.M.,
Meersseman W., Akkerman E., Niezen-Koning K.E., Mulder M.F.,
Visser G., Wijburg F.A., Lefeber D., Poorthuis B.J.;
"Acid sphingomyelinase (Asm) deficiency patients in The Netherlands
and Belgium: disease spectrum and natural course in attenuated
patients.";
Mol. Genet. Metab. 107:526-533(2012).
[42]
VARIANTS NPDA ARG-226 AND ARG-385, AND VARIANTS NPDB CYS-228; SER-245;
HIS-376; TRP-474; SER-490; PHE-597 AND ARG-608 DEL.
PubMed=23252888; DOI=10.1111/cge.12076;
Irun P., Mallen M., Dominguez C., Rodriguez-Sureda V.,
Alvarez-Sala L.A., Arslan N., Bermejo N., Guerrero C.,
Perez de Soto I., Villalon L., Giraldo P., Pocovi M.;
"Identification of seven novel SMPD1 mutations causing Niemann-Pick
disease types A and B.";
Clin. Genet. 84:356-361(2013).
[43]
CHARACTERIZATION OF VARIANT NPDB ALA-323, AND CHARACTERIZATION OF
VARIANT VAL-485.
PubMed=23430512; DOI=10.1007/8904_2012_147;
Rhein C., Naumann J., Muehle C., Zill P., Adli M., Hegerl U.,
Hiemke C., Mergl R., Moeller H.J., Reichel M., Kornhuber J.;
"The acid sphingomyelinase sequence variant p.A487V is not associated
with decreased levels of enzymatic activity.";
JIMD Rep. 8:1-6(2013).
[44]
VARIANTS ALA-36; PHE-508 AND GLY-603, VARIANTS NPDA ARG-214; CYS-228;
SER-253; ARG-317; PRO-322; ARG-341; ARG-361; HIS-389; ARG-391;
SER-424; ILE-492; HIS-496; ARG-533 AND HIS-600, AND VARIANTS NPDB
PRO-103; PHE-280; ASP-318; CYS-367; SER-463; LEU-518 AND LYS-547.
PubMed=27338287; DOI=10.1002/ajmg.a.37817;
Ranganath P., Matta D., Bhavani G.S., Wangnekar S., Jain J.M.,
Verma I.C., Kabra M., Puri R.D., Danda S., Gupta N., Girisha K.M.,
Sankar V.H., Patil S.J., Ramadevi A.R., Bhat M., Gowrishankar K.,
Mandal K., Aggarwal S., Tamhankar P.M., Tilak P., Phadke S.R.,
Dalal A.;
"Spectrum of SMPD1 mutations in Asian-Indian patients with acid
sphingomyelinase (ASM)-deficient Niemann-Pick disease.";
Am. J. Med. Genet. A 170:2719-2730(2016).
[45]
VARIANTS NPDB ILE-256; GLN-474; ASP-575; ARG-596 AND CYS-608, VARIANT
NPDA PHE-480 DEL, AND REVIEW ON VARIANTS.
PubMed=26499107; DOI=10.1002/humu.22923;
Zampieri S., Filocamo M., Pianta A., Lualdi S., Gort L., Coll M.J.,
Sinnott R., Geberhiwot T., Bembi B., Dardis A.;
"SMPD1 mutation update: database and comprehensive analysis of
published and novel variants.";
Hum. Mutat. 37:139-147(2016).
[46]
CHARACTERIZATION OF VARIANT NPDB ALA-323, CHARACTERIZATION OF VARIANTS
ALA-36; VAL-485 AND ARG-506, AND CATALYTIC ACTIVITY.
PubMed=26084044; DOI=10.3390/ijms160613649;
Rhein C., Muehle C., Kornhuber J., Reichel M.;
"Alleged detrimental mutations in the SMPD1 gene in patients with
Niemann-Pick disease.";
Int. J. Mol. Sci. 16:13649-13652(2015).
-!- FUNCTION: Converts sphingomyelin to ceramide (PubMed:1840600,
PubMed:18815062, PubMed:27659707, PubMed:25920558). Also has
phospholipase C activities toward 1,2-diacylglycerolphosphocholine
and 1,2-diacylglycerolphosphoglycerol.
{ECO:0000269|PubMed:1840600, ECO:0000269|PubMed:18815062,
ECO:0000269|PubMed:25920558, ECO:0000269|PubMed:27659707,
ECO:0000305}.
-!- FUNCTION: Isoform 2 lacks residues that bind the cofactor Zn(2+)
and has no enzyme activity. {ECO:0000269|PubMed:1840600,
ECO:0000305}.
-!- FUNCTION: Isoform 3 lacks residues that bind the cofactor Zn(2+)
and has no enzyme activity. {ECO:0000269|PubMed:1840600,
ECO:0000305}.
-!- CATALYTIC ACTIVITY: Sphingomyelin + H(2)O = N-acylsphingosine +
phosphocholine. {ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:1718266, ECO:0000269|PubMed:1840600,
ECO:0000269|PubMed:18815062, ECO:0000269|PubMed:26084044,
ECO:0000269|PubMed:27349982, ECO:0000269|PubMed:8702487}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:8702487};
Note=Binds 2 Zn(2+) ions per subunit (PubMed:27349982,
PubMed:27725636). Zn(2+) is particularly important for enzyme
activity at neutral pH (PubMed:8702487).
{ECO:0000269|PubMed:27349982, ECO:0000269|PubMed:27725636,
ECO:0000269|PubMed:8702487};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:27349982}.
-!- INTERACTION:
P55210:CASP7; NbExp=6; IntAct=EBI-7095800, EBI-523958;
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:18815062,
ECO:0000269|PubMed:27659707}. Secreted
{ECO:0000269|PubMed:25920558, ECO:0000269|PubMed:27659707,
ECO:0000269|PubMed:8702487}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=ASM-1;
IsoId=P17405-1; Sequence=Displayed;
Note=Most abundant (90%).;
Name=2; Synonyms=ASM-2;
IsoId=P17405-2; Sequence=VSP_000331, VSP_000332;
Note=Intermediate abundance (10%).;
Name=3; Synonyms=ASM-3;
IsoId=P17405-3; Sequence=VSP_000333;
Note=Low abundance (<1%).;
Name=4;
IsoId=P17405-4; Sequence=VSP_046964;
-!- POLYMORPHISM: A common polymorphism arises from a variable number
of hexanucleotide repeat sequence within the signal peptide
region.
-!- DISEASE: Niemann-Pick disease A (NPDA) [MIM:257200]: An early-
onset lysosomal storage disorder caused by failure to hydrolyze
sphingomyelin to ceramide. It results in the accumulation of
sphingomyelin and other metabolically related lipids in
reticuloendothelial and other cell types throughout the body,
leading to cell death. Niemann-Pick disease type A is a primarily
neurodegenerative disorder characterized by onset within the first
year of life, mental retardation, digestive disorders, failure to
thrive, major hepatosplenomegaly, and severe neurologic symptoms.
The severe neurological disorders and pulmonary infections lead to
an early death, often around the age of four. Clinical features
are variable. A phenotypic continuum exists between type A (basic
neurovisceral) and type B (purely visceral) forms of Niemann-Pick
disease, and the intermediate types encompass a cluster of
variants combining clinical features of both types A and B.
{ECO:0000269|PubMed:12556236, ECO:0000269|PubMed:1391960,
ECO:0000269|PubMed:15221801, ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:1618760, ECO:0000269|PubMed:1718266,
ECO:0000269|PubMed:18815062, ECO:0000269|PubMed:19405096,
ECO:0000269|PubMed:2023926, ECO:0000269|PubMed:20386867,
ECO:0000269|PubMed:22818240, ECO:0000269|PubMed:23252888,
ECO:0000269|PubMed:23430884, ECO:0000269|PubMed:26499107,
ECO:0000269|PubMed:27338287, ECO:0000269|PubMed:8680412,
ECO:0000269|PubMed:8693491, ECO:0000269|PubMed:9266408}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Niemann-Pick disease B (NPDB) [MIM:607616]: A late-onset
lysosomal storage disorder caused by failure to hydrolyze
sphingomyelin to ceramide. It results in the accumulation of
sphingomyelin and other metabolically related lipids in
reticuloendothelial and other cell types throughout the body,
leading to cell death. Clinical signs involve only visceral
organs. The most constant sign is hepatosplenomegaly which can be
associated with pulmonary symptoms. Patients remain free of
neurologic manifestations. However, a phenotypic continuum exists
between type A (basic neurovisceral) and type B (purely visceral)
forms of Niemann-Pick disease, and the intermediate types
encompass a cluster of variants combining clinical features of
both types A and B. In Niemann-Pick disease type B, onset of the
first symptoms occurs in early childhood and patients can survive
into adulthood. {ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:12556236, ECO:0000269|PubMed:1301192,
ECO:0000269|PubMed:15241805, ECO:0000269|PubMed:16010684,
ECO:0000269|PubMed:1618760, ECO:0000269|PubMed:16472269,
ECO:0000269|PubMed:18815062, ECO:0000269|PubMed:1885770,
ECO:0000269|PubMed:19050888, ECO:0000269|PubMed:19405096,
ECO:0000269|PubMed:20386867, ECO:0000269|PubMed:21621718,
ECO:0000269|PubMed:22613662, ECO:0000269|PubMed:22818240,
ECO:0000269|PubMed:23252888, ECO:0000269|PubMed:23430512,
ECO:0000269|PubMed:25920558, ECO:0000269|PubMed:26084044,
ECO:0000269|PubMed:26499107, ECO:0000269|PubMed:27338287,
ECO:0000269|PubMed:27659707, ECO:0000269|PubMed:8051942,
ECO:0000269|PubMed:8664904}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: There are two types of sphingomyelinases: ASM
(acid), and NSM (neutral).
-!- SIMILARITY: Belongs to the acid sphingomyelinase family.
{ECO:0000305}.
-!- CAUTION: Variants Gln-294 and Val-485 have been originally
reported as disease-causing mutations in NPDA and NPDB
(PubMed:12369017, PubMed:15221801). These variants have been
reclassified as benign polymorphisms (PubMed:23430512).
{ECO:0000269|PubMed:12369017, ECO:0000269|PubMed:15221801,
ECO:0000269|PubMed:23430512}.
-!- WEB RESOURCE: Name=Mendelian genes sphingomyelin phosphodiesterase
1, acid lysosomal (SMPD1); Note=Leiden Open Variation Database
(LOVD);
URL="http://www.lovd.nl/SMPD1";
-----------------------------------------------------------------------
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EMBL; M59916; AAA58377.1; -; mRNA.
EMBL; M59917; AAA58378.1; -; Genomic_DNA.
EMBL; X63600; CAA45145.1; -; Genomic_DNA.
EMBL; M81780; AAA75008.1; -; Genomic_DNA.
EMBL; M81780; AAA75009.1; -; Genomic_DNA.
EMBL; X59960; CAA42584.1; -; mRNA.
EMBL; AK292388; BAF85077.1; -; mRNA.
EMBL; AC068733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X52678; CAA36901.1; -; mRNA.
EMBL; X52679; CAA36902.1; -; mRNA.
PIR; S06958; S06958.
PIR; S27009; A39825.
RefSeq; NP_000534.3; NM_000543.4.
RefSeq; NP_001007594.2; NM_001007593.2.
RefSeq; NP_001305016.1; NM_001318087.1.
RefSeq; NP_001305017.1; NM_001318088.1.
UniGene; Hs.498173; -.
PDB; 5I81; X-ray; 2.25 A; A=47-629.
PDB; 5I85; X-ray; 2.50 A; A=47-629.
PDB; 5I8R; X-ray; 3.65 A; A/B/C=47-629.
PDB; 5JG8; X-ray; 2.80 A; A/B=47-629.
PDBsum; 5I81; -.
PDBsum; 5I85; -.
PDBsum; 5I8R; -.
PDBsum; 5JG8; -.
ProteinModelPortal; P17405; -.
SMR; P17405; -.
BioGrid; 112493; 14.
IntAct; P17405; 7.
MINT; MINT-3008689; -.
STRING; 9606.ENSP00000340409; -.
BindingDB; P17405; -.
ChEMBL; CHEMBL2760; -.
DrugBank; DB00381; Amlodipine.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB01151; Desipramine.
iPTMnet; P17405; -.
PhosphoSitePlus; P17405; -.
BioMuta; SMPD1; -.
DMDM; 224471897; -.
MaxQB; P17405; -.
PaxDb; P17405; -.
PeptideAtlas; P17405; -.
PRIDE; P17405; -.
DNASU; 6609; -.
Ensembl; ENST00000342245; ENSP00000340409; ENSG00000166311.
Ensembl; ENST00000527275; ENSP00000435350; ENSG00000166311.
GeneID; 6609; -.
KEGG; hsa:6609; -.
UCSC; uc001mcw.4; human. [P17405-1]
CTD; 6609; -.
DisGeNET; 6609; -.
EuPathDB; HostDB:ENSG00000166311.9; -.
GeneCards; SMPD1; -.
GeneReviews; SMPD1; -.
HGNC; HGNC:11120; SMPD1.
MalaCards; SMPD1; -.
MIM; 257200; phenotype.
MIM; 607608; gene.
MIM; 607616; phenotype.
neXtProt; NX_P17405; -.
Orphanet; 77292; Niemann-Pick disease type A.
Orphanet; 77293; Niemann-Pick disease type B.
PharmGKB; PA35969; -.
eggNOG; KOG3770; Eukaryota.
eggNOG; ENOG410YYPB; LUCA.
HOVERGEN; HBG004288; -.
InParanoid; P17405; -.
KO; K12350; -.
OrthoDB; EOG091G03M6; -.
PhylomeDB; P17405; -.
TreeFam; TF313674; -.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
SIGNOR; P17405; -.
ChiTaRS; SMPD1; human.
GeneWiki; Sphingomyelin_phosphodiesterase_1; -.
GenomeRNAi; 6609; -.
PRO; PR:P17405; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000166311; -.
CleanEx; HS_SMPD1; -.
ExpressionAtlas; P17405; baseline and differential.
Genevisible; P17405; HS.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0042599; C:lamellar body; IEA:Ensembl.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0061750; F:acid sphingomyelin phosphodiesterase activity; IDA:UniProtKB.
GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0046513; P:ceramide biosynthetic process; IDA:UniProtKB.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:BHF-UCL.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:BHF-UCL.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006685; P:sphingomyelin catabolic process; IDA:UniProtKB.
GO; GO:0006684; P:sphingomyelin metabolic process; TAS:ProtInc.
GO; GO:0023021; P:termination of signal transduction; IMP:BHF-UCL.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR011001; Saposin-like.
InterPro; IPR008139; SaposinB_dom.
InterPro; IPR011160; Sphingomy_PDE.
Pfam; PF00149; Metallophos; 1.
PIRSF; PIRSF000948; Sphingomy_PDE; 1.
SMART; SM00741; SapB; 1.
SUPFAM; SSF47862; SSF47862; 1.
SUPFAM; SSF56300; SSF56300; 1.
PROSITE; PS50015; SAP_B; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Glycosidase; Hydrolase; Lysosome; Metal-binding;
Neurodegeneration; Niemann-Pick disease; Reference proteome; Secreted;
Signal; Zinc.
SIGNAL 1 46
CHAIN 47 629 Sphingomyelin phosphodiesterase.
/FTId=PRO_0000002323.
DOMAIN 85 169 Saposin B-type. {ECO:0000255|PROSITE-
ProRule:PRU00415}.
METAL 206 206 Zinc 1. {ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000269|PubMed:27349982}.
METAL 208 208 Zinc 1; via tele nitrogen.
{ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000269|PubMed:27349982}.
METAL 278 278 Zinc 1. {ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000269|PubMed:27349982}.
METAL 278 278 Zinc 2. {ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000269|PubMed:27349982}.
METAL 318 318 Zinc 2. {ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000269|PubMed:27349982}.
METAL 425 425 Zinc 2; via tele nitrogen.
{ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000269|PubMed:27349982}.
METAL 457 457 Zinc 2; via pros nitrogen.
{ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000269|PubMed:27349982}.
METAL 459 459 Zinc 1; via tele nitrogen.
{ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000269|PubMed:27349982}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:27349982,
ECO:0000269|PubMed:9030779}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:27349982,
ECO:0000269|PubMed:9030779}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:27349982,
ECO:0000269|PubMed:9030779}.
CARBOHYD 395 395 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:27349982,
ECO:0000269|PubMed:9030779}.
CARBOHYD 503 503 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000269|PubMed:27349982}.
CARBOHYD 520 520 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5I81,
ECO:0000244|PDB:5I85,
ECO:0000244|PDB:5I8R,
ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:27349982,
ECO:0000269|PubMed:9030779}.
DISULFID 89 165 {ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:27349982}.
DISULFID 92 157 {ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:27349982}.
DISULFID 120 131 {ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:12631268,
ECO:0000269|PubMed:27349982}.
DISULFID 221 226 {ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:12631268,
ECO:0000269|PubMed:27349982}.
DISULFID 227 250 {ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:12631268,
ECO:0000269|PubMed:27349982}.
DISULFID 385 431 {ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:12631268,
ECO:0000269|PubMed:27349982}.
DISULFID 584 588 {ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:12631268,
ECO:0000269|PubMed:27349982}.
DISULFID 594 607 {ECO:0000244|PDB:5JG8,
ECO:0000255|PROSITE-ProRule:PRU00415,
ECO:0000269|PubMed:12631268,
ECO:0000269|PubMed:27349982}.
VAR_SEQ 104 104 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046964.
VAR_SEQ 363 418 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_000333.
VAR_SEQ 363 374 IGGFYALSPYPG -> YLSSVETQEGKR (in isoform
2). {ECO:0000305}.
/FTId=VSP_000331.
VAR_SEQ 375 418 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_000332.
VARIANT 36 36 V -> A (polymorphism; does not affect
enzymatic activity; dbSNP:rs1050228).
{ECO:0000269|PubMed:1740330,
ECO:0000269|PubMed:26084044,
ECO:0000269|PubMed:27338287}.
/FTId=VAR_038191.
VARIANT 49 49 D -> V (in NPDB; unknown pathological
significance).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060870.
VARIANT 89 89 C -> H (in NPDB; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:22818240}.
/FTId=VAR_075322.
VARIANT 92 92 C -> W (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060871.
VARIANT 103 103 L -> P (in NPDA and NPDB; expresses
protein level comparable to wild-type
SMPD1 expressing cells; retains very low
enzyme activity).
{ECO:0000269|PubMed:15221801,
ECO:0000269|PubMed:15241805,
ECO:0000269|PubMed:16010684,
ECO:0000269|PubMed:22818240,
ECO:0000269|PubMed:27338287}.
/FTId=VAR_060872.
VARIANT 130 130 V -> A (in NPDB; expresses protein level
comparable to wild-type SMPD1 expressing
cells; retains 13% residual enzyme
activity). {ECO:0000269|PubMed:16010684}.
/FTId=VAR_060873.
VARIANT 137 137 L -> P (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060874.
VARIANT 157 157 C -> R (in NPDB).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:8407868}.
/FTId=VAR_011387.
VARIANT 161 161 L -> P (in NPDB).
{ECO:0000269|PubMed:22818240}.
/FTId=VAR_075323.
VARIANT 166 166 G -> R (in NPDB; also in patients with an
intermediate form).
{ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:16472269}.
/FTId=VAR_060875.
VARIANT 176 176 I -> N (in NPDB).
{ECO:0000269|PubMed:16472269}.
/FTId=VAR_060876.
VARIANT 184 184 P -> L (in NPDA; reduces enzyme activity;
intermediate form with clinical features
of both Niemann-Pick disease types A and
B). {ECO:0000269|PubMed:15877209}.
/FTId=VAR_060877.
VARIANT 196 196 A -> P (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060878.
VARIANT 200 200 R -> C (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060879.
VARIANT 209 209 W -> R (in NPDA; results in less than
0.5% of wild-type activity).
{ECO:0000269|PubMed:20386867}.
/FTId=VAR_068435.
VARIANT 214 214 L -> R (in NPDA).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077311.
VARIANT 225 225 L -> M (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060880.
VARIANT 225 225 L -> P (in NPDB; expresses protein level
comparable to wild-type SMPD1 expressing
cells; retains no enzyme activity).
{ECO:0000269|PubMed:15241805,
ECO:0000269|PubMed:16010684}.
/FTId=VAR_060881.
VARIANT 226 226 C -> R (in NPDA).
{ECO:0000269|PubMed:23252888}.
/FTId=VAR_075324.
VARIANT 228 228 R -> C (in NPDB and NPDA; some patients
have a NPDA/NPDB intermediate phenotype).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:19405096,
ECO:0000269|PubMed:22818240,
ECO:0000269|PubMed:23252888,
ECO:0000269|PubMed:27338287}.
/FTId=VAR_060882.
VARIANT 228 228 R -> H (in NPDA; intermediate form with
clinical features of both Niemann-Pick
disease types A and B).
{ECO:0000269|PubMed:15877209}.
/FTId=VAR_060883.
VARIANT 232 232 G -> D (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060884.
VARIANT 241 241 A -> V (in NPDA; intermediate form with
clinical features of both Niemann-Pick
disease types A and B).
{ECO:0000269|PubMed:15877209}.
/FTId=VAR_060885.
VARIANT 242 242 G -> R (in NPDB).
{ECO:0000269|PubMed:1618760}.
/FTId=VAR_005058.
VARIANT 244 244 W -> C (in NPDB; expresses protein level
comparable to wild-type SMPD1 expressing
cells; retains no enzyme activity).
{ECO:0000269|PubMed:15241805,
ECO:0000269|PubMed:16010684}.
/FTId=VAR_060886.
VARIANT 245 245 G -> D (in NPDA; severe decrease in
activity; the mutant is highly unstable).
{ECO:0000269|PubMed:23430884}.
/FTId=VAR_075325.
VARIANT 245 245 G -> S (in NPDA and NPDB).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:15221801,
ECO:0000269|PubMed:19405096,
ECO:0000269|PubMed:23252888}.
/FTId=VAR_060887.
VARIANT 246 246 E -> K (in NPDA).
{ECO:0000269|PubMed:15221801}.
/FTId=VAR_060888.
VARIANT 246 246 E -> Q (in NPDB; 30% residual activity).
{ECO:0000269|PubMed:8664904}.
/FTId=VAR_005059.
VARIANT 248 248 S -> R (in NPDA and NPDB; also found in
patients with an intermediate form).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:12556236,
ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:22818240}.
/FTId=VAR_015287.
VARIANT 251 251 D -> E (in NPDA; strongly reduces enzyme
activity; intermediate form with clinical
features of both Niemann-Pick disease
types A and B).
{ECO:0000269|PubMed:15877209}.
/FTId=VAR_060889.
VARIANT 251 251 D -> H (in NPDA; results in loss of
activity). {ECO:0000269|PubMed:20386867}.
/FTId=VAR_068436.
VARIANT 253 253 P -> S (in NPDA).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077312.
VARIANT 256 256 T -> I (in NPDB).
{ECO:0000269|PubMed:26499107}.
/FTId=VAR_075326.
VARIANT 278 278 D -> A (in NPDA; strongly reduces enzyme
activity; intermediate form with clinical
features of both Niemann-Pick disease
types A and B).
{ECO:0000269|PubMed:15877209}.
/FTId=VAR_060890.
VARIANT 280 280 P -> F (in NPDB; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077313.
VARIANT 281 281 A -> T (in NPDB; expresses protein level
comparable to wild-type SMPD1 expressing
cells; retains no enzyme activity).
{ECO:0000269|PubMed:15241805,
ECO:0000269|PubMed:16010684}.
/FTId=VAR_060891.
VARIANT 289 289 R -> H (in NPDB; also in patients with an
intermediate form; unknown pathological
significance).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:15877209}.
/FTId=VAR_060892.
VARIANT 292 292 Q -> K (in NPDA; strongly reduces enzyme
activity; intermediate form with clinical
features of both Niemann-Pick disease
types A and B).
{ECO:0000269|PubMed:15241805,
ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:9266408}.
/FTId=VAR_060893.
VARIANT 294 294 R -> Q (in dbSNP:rs35824453).
{ECO:0000269|PubMed:15221801}.
/FTId=VAR_060894.
VARIANT 302 302 L -> P (in NPDA; in 23% of NPDA Ashkenazi
Jewish patients; abolishes enzyme
activity). {ECO:0000269|PubMed:1391960,
ECO:0000269|PubMed:18815062}.
/FTId=VAR_005060.
VARIANT 312 312 V -> M (in NPDB; results in 20% of wild-
type activity).
{ECO:0000269|PubMed:20386867}.
/FTId=VAR_068437.
VARIANT 313 313 Y -> H (in NPDA).
{ECO:0000269|PubMed:15221801}.
/FTId=VAR_060895.
VARIANT 316 316 V -> E (in dbSNP:rs12575136).
/FTId=VAR_054642.
VARIANT 317 317 G -> R (in NPDA).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077314.
VARIANT 318 318 N -> D (in NPDB; unknown pathological
significance).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077315.
VARIANT 319 319 H -> Y (in NPDA).
{ECO:0000269|PubMed:12556236,
ECO:0000269|PubMed:22818240}.
/FTId=VAR_015288.
VARIANT 322 322 T -> I (in dbSNP:rs1050233).
{ECO:0000269|PubMed:1840600,
ECO:0000269|PubMed:2555181,
ECO:0000269|PubMed:26084044}.
/FTId=VAR_054643.
VARIANT 322 322 T -> P (in NPDA; unknown pathological
significance).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077316.
VARIANT 323 323 P -> A (in NPDB; results in 1-4% of wild
type activity).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:23430512,
ECO:0000269|PubMed:26084044}.
/FTId=VAR_060896.
VARIANT 330 330 P -> R (in NPDB).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:19050888}.
/FTId=VAR_060897.
VARIANT 341 341 L -> P (in NPDA; strongly reduces enzyme
activity; intermediate form with clinical
features of both Niemann-Pick disease
types A and B).
{ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:9266408}.
/FTId=VAR_060898.
VARIANT 341 341 L -> R (in NPDA).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077317.
VARIANT 357 357 A -> D (in NPDB; sphingomyelinase
activity is decreased to 4% of wild-type
activity; no effect on protein abundance;
no effect on protein localization to
lysosome; no effect on protein
localization to extracellular space).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:25920558,
ECO:0000269|PubMed:27659707}.
/FTId=VAR_060899.
VARIANT 361 361 L -> R (in NPDA; unknown pathological
significance).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077318.
VARIANT 367 367 Y -> C (in NPDA).
{ECO:0000269|PubMed:19405096,
ECO:0000269|PubMed:27338287}.
/FTId=VAR_060900.
VARIANT 371 371 P -> S (in NPDB).
{ECO:0000269|PubMed:12556236,
ECO:0000269|PubMed:22818240}.
/FTId=VAR_015289.
VARIANT 376 376 R -> H (in NPDB; reduces enzyme activity;
some patients have a NPDA/NPDB
intermediate phenotype).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:19405096,
ECO:0000269|PubMed:23252888}.
/FTId=VAR_060901.
VARIANT 376 376 R -> L (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060902.
VARIANT 379 379 S -> P (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060903.
VARIANT 382 382 M -> I (in NPDA and NPDB).
{ECO:0000269|PubMed:15241805,
ECO:0000269|PubMed:1618760}.
/FTId=VAR_005061.
VARIANT 383 383 N -> S (in NPDB).
{ECO:0000269|PubMed:1618760}.
/FTId=VAR_005062.
VARIANT 385 385 C -> R (in NPDA).
{ECO:0000269|PubMed:23252888}.
/FTId=VAR_075327.
VARIANT 389 389 N -> H (in NPDA).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077319.
VARIANT 389 389 N -> T (in NPDA).
{ECO:0000269|PubMed:8680412}.
/FTId=VAR_005063.
VARIANT 390 390 Missing (in NPDA).
{ECO:0000269|PubMed:19405096}.
/FTId=VAR_060904.
VARIANT 391 391 W -> G (in NPDB; low sphingomyelin
degradation rates).
{ECO:0000269|PubMed:8051942}.
/FTId=VAR_005064.
VARIANT 391 391 W -> R (in NPDA; intermediate form).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077320.
VARIANT 413 413 A -> V (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060905.
VARIANT 421 421 H -> R (in NPDA).
{ECO:0000269|PubMed:19405096}.
/FTId=VAR_060906.
VARIANT 421 421 H -> Y (in NPDB; abolishes enzyme
activity). {ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:18815062}.
/FTId=VAR_015290.
VARIANT 424 424 G -> S (in NPDA).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077321.
VARIANT 425 425 H -> R (in NPDB; results in loss of
activity; the patient also carries
mutation H-228 that has sufficient
activity to account for the Niemann-Pick
disease type B phenotype).
{ECO:0000269|PubMed:20386867}.
/FTId=VAR_068438.
VARIANT 431 431 C -> R (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060907.
VARIANT 432 432 L -> P (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060908.
VARIANT 435 435 W -> C (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060909.
VARIANT 436 436 S -> R (in NPDB).
{ECO:0000269|PubMed:1301192}.
/FTId=VAR_005065.
VARIANT 446 446 Y -> C (in NPDA).
{ECO:0000269|PubMed:8693491}.
/FTId=VAR_011388.
VARIANT 450 450 L -> P (in NPDA).
{ECO:0000269|PubMed:15221801}.
/FTId=VAR_060910.
VARIANT 451 451 A -> D (in NPDB).
{ECO:0000269|PubMed:19050888}.
/FTId=VAR_068439.
VARIANT 452 452 A -> V (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060911.
VARIANT 456 456 G -> D (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060912.
VARIANT 463 463 F -> S (in NPDA).
{ECO:0000269|PubMed:12556236,
ECO:0000269|PubMed:27338287}.
/FTId=VAR_015291.
VARIANT 467 467 Y -> S (in NPDA).
{ECO:0000269|PubMed:19405096}.
/FTId=VAR_060913.
VARIANT 474 474 R -> Q (in NPDB; unknown pathological
significance).
{ECO:0000269|PubMed:26499107}.
/FTId=VAR_075328.
VARIANT 474 474 R -> W (in NPDB; some patients have a
NPDA/NPDB intermediate phenotype).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:19405096,
ECO:0000269|PubMed:23252888}.
/FTId=VAR_060914.
VARIANT 475 475 P -> L (in NPDA and NPDB).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:12556236,
ECO:0000269|PubMed:15221801,
ECO:0000269|PubMed:22818240}.
/FTId=VAR_015292.
VARIANT 480 480 F -> L (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060915.
VARIANT 480 480 Missing (in NPDA; unknown pathological
significance).
{ECO:0000269|PubMed:26499107}.
/FTId=VAR_075329.
VARIANT 482 482 A -> E (in NPDA).
{ECO:0000269|PubMed:19405096}.
/FTId=VAR_060916.
VARIANT 485 485 A -> V (polymorphism; does not affect
enzymatic activity; dbSNP:rs141641266).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:23430512,
ECO:0000269|PubMed:26084044}.
/FTId=VAR_060917.
VARIANT 486 486 T -> A (in NPDB).
{ECO:0000269|PubMed:19405096}.
/FTId=VAR_060918.
VARIANT 488 488 Y -> N (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060919.
VARIANT 490 490 G -> S (in NPDB).
{ECO:0000269|PubMed:23252888}.
/FTId=VAR_075330.
VARIANT 492 492 N -> I (in NPDA; intermediate form).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077322.
VARIANT 494 494 G -> S (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060920.
VARIANT 496 496 R -> C (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060921.
VARIANT 496 496 R -> H (in NPDA).
{ECO:0000269|PubMed:15221801,
ECO:0000269|PubMed:27338287}.
/FTId=VAR_060922.
VARIANT 496 496 R -> L (in NPDA; in 32% of NPDA Ashkenazi
Jewish patients; nearly abolishes enzyme
activity). {ECO:0000269|PubMed:15221801,
ECO:0000269|PubMed:18815062,
ECO:0000269|PubMed:2023926}.
/FTId=VAR_005066.
VARIANT 505 505 S -> G. {ECO:0000269|PubMed:16472269}.
/FTId=VAR_060923.
VARIANT 506 506 G -> R (polymorphism; does not affect
enzymatic activity; dbSNP:rs1050239).
{ECO:0000269|PubMed:1292508,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:1840600,
ECO:0000269|PubMed:2555181}.
/FTId=VAR_054644.
VARIANT 508 508 S -> F. {ECO:0000269|PubMed:27338287}.
/FTId=VAR_077323.
VARIANT 514 514 H -> Q (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060924.
VARIANT 515 515 E -> V (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060925.
VARIANT 517 517 Y -> C (in NPDA).
{ECO:0000269|PubMed:15221801}.
/FTId=VAR_060926.
VARIANT 518 518 I -> L (in NPDB).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077324.
VARIANT 520 520 N -> S (in NPDB).
{ECO:0000269|PubMed:22613662}.
/FTId=VAR_068440.
VARIANT 523 523 Q -> H (in NPDB; results in 64% of wild-
type activity).
{ECO:0000269|PubMed:20386867}.
/FTId=VAR_068441.
VARIANT 533 533 W -> R (in NPDB and NPDA; also in
patients with an intermediate form).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:27338287}.
/FTId=VAR_060927.
VARIANT 537 537 Y -> H (in NPDA).
{ECO:0000269|PubMed:12556236,
ECO:0000269|PubMed:22818240}.
/FTId=VAR_015293.
VARIANT 547 547 N -> K (in NPDB).
{ECO:0000269|PubMed:27338287}.
/FTId=VAR_077325.
VARIANT 549 549 L -> P (in NPDB).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:22818240}.
/FTId=VAR_060928.
VARIANT 563 563 D -> Y (in NPDB; expresses protein level
comparable to wild-type SMPD1 expressing
cells; retains 6.8% residual enzyme
activity). {ECO:0000269|PubMed:16010684}.
/FTId=VAR_060929.
VARIANT 570 570 F -> L (in NPDA; results in decreased
activity; decreased stability).
{ECO:0000269|PubMed:23430884}.
/FTId=VAR_075331.
VARIANT 575 575 H -> D (in NPDB; unknown pathological
significance).
{ECO:0000269|PubMed:26499107}.
/FTId=VAR_075332.
VARIANT 576 576 K -> N (in NPDB).
{ECO:0000269|PubMed:12369017}.
/FTId=VAR_060930.
VARIANT 577 577 G -> S (in NPDA; impairs enzyme activity;
also in patients with an intermediate
form). {ECO:0000269|PubMed:15877209,
ECO:0000269|PubMed:1718266}.
/FTId=VAR_005067.
VARIANT 592 592 Missing (in NPDA).
{ECO:0000269|PubMed:19405096}.
/FTId=VAR_060931.
VARIANT 596 596 Q -> R (in NPDB).
{ECO:0000269|PubMed:26499107}.
/FTId=VAR_075333.
VARIANT 597 597 L -> F (in NPDB; unknown pathological
significance).
{ECO:0000269|PubMed:23252888}.
/FTId=VAR_075334.
VARIANT 600 600 R -> H (in NPDB and NPDA; expresses
protein level comparable to wild-type
SMPD1 expressing cells; retains about 10%
residual enzyme activity).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:16010684,
ECO:0000269|PubMed:27338287}.
/FTId=VAR_060932.
VARIANT 600 600 R -> P (in NPDB; expresses protein level
comparable to wild-type SMPD1 expressing
cells; retains very low enzyme activity).
{ECO:0000269|PubMed:12369017,
ECO:0000269|PubMed:16010684}.
/FTId=VAR_060933.
VARIANT 603 603 S -> G. {ECO:0000269|PubMed:27338287}.
/FTId=VAR_077326.
VARIANT 608 608 R -> C (in NPDB; unknown pathological
significance).
{ECO:0000269|PubMed:26499107}.
/FTId=VAR_075335.
VARIANT 608 608 Missing (in NPDB; nearly abolishes enzyme
activity; some patients have a NPDA/NPDB
intermediate phenotype).
{ECO:0000269|PubMed:12556236,
ECO:0000269|PubMed:18815062,
ECO:0000269|PubMed:1885770,
ECO:0000269|PubMed:19405096,
ECO:0000269|PubMed:22818240,
ECO:0000269|PubMed:23252888}.
/FTId=VAR_005068.
CONFLICT 35 36 Missing (in Ref. 4; CAA42584).
{ECO:0000305}.
CONFLICT 268 268 G -> D (in Ref. 5; BAF85077).
{ECO:0000305}.
HELIX 85 87 {ECO:0000244|PDB:5I81}.
HELIX 88 103 {ECO:0000244|PDB:5I81}.
HELIX 106 122 {ECO:0000244|PDB:5I81}.
HELIX 128 148 {ECO:0000244|PDB:5I81}.
TURN 149 151 {ECO:0000244|PDB:5I81}.
HELIX 153 161 {ECO:0000244|PDB:5I81}.
TURN 163 165 {ECO:0000244|PDB:5I81}.
STRAND 198 204 {ECO:0000244|PDB:5I81}.
STRAND 222 225 {ECO:0000244|PDB:5I81}.
STRAND 247 249 {ECO:0000244|PDB:5I81}.
HELIX 254 262 {ECO:0000244|PDB:5I81}.
HELIX 265 267 {ECO:0000244|PDB:5I81}.
STRAND 271 275 {ECO:0000244|PDB:5I81}.
HELIX 289 307 {ECO:0000244|PDB:5I81}.
STRAND 312 314 {ECO:0000244|PDB:5I81}.
STRAND 320 323 {ECO:0000244|PDB:5I81}.
STRAND 334 338 {ECO:0000244|PDB:5JG8}.
HELIX 339 348 {ECO:0000244|PDB:5I81}.
TURN 350 352 {ECO:0000244|PDB:5I81}.
HELIX 355 364 {ECO:0000244|PDB:5I81}.
STRAND 367 372 {ECO:0000244|PDB:5I81}.
STRAND 375 379 {ECO:0000244|PDB:5I81}.
HELIX 382 385 {ECO:0000244|PDB:5I81}.
HELIX 390 393 {ECO:0000244|PDB:5I81}.
HELIX 399 401 {ECO:0000244|PDB:5I81}.
HELIX 402 416 {ECO:0000244|PDB:5I81}.
STRAND 419 423 {ECO:0000244|PDB:5I81}.
HELIX 428 430 {ECO:0000244|PDB:5I81}.
HELIX 433 445 {ECO:0000244|PDB:5I81}.
TURN 446 449 {ECO:0000244|PDB:5I81}.
STRAND 450 455 {ECO:0000244|PDB:5I81}.
STRAND 462 467 {ECO:0000244|PDB:5I81}.
TURN 469 471 {ECO:0000244|PDB:5I81}.
STRAND 474 481 {ECO:0000244|PDB:5I81}.
TURN 488 490 {ECO:0000244|PDB:5I81}.
STRAND 494 501 {ECO:0000244|PDB:5I81}.
STRAND 511 518 {ECO:0000244|PDB:5I81}.
HELIX 521 524 {ECO:0000244|PDB:5I81}.
STRAND 534 538 {ECO:0000244|PDB:5I81}.
HELIX 539 543 {ECO:0000244|PDB:5I81}.
HELIX 550 561 {ECO:0000244|PDB:5I81}.
HELIX 564 574 {ECO:0000244|PDB:5I81}.
TURN 575 577 {ECO:0000244|PDB:5I81}.
HELIX 586 597 {ECO:0000244|PDB:5I81}.
STRAND 600 602 {ECO:0000244|PDB:5JG8}.
HELIX 604 607 {ECO:0000244|PDB:5I81}.
TURN 608 610 {ECO:0000244|PDB:5I81}.
SEQUENCE 629 AA; 69752 MW; C9888CB8359C42AC CRC64;
MPRYGASLRQ SCPRSGREQG QDGTAGAPGL LWMGLVLALA LALALALSDS RVLWAPAEAH
PLSPQGHPAR LHRIVPRLRD VFGWGNLTCP ICKGLFTAIN LGLKKEPNVA RVGSVAIKLC
NLLKIAPPAV CQSIVHLFED DMVEVWRRSV LSPSEACGLL LGSTCGHWDI FSSWNISLPT
VPKPPPKPPS PPAPGAPVSR ILFLTDLHWD HDYLEGTDPD CADPLCCRRG SGLPPASRPG
AGYWGEYSKC DLPLRTLESL LSGLGPAGPF DMVYWTGDIP AHDVWHQTRQ DQLRALTTVT
ALVRKFLGPV PVYPAVGNHE STPVNSFPPP FIEGNHSSRW LYEAMAKAWE PWLPAEALRT
LRIGGFYALS PYPGLRLISL NMNFCSRENF WLLINSTDPA GQLQWLVGEL QAAEDRGDKV
HIIGHIPPGH CLKSWSWNYY RIVARYENTL AAQFFGHTHV DEFEVFYDEE TLSRPLAVAF
LAPSATTYIG LNPGYRVYQI DGNYSGSSHV VLDHETYILN LTQANIPGAI PHWQLLYRAR
ETYGLPNTLP TAWHNLVYRM RGDMQLFQTF WFLYHKGHPP SEPCGTPCRL ATLCAQLSAR
ADSPALCRHL MPDGSLPEAQ SLWPRPLFC


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U1360b CLIA Acid sphingomyelinase,aSMase,Bos taurus,Bovine,SMPD1,Sphingomyelin phosphodiesterase 96T
E1360m ELISA Acid sphingomyelinase,Asm,aSMase,Mouse,Mus musculus,Smpd1,Sphingomyelin phosphodiesterase 96T
E1360m ELISA kit Acid sphingomyelinase,Asm,aSMase,Mouse,Mus musculus,Smpd1,Sphingomyelin phosphodiesterase 96T
E1360h ELISA kit Acid sphingomyelinase,ASM,aSMase,Homo sapiens,Human,SMPD1,Sphingomyelin phosphodiesterase 96T
U1360h CLIA Acid sphingomyelinase,ASM,aSMase,Homo sapiens,Human,SMPD1,Sphingomyelin phosphodiesterase 96T
E1360h ELISA Acid sphingomyelinase,ASM,aSMase,Homo sapiens,Human,SMPD1,Sphingomyelin phosphodiesterase 96T
EIAAB27971 Homo sapiens,Human,Neutral sphingomyelinase 2,Neutral sphingomyelinase II,nSMase2,nSMase-2,SMPD3,Sphingomyelin phosphodiesterase 3
EIAAB27975 Kiaa1418,Mouse,Mus musculus,Neutral sphingomyelinase 3,Neutral sphingomyelinase III,nSMase3,nSMase-3,Smpd4,Sphingomyelin phosphodiesterase 4
EIAAB27974 Homo sapiens,Human,KIAA1418,Neutral sphingomyelinase 3,Neutral sphingomyelinase III,nSMase3,nSMase-3,SMPD4,Sphingomyelin phosphodiesterase 4
EIAAB27973 Mouse,Mus musculus,Neutral sphingomyelinase 2,Neutral sphingomyelinase II,nSMase2,nSMase-2,Smpd3,Sphingomyelin phosphodiesterase 3
EIAAB27972 Cca1,Confluent 3Y1 cell-associated protein 1,Neutral sphingomyelinase 2,Neutral sphingomyelinase II,nSMase2,nSMase-2,Rat,Rattus norvegicus,Smpd3,Sphingomyelin phosphodiesterase 3
GWB-908C4E Anti- SMPD2 (sphingomyelin phosphodiesterase 2. neutral membrane (neutral sphingomyelinase)) Antibody
18-003-42450 Acid sphingomyelinase-like phosphodiesterase 3b - EC 3.1.4.-; ASM-like phosphodiesterase 3b Polyclonal 0.05 mg Aff Pur
CSB-EL021846RA Rat sphingomyelin phosphodiesterase 2, neutral membrane (neutral sphingomyelinase) (SMPD2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL021847RA Rat sphingomyelin phosphodiesterase 3, neutral membrane (neutral sphingomyelinase II) (SMPD3) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB13001 Alkaline sphingomyelin phosphodiesterase,Alk-SMase,Ectonucleotide pyrophosphatase_phosphodiesterase family member 7,E-NPP 7,Enpp7,Intestinal alkaline sphingomyelinase,NPP-7,Rat,Rattus norvegicus
EIAAB27970 Lyso-PAF-PLC,Lyso-platelet-activating factor-phospholipase C,Mouse,Mus musculus,Neutral sphingomyelinase,nSMase,N-SMase,Smpd2,Sphingomyelin phosphodiesterase 2
EIAAB27969 Lyso-PAF-PLC,Lyso-platelet-activating factor-phospholipase C,Neutral sphingomyelinase,nSMase,N-SMase,Rat,Rattus norvegicus,Smpd2,Sphingomyelin phosphodiesterase 2
EIAAB27968 Homo sapiens,Human,Lyso-PAF-PLC,Lyso-platelet-activating factor-phospholipase C,Neutral sphingomyelinase,nSMase,N-SMase,SMPD2,Sphingomyelin phosphodiesterase 2
EIAAB13000 Alkaline sphingomyelin phosphodiesterase,Alk-SMase,Ectonucleotide pyrophosphatase_phosphodiesterase family member 7,E-NPP 7,ENPP7,Homo sapiens,Human,Intestinal alkaline sphingomyelinase,NPP-7,UNQ3077_
CSB-EL021846MO Mouse sphingomyelin phosphodiesterase 2, neutral membrane (neutral sphingomyelinase) (SMPD2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL021847HU Human sphingomyelin phosphodiesterase 3, neutral membrane (neutral sphingomyelinase II) (SMPD3) ELISA kit, Species Human, Sample Type serum, plasma 96T


 

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