ENPP6_HUMAN
ID ENPP6_HUMAN Reviewed; 440 AA.
AC Q6UWR7; Q4W5Q1; Q96M57;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glycerophosphocholine cholinephosphodiesterase ENPP6 {ECO:0000305};
DE Short=GPC-Cpde;
DE EC=3.1.4.- {ECO:0000250|UniProtKB:Q8BGN3};
DE EC=3.1.4.38 {ECO:0000269|PubMed:15788404};
DE AltName: Full=Choline-specific glycerophosphodiester phosphodiesterase {ECO:0000303|PubMed:15788404};
DE AltName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 6;
DE Short=E-NPP 6;
DE Short=NPP-6;
DE Flags: Precursor;
GN Name=ENPP6 {ECO:0000312|HGNC:HGNC:23409}; ORFNames=UNQ1889/PRO4334;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-419.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBSTRATE SPECIFICITY,
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=15788404; DOI=10.1074/jbc.m413438200;
RA Sakagami H., Aoki J., Natori Y., Nishikawa K., Kakehi Y., Natori Y.,
RA Arai H.;
RT "Biochemical and molecular characterization of a novel choline-specific
RT glycerophosphodiester phosphodiesterase belonging to the nucleotide
RT pyrophosphatase/phosphodiesterase family.";
RL J. Biol. Chem. 280:23084-23093(2005).
RN [6]
RP HOMODIMERIZATION, AND GPI-ANCHOR.
RC TISSUE=Brain;
RX PubMed=23161088; DOI=10.1007/s11064-012-0921-z;
RA Greiner-Tollersrud L., Berg T., Stensland H.M., Evjen G.,
RA Greiner-Tollersrud O.K.;
RT "Bovine brain myelin glycerophosphocholine choline phosphodiesterase is an
RT alkaline lysosphingomyelinase of the eNPP-family, regulated by lysosomal
RT sorting.";
RL Neurochem. Res. 38:300-310(2013).
CC -!- FUNCTION: Choline-specific glycerophosphodiesterase that hydrolyzes
CC glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and
CC contributes to supplying choline to the cells (PubMed:15788404). Has a
CC preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2
CC and 20:4) fatty acids. In vitro, hydrolyzes only choline-containing
CC lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet-
CC activating factor (PAF) and lysoPAF, but not other lysophospholipids
CC (By similarity). {ECO:0000250|UniProtKB:Q8BGN3,
CC ECO:0000269|PubMed:15788404}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 3-phosphocholine = glycerol + H(+) +
CC phosphocholine; Xref=Rhea:RHEA:19545, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:295975; EC=3.1.4.38;
CC Evidence={ECO:0000269|PubMed:15788404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19546;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:44720,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:64683, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000269|PubMed:15788404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44721;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-
CC glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:36083,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15850,
CC ChEBI:CHEBI:30909, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36084;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + H2O = 1-dodecanoyl-
CC sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41127,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74966,
CC ChEBI:CHEBI:75529, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41128;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycerol + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:41119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75542, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41120;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + H(+) +
CC phosphocholine; Xref=Rhea:RHEA:41003, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:34071, ChEBI:CHEBI:74344,
CC ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41004;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC tetradecanoyl-sn-glycerol + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:40999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64489, ChEBI:CHEBI:75536, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41000;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sphing-4-enine-phosphocholine = H(+) + phosphocholine +
CC sphing-4-enine; Xref=Rhea:RHEA:41095, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57756, ChEBI:CHEBI:58906,
CC ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41096;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:41091, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:75757, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41092;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-(9Z,12Z-octadecadienoyl)-sn-glycerol + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:41115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28733, ChEBI:CHEBI:75561, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41116;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycero-2-phosphocholine + H2O = glycerol + H(+) +
CC phosphocholine; Xref=Rhea:RHEA:61684, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:144950,
CC ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61685;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8BGN3};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q8BGN3};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and EGTA in vitro.
CC {ECO:0000269|PubMed:15788404}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=344 uM for GPC {ECO:0000269|PubMed:15788404};
CC KM=296 uM for 12:0-LPC {ECO:0000269|PubMed:15788404};
CC KM=440 uM for 14:0-LPC {ECO:0000269|PubMed:15788404};
CC KM=165 uM for 16:0-LPC {ECO:0000269|PubMed:15788404};
CC KM=434 uM for 18:2-LPC {ECO:0000269|PubMed:15788404};
CC KM=563 uM for 20:4-LPC {ECO:0000269|PubMed:15788404};
CC Vmax=484 nmol/min/mg enzyme with GPC as substrate
CC {ECO:0000269|PubMed:15788404};
CC Vmax=463 nmol/min/mg enzyme with 12:0-LPC as substrate
CC {ECO:0000269|PubMed:15788404};
CC Vmax=367 nmol/min/mg enzyme with 14:0-LPC as substrate
CC {ECO:0000269|PubMed:15788404};
CC Vmax=89 nmol/min/mg enzyme with 16:0-LPC as substrate
CC {ECO:0000269|PubMed:15788404};
CC Vmax=285 nmol/min/mg enzyme with 18:2-LPC as substrate
CC {ECO:0000269|PubMed:15788404};
CC Vmax=470 nmol/min/mg enzyme with 20:4-LPC as substrate
CC {ECO:0000269|PubMed:15788404};
CC pH dependence:
CC Optimum pH is 8.5-7.5. {ECO:0000269|PubMed:15788404};
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homotetramer. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8BGN3}.
CC -!- INTERACTION:
CC Q6UWR7; Q12797-6: ASPH; NbExp=3; IntAct=EBI-13382816, EBI-12092171;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15788404};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15788404}. Note=A small
CC amount of the protein may be found in the extracellular milieu.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in kidney and brain. In the
CC kidney, expressed specifically in the proximal tubules and thin
CC descending limbs of Henle (at protein level).
CC {ECO:0000269|PubMed:15788404}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; AY358676; AAQ89039.1; -; mRNA.
DR EMBL; AK057370; BAB71455.1; -; mRNA.
DR EMBL; AC079080; AAY40908.1; -; Genomic_DNA.
DR EMBL; AC107222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035035; AAH35035.1; -; mRNA.
DR CCDS; CCDS3834.1; -.
DR RefSeq; NP_699174.1; NM_153343.3.
DR AlphaFoldDB; Q6UWR7; -.
DR SMR; Q6UWR7; -.
DR BioGRID; 126350; 45.
DR IntAct; Q6UWR7; 31.
DR STRING; 9606.ENSP00000296741; -.
DR ChEMBL; CHEMBL6033; -.
DR GlyGen; Q6UWR7; 4 sites.
DR iPTMnet; Q6UWR7; -.
DR PhosphoSitePlus; Q6UWR7; -.
DR BioMuta; ENPP6; -.
DR DMDM; 108935979; -.
DR EPD; Q6UWR7; -.
DR jPOST; Q6UWR7; -.
DR MassIVE; Q6UWR7; -.
DR PaxDb; Q6UWR7; -.
DR PeptideAtlas; Q6UWR7; -.
DR PRIDE; Q6UWR7; -.
DR ProteomicsDB; 67516; -.
DR Antibodypedia; 28837; 207 antibodies from 21 providers.
DR DNASU; 133121; -.
DR Ensembl; ENST00000296741.7; ENSP00000296741.2; ENSG00000164303.11.
DR GeneID; 133121; -.
DR KEGG; hsa:133121; -.
DR MANE-Select; ENST00000296741.7; ENSP00000296741.2; NM_153343.4; NP_699174.1.
DR UCSC; uc003iwc.3; human.
DR CTD; 133121; -.
DR DisGeNET; 133121; -.
DR GeneCards; ENPP6; -.
DR HGNC; HGNC:23409; ENPP6.
DR HPA; ENSG00000164303; Tissue enhanced (brain, kidney).
DR MIM; 616983; gene.
DR neXtProt; NX_Q6UWR7; -.
DR OpenTargets; ENSG00000164303; -.
DR PharmGKB; PA134945118; -.
DR VEuPathDB; HostDB:ENSG00000164303; -.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000158457; -.
DR HOGENOM; CLU_017594_2_0_1; -.
DR InParanoid; Q6UWR7; -.
DR OMA; KEAWQNG; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; Q6UWR7; -.
DR TreeFam; TF330032; -.
DR BRENDA; 3.1.4.3; 2681.
DR PathwayCommons; Q6UWR7; -.
DR Reactome; R-HSA-6814848; Glycerophospholipid catabolism.
DR SignaLink; Q6UWR7; -.
DR BioGRID-ORCS; 133121; 11 hits in 1066 CRISPR screens.
DR ChiTaRS; ENPP6; human.
DR GenomeRNAi; 133121; -.
DR Pharos; Q6UWR7; Tbio.
DR PRO; PR:Q6UWR7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6UWR7; protein.
DR Bgee; ENSG00000164303; Expressed in C1 segment of cervical spinal cord and 126 other tissues.
DR ExpressionAtlas; Q6UWR7; baseline and differential.
DR Genevisible; Q6UWR7; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0047390; F:glycerophosphocholine cholinephosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0019695; P:choline metabolic process; IDA:UniProtKB.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; TAS:Reactome.
DR GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR029889; ENPP6.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151:SF66; PTHR10151:SF66; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..419
FT /note="Glycerophosphocholine cholinephosphodiesterase
FT ENPP6"
FT /id="PRO_0000239361"
FT PROPEP 420..440
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420890"
FT ACT_SITE 71
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B0BND0"
FT LIPID 419
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT DISULFID 142..154
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT DISULFID 412
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VARIANT 357
FT /note="D -> N (in dbSNP:rs4488969)"
FT /id="VAR_052942"
FT VARIANT 419
FT /note="S -> G (in dbSNP:rs4479748)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_026644"
SQ 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
