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Ectonucleotide pyrophosphatase/phosphodiesterase family member 7 (E-NPP 7) (NPP-7) (EC 3.1.4.12) (Alkaline sphingomyelin phosphodiesterase) (Intestinal alkaline sphingomyelinase) (Alk-SMase)

 ENPP7_HUMAN             Reviewed;         458 AA.
Q6UWV6; Q6ZTS5; Q8IUS8;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 3.
28-FEB-2018, entry version 129.
RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 7;
Short=E-NPP 7;
Short=NPP-7;
EC=3.1.4.12;
AltName: Full=Alkaline sphingomyelin phosphodiesterase;
AltName: Full=Intestinal alkaline sphingomyelinase;
Short=Alk-SMase;
Flags: Precursor;
Name=ENPP7 {ECO:0000312|EMBL:AAH41453.2}; ORFNames=UNQ3077/PRO9912;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAP69661.1}
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 137-151; 239-248;
256-271 AND 313-326, VARIANT PRO-4, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Colon {ECO:0000269|PubMed:12885774},
Kidney {ECO:0000269|PubMed:12885774},
Small intestine {ECO:0000269|PubMed:12885774}, and
Stomach {ECO:0000269|PubMed:12885774};
PubMed=12885774; DOI=10.1074/jbc.M305437200;
Duan R.-D., Bergman T., Xu N., Wu J., Cheng Y., Duan J., Nelander S.,
Palmberg C., Nilsson A.;
"Identification of human intestinal alkaline sphingomyelinase as a
novel ecto-enzyme related to the nucleotide phosphodiesterase
family.";
J. Biol. Chem. 278:38528-38536(2003).
[2] {ECO:0000305, ECO:0000312|EMBL:AAQ88985.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3] {ECO:0000305, ECO:0000312|EMBL:BAC86504.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-4.
TISSUE=Liver {ECO:0000312|EMBL:BAC86504.1};
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).
[4] {ECO:0000305, ECO:0000312|EMBL:AAH41453.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-4.
TISSUE=Colon {ECO:0000312|EMBL:AAH41453.2};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5] {ECO:0000305}
PROTEIN SEQUENCE OF 22-36.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[6] {ECO:0000305}
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12671034; DOI=10.1194/jlr.M300037-JLR200;
Duan R.-D., Cheng Y., Hansen G., Hertervig E., Liu J.-J., Syk I.,
Sjostrom H., Nilsson A.;
"Purification, localization, and expression of human intestinal
alkaline sphingomyelinase.";
J. Lipid Res. 44:1241-1250(2003).
[7] {ECO:0000305}
MUTAGENESIS OF HIS-353.
PubMed=15016655; DOI=10.1093/carcin/bgh140;
Wu J., Cheng Y., Nilsson A., Duan R.-D.;
"Identification of one exon deletion of intestinal alkaline
sphingomyelinase in colon cancer HT-29 cells and a differentiation-
related expression of the wild-type enzyme in Caco-2 cells.";
Carcinogenesis 25:1327-1333(2004).
[8] {ECO:0000305}
GLYCOSYLATION AT ASN-100; ASN-121; ASN-146; ASN-168 AND ASN-267, AND
MUTAGENESIS OF SER-76; CYS-78; ASN-100; ASN-121; ASN-146; ASN-168 AND
ASN-267.
PubMed=15458386; DOI=10.1042/BJ20041455;
Wu J., Hansen G.H., Nilsson A., Duan R.-D.;
"Functional studies of human intestinal alkaline sphingomyelinase by
deglycosylation and mutagenesis.";
Biochem. J. 386:153-160(2005).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
-!- FUNCTION: Converts sphingomyelin to ceramide. Also has
phospholipase C activity toward palmitoyl lyso-phosphocholine.
Does not appear to have nucleotide pyrophosphatase activity.
{ECO:0000269|PubMed:12885774}.
-!- CATALYTIC ACTIVITY: Sphingomyelin + H(2)O = N-acylsphingosine +
phosphocholine. {ECO:0000269|PubMed:12885774}.
-!- ENZYME REGULATION: Inhibited in a dose dependent manner by ATP,
imidazole, orthovanadate and zinc ion. Not inhibited by ADP, AMP
and EDTA. {ECO:0000269|PubMed:12885774}.
-!- INTERACTION:
Q08379:GOLGA2; NbExp=4; IntAct=EBI-12047821, EBI-618309;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12671034,
ECO:0000305}; Single-pass type I membrane protein
{ECO:0000269|PubMed:12671034, ECO:0000305}. Note=Localized at the
surface of the microvillar membrane in small intestine
enterocytes, and in endosome-like structures situated beneath the
microvillar membrane, and in Golgi complex.
{ECO:0000269|PubMed:12671034, ECO:0000269|PubMed:12885774}.
-!- TISSUE SPECIFICITY: Detected in the colon (at protein level).
Expressed in the duodenum, jejunum and liver and at low levels in
the ileum. Expression was very low in the esophagus, stomach and
colon. {ECO:0000269|PubMed:12671034, ECO:0000269|PubMed:12885774}.
-!- PTM: N-glycosylated; required for activity and transport to the
plasma membrane. {ECO:0000269|PubMed:15458386,
ECO:0000269|PubMed:19159218}.
-!- MISCELLANEOUS: Decreased levels of alkaline sphingomyelin
phosphodiesterase may be associated with colon cancer.
{ECO:0000303|PubMed:12671034, ECO:0000303|PubMed:15016655}.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ENPP7ID44055ch17q25.html";
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EMBL; AY230663; AAP69661.1; -; mRNA.
EMBL; AY358622; AAQ88985.1; -; mRNA.
EMBL; AK126250; BAC86504.1; -; mRNA.
EMBL; BC041453; AAH41453.2; -; mRNA.
CCDS; CCDS11763.1; -.
RefSeq; NP_848638.3; NM_178543.4.
UniGene; Hs.114084; -.
PDB; 5TCD; X-ray; 2.40 A; A=22-433.
PDB; 5UDY; X-ray; 2.60 A; A=22-433.
PDBsum; 5TCD; -.
PDBsum; 5UDY; -.
ProteinModelPortal; Q6UWV6; -.
SMR; Q6UWV6; -.
BioGrid; 130844; 12.
IntAct; Q6UWV6; 8.
STRING; 9606.ENSP00000332656; -.
ChEMBL; CHEMBL6058; -.
SwissLipids; SLP:000000173; -.
iPTMnet; Q6UWV6; -.
PhosphoSitePlus; Q6UWV6; -.
DMDM; 134047772; -.
PaxDb; Q6UWV6; -.
PeptideAtlas; Q6UWV6; -.
PRIDE; Q6UWV6; -.
Ensembl; ENST00000328313; ENSP00000332656; ENSG00000182156.
GeneID; 339221; -.
KEGG; hsa:339221; -.
UCSC; uc002jxa.5; human.
CTD; 339221; -.
DisGeNET; 339221; -.
EuPathDB; HostDB:ENSG00000182156.9; -.
GeneCards; ENPP7; -.
H-InvDB; HIX0027161; -.
HGNC; HGNC:23764; ENPP7.
HPA; HPA024603; -.
MIM; 616997; gene.
neXtProt; NX_Q6UWV6; -.
PharmGKB; PA134986550; -.
eggNOG; KOG2645; Eukaryota.
eggNOG; COG1524; LUCA.
HOGENOM; HOG000231018; -.
HOVERGEN; HBG106748; -.
InParanoid; Q6UWV6; -.
KO; K12354; -.
OrthoDB; EOG091G06NA; -.
PhylomeDB; Q6UWV6; -.
TreeFam; TF330032; -.
BRENDA; 3.1.4.12; 2681.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
GeneWiki; ENPP7; -.
GenomeRNAi; 339221; -.
PRO; PR:Q6UWV6; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000182156; -.
CleanEx; HS_ENPP7; -.
ExpressionAtlas; Q6UWV6; baseline and differential.
Genevisible; Q6UWV6; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0005902; C:microvillus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IDA:UniProtKB.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0008156; P:negative regulation of DNA replication; IDA:UniProtKB.
GO; GO:0006685; P:sphingomyelin catabolic process; IEA:InterPro.
GO; GO:0006684; P:sphingomyelin metabolic process; IDA:UniProtKB.
Gene3D; 3.40.720.10; -; 2.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR029895; ENPP7.
InterPro; IPR002591; Phosphodiest/P_Trfase.
PANTHER; PTHR10151:SF63; PTHR10151:SF63; 1.
Pfam; PF01663; Phosphodiest; 1.
SUPFAM; SSF53649; SSF53649; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Glycoprotein; Hydrolase; Membrane; Polymorphism; Reference proteome;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255,
ECO:0000269|PubMed:15340161}.
CHAIN 22 458 Ectonucleotide
pyrophosphatase/phosphodiesterase family
member 7.
/FTId=PRO_0000036403.
TRANSMEM 434 454 Helical. {ECO:0000255}.
REGION 72 78 Required for enzyme activity.
ACT_SITE 75 75 Nucleophile. {ECO:0000250}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15458386}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15458386}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15458386,
ECO:0000269|PubMed:19159218}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15458386}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15458386}.
VARIANT 4 4 L -> P (in dbSNP:rs8074547).
{ECO:0000269|PubMed:12885774,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_021506.
MUTAGEN 76 76 S->F: Loss of activity.
{ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:15458386}.
MUTAGEN 78 78 C->N: Strongly reduces activity.
{ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:15458386}.
MUTAGEN 100 100 N->Q: Strongly reduces N-glycosylation
and enzyme activity; when associated with
Q-121; Q-146; Q-168 and Q-267.
{ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:15458386}.
MUTAGEN 121 121 N->Q: Strongly reduces N-glycosylation
and enzyme activity; when associated with
Q-100; Q-146; Q-168 and Q-267.
{ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:15458386}.
MUTAGEN 146 146 N->Q: Strongly reduces N-glycosylation
and enzyme activity; when associated with
Q-100; Q-146; Q-168 and Q-267.
{ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:15458386}.
MUTAGEN 168 168 N->Q: Strongly reduces N-glycosylation
and enzyme activity; when associated with
Q-100; Q-121; Q-168 and Q-267.
{ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:15458386}.
MUTAGEN 267 267 N->Q: Strongly reduces N-glycosylation
and enzyme activity; when associated with
Q-100; Q-121; Q-146 and Q-168.
{ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:15458386}.
MUTAGEN 353 353 H->A: Loss of activity.
{ECO:0000269|PubMed:15016655}.
CONFLICT 101 101 T -> I (in Ref. 2; AAQ88985).
{ECO:0000305}.
CONFLICT 388 388 Y -> N (in Ref. 3; BAC86504).
{ECO:0000305}.
STRAND 32 38 {ECO:0000244|PDB:5TCD}.
TURN 43 48 {ECO:0000244|PDB:5TCD}.
HELIX 52 60 {ECO:0000244|PDB:5TCD}.
STRAND 61 65 {ECO:0000244|PDB:5TCD}.
HELIX 75 84 {ECO:0000244|PDB:5TCD}.
HELIX 88 91 {ECO:0000244|PDB:5TCD}.
STRAND 96 100 {ECO:0000244|PDB:5TCD}.
TURN 101 104 {ECO:0000244|PDB:5TCD}.
STRAND 105 107 {ECO:0000244|PDB:5TCD}.
HELIX 109 112 {ECO:0000244|PDB:5TCD}.
HELIX 116 119 {ECO:0000244|PDB:5TCD}.
HELIX 126 131 {ECO:0000244|PDB:5TCD}.
TURN 132 134 {ECO:0000244|PDB:5TCD}.
STRAND 137 141 {ECO:0000244|PDB:5TCD}.
TURN 143 146 {ECO:0000244|PDB:5TCD}.
STRAND 155 158 {ECO:0000244|PDB:5TCD}.
HELIX 169 185 {ECO:0000244|PDB:5TCD}.
STRAND 189 195 {ECO:0000244|PDB:5TCD}.
HELIX 199 205 {ECO:0000244|PDB:5TCD}.
HELIX 210 232 {ECO:0000244|PDB:5TCD}.
TURN 236 238 {ECO:0000244|PDB:5TCD}.
STRAND 239 244 {ECO:0000244|PDB:5TCD}.
HELIX 262 264 {ECO:0000244|PDB:5TCD}.
HELIX 270 272 {ECO:0000244|PDB:5TCD}.
STRAND 273 277 {ECO:0000244|PDB:5TCD}.
STRAND 283 288 {ECO:0000244|PDB:5TCD}.
HELIX 293 300 {ECO:0000244|PDB:5TCD}.
STRAND 307 311 {ECO:0000244|PDB:5TCD}.
HELIX 312 314 {ECO:0000244|PDB:5TCD}.
HELIX 317 319 {ECO:0000244|PDB:5TCD}.
STRAND 329 334 {ECO:0000244|PDB:5TCD}.
STRAND 350 352 {ECO:0000244|PDB:5TCD}.
HELIX 360 362 {ECO:0000244|PDB:5TCD}.
STRAND 366 370 {ECO:0000244|PDB:5TCD}.
STRAND 375 379 {ECO:0000244|PDB:5TCD}.
HELIX 384 386 {ECO:0000244|PDB:5TCD}.
HELIX 387 395 {ECO:0000244|PDB:5TCD}.
HELIX 406 408 {ECO:0000244|PDB:5TCD}.
HELIX 410 412 {ECO:0000244|PDB:5TCD}.
SEQUENCE 458 AA; 51494 MW; F6A06913C33E4398 CRC64;
MRGLAVLLTV ALATLLAPGA GAPVQSQGSQ NKLLLVSFDG FRWNYDQDVD TPNLDAMARD
GVKARYMTPA FVTMTSPCHF TLVTGKYIEN HGVVHNMYYN TTSKVKLPYH ATLGIQRWWD
NGSVPIWITA QRQGLRAGSF FYPGGNVTYQ GVAVTRSRKE GIAHNYKNET EWRANIDTVM
AWFTEEDLDL VTLYFGEPDS TGHRYGPESP ERREMVRQVD RTVGYLRESI ARNHLTDRLN
LIITSDHGMT TVDKRAGDLV EFHKFPNFTF RDIEFELLDY GPNGMLLPKE GRLEKVYDAL
KDAHPKLHVY KKEAFPEAFH YANNPRVTPL LMYSDLGYVI HGRINVQFNN GEHGFDNKDM
DMKTIFRAVG PSFRAGLEVE PFESVHVYEL MCRLLGIVPE ANDGHLATLL PMLHTESALP
PDGRPTLLPK GRSALPPSSR PLLVMGLLGT VILLSEVA


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