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Ectonucleotide pyrophosphatase/phosphodiesterase family member 6 (E-NPP 6) (NPP-6) (EC 3.1.4.-) (EC 3.1.4.38) (Choline-specific glycerophosphodiester phosphodiesterase) (Glycerophosphocholine cholinephosphodiesterase) (GPC-Cpde)

 ENPP6_HUMAN             Reviewed;         440 AA.
Q6UWR7; Q4W5Q1; Q96M57;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
13-JUN-2006, sequence version 2.
25-OCT-2017, entry version 116.
RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 6;
Short=E-NPP 6;
Short=NPP-6;
EC=3.1.4.-;
EC=3.1.4.38;
AltName: Full=Choline-specific glycerophosphodiester phosphodiesterase;
AltName: Full=Glycerophosphocholine cholinephosphodiesterase;
Short=GPC-Cpde;
Flags: Precursor;
Name=ENPP6; ORFNames=UNQ1889/PRO4334;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-419.
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBSTRATE
SPECIFICITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=15788404; DOI=10.1074/jbc.M413438200;
Sakagami H., Aoki J., Natori Y., Nishikawa K., Kakehi Y., Natori Y.,
Arai H.;
"Biochemical and molecular characterization of a novel choline-
specific glycerophosphodiester phosphodiesterase belonging to the
nucleotide pyrophosphatase/phosphodiesterase family.";
J. Biol. Chem. 280:23084-23093(2005).
[6]
HOMODIMERIZATION, AND GPI-ANCHOR.
TISSUE=Brain;
PubMed=23161088; DOI=10.1007/s11064-012-0921-z;
Greiner-Tollersrud L., Berg T., Stensland H.M., Evjen G.,
Greiner-Tollersrud O.K.;
"Bovine brain myelin glycerophosphocholine choline phosphodiesterase
is an alkaline lysosphingomyelinase of the eNPP-family, regulated by
lysosomal sorting.";
Neurochem. Res. 38:300-310(2013).
-!- FUNCTION: Choline-specific glycerophosphodiester
phosphodiesterase. The preferred substrate may be
lysosphingomyelin (By similarity). Hydrolyzes
lysophosphatidylcholine (LPC) to form monoacylglycerol and
phosphorylcholine but not lysophosphatidic acid, showing it has a
lysophospholipase C activity. Has a preference for LPC with short
(12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids.
Also hydrolyzes glycerophosphorylcholine and
sphingosylphosphorylcholine efficiently. Hydrolyzes the classical
substrate for phospholipase C, p-nitrophenyl phosphorylcholine in
vitro, while it does not hydrolyze the classical nucleotide
phosphodiesterase substrate, p-nitrophenyl thymidine 5'-
monophosphate. Does not hydrolyze diacyl phospholipids such as
phosphatidylethanolamine, phosphatidylinositol,
phosphatidylserine, phosphatidylglycerol and phosphatidic acid.
{ECO:0000250, ECO:0000269|PubMed:15788404}.
-!- CATALYTIC ACTIVITY: A lysophosphatidylcholine + H(2)O = a
monoacylglycerol + phosphocholine. {ECO:0000269|PubMed:15788404}.
-!- CATALYTIC ACTIVITY: sn-glycero-3-phosphocholine + H(2)O = glycerol
+ phosphocholine. {ECO:0000269|PubMed:15788404}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000269|PubMed:15788404};
-!- ENZYME REGULATION: Inhibited by EDTA and EGTA in vitro.
{ECO:0000269|PubMed:15788404}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=344 uM for GPC {ECO:0000269|PubMed:15788404};
KM=296 uM for 12:0-LPC {ECO:0000269|PubMed:15788404};
KM=440 uM for 14:0-LPC {ECO:0000269|PubMed:15788404};
KM=165 uM for 16:0-LPC {ECO:0000269|PubMed:15788404};
KM=434 uM for 18:2-LPC {ECO:0000269|PubMed:15788404};
KM=563 uM for 20:4-LPC {ECO:0000269|PubMed:15788404};
Vmax=484 nmol/min/mg enzyme with GPC as substrate
{ECO:0000269|PubMed:15788404};
Vmax=463 nmol/min/mg enzyme with 12:0-LPC as substrate
{ECO:0000269|PubMed:15788404};
Vmax=367 nmol/min/mg enzyme with 14:0-LPC as substrate
{ECO:0000269|PubMed:15788404};
Vmax=89 nmol/min/mg enzyme with 16:0-LPC as substrate
{ECO:0000269|PubMed:15788404};
Vmax=285 nmol/min/mg enzyme with 18:2-LPC as substrate
{ECO:0000269|PubMed:15788404};
Vmax=470 nmol/min/mg enzyme with 20:4-LPC as substrate
{ECO:0000269|PubMed:15788404};
pH dependence:
Optimum pH is 8.5-7.5. {ECO:0000269|PubMed:15788404};
-!- SUBUNIT: Homodimer; disulfide-linked.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15788404};
Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15788404}. Note=A
small amount of the protein may be found in the extracellular
milieu.
-!- TISSUE SPECIFICITY: Predominantly expressed in kidney and brain.
In the kidney, expressed specifically in the proximal tubules and
thin descending limbs of Henle (at protein level).
{ECO:0000269|PubMed:15788404}.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY358676; AAQ89039.1; -; mRNA.
EMBL; AK057370; BAB71455.1; -; mRNA.
EMBL; AC079080; AAY40908.1; -; Genomic_DNA.
EMBL; AC107222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC035035; AAH35035.1; -; mRNA.
CCDS; CCDS3834.1; -.
RefSeq; NP_699174.1; NM_153343.3.
UniGene; Hs.297814; -.
ProteinModelPortal; Q6UWR7; -.
SMR; Q6UWR7; -.
BioGrid; 126350; 42.
IntAct; Q6UWR7; 1.
STRING; 9606.ENSP00000296741; -.
ChEMBL; CHEMBL6033; -.
iPTMnet; Q6UWR7; -.
PhosphoSitePlus; Q6UWR7; -.
BioMuta; ENPP6; -.
DMDM; 108935979; -.
PaxDb; Q6UWR7; -.
PeptideAtlas; Q6UWR7; -.
PRIDE; Q6UWR7; -.
Ensembl; ENST00000296741; ENSP00000296741; ENSG00000164303.
GeneID; 133121; -.
KEGG; hsa:133121; -.
UCSC; uc003iwc.3; human.
CTD; 133121; -.
EuPathDB; HostDB:ENSG00000164303.10; -.
GeneCards; ENPP6; -.
HGNC; HGNC:23409; ENPP6.
HPA; HPA042740; -.
MIM; 616983; gene.
neXtProt; NX_Q6UWR7; -.
OpenTargets; ENSG00000164303; -.
PharmGKB; PA134945118; -.
eggNOG; KOG2645; Eukaryota.
eggNOG; COG1524; LUCA.
GeneTree; ENSGT00760000119157; -.
HOGENOM; HOG000112376; -.
HOVERGEN; HBG107851; -.
InParanoid; Q6UWR7; -.
KO; K08743; -.
OMA; KVYMYYW; -.
OrthoDB; EOG091G06NA; -.
PhylomeDB; Q6UWR7; -.
TreeFam; TF330032; -.
BRENDA; 3.1.4.3; 2681.
Reactome; R-HSA-6814848; Glycerophospholipid catabolism.
GenomeRNAi; 133121; -.
PRO; PR:Q6UWR7; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000164303; -.
CleanEx; HS_ENPP6; -.
ExpressionAtlas; Q6UWR7; baseline and differential.
Genevisible; Q6UWR7; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0047390; F:glycerophosphocholine cholinephosphodiesterase activity; IDA:UniProtKB.
GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:Ensembl.
GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:UniProtKB.
GO; GO:0019695; P:choline metabolic process; IDA:UniProtKB.
GO; GO:0046475; P:glycerophospholipid catabolic process; TAS:Reactome.
GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core.
InterPro; IPR029889; ENPP6.
InterPro; IPR002591; Phosphodiest/P_Trfase.
PANTHER; PTHR10151:SF66; PTHR10151:SF66; 1.
Pfam; PF01663; Phosphodiest; 1.
SUPFAM; SSF53649; SSF53649; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
GPI-anchor; Hydrolase; Lipid degradation; Lipid metabolism;
Lipoprotein; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Signal.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 419 Ectonucleotide
pyrophosphatase/phosphodiesterase family
member 6.
/FTId=PRO_0000239361.
PROPEP 420 440 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000420890.
ACT_SITE 71 71 Nucleophile. {ECO:0000255}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000250|UniProtKB:B0BND0}.
LIPID 419 419 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 404 404 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 142 154 {ECO:0000250}.
DISULFID 412 412 Interchain. {ECO:0000250}.
VARIANT 357 357 D -> N (in dbSNP:rs4488969).
/FTId=VAR_052942.
VARIANT 419 419 S -> G (in dbSNP:rs4479748).
{ECO:0000269|PubMed:12975309}.
/FTId=VAR_026644.
SEQUENCE 440 AA; 50241 MW; 5F4F930D26EFB6B6 CRC64;
MAVKLGTLLL ALALGLAQPA SARRKLLVFL LDGFRSDYIS DEALESLPGF KEIVSRGVKV
DYLTPDFPSL SYPNYYTLMT GRHCEVHQMI GNYMWDPTTN KSFDIGVNKD SLMPLWWNGS
EPLWVTLTKA KRKVYMYYWP GCEVEILGVR PTYCLEYKNV PTDINFANAV SDALDSFKSG
RADLAAIYHE RIDVEGHHYG PASPQRKDAL KAVDTVLKYM TKWIQERGLQ DRLNVIIFSD
HGMTDIFWMD KVIELNKYIS LNDLQQVKDR GPVVSLWPAP GKHSEIYNKL STVEHMTVYE
KEAIPSRFYY KKGKFVSPLT LVADEGWFIT ENREMLPFWM NSTGRREGWQ RGWHGYDNEL
MDMRGIFLAF GPDFKSNFRA APIRSVDVYN VMCNVVGITP LPNNGSWSRV MCMLKGRAST
APPVWPSHCA LALILLFLLA


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