ENPP6_PIG
ID ENPP6_PIG Reviewed; 440 AA.
AC Q58D68;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Glycerophosphocholine cholinephosphodiesterase ENPP6 {ECO:0000250|UniProtKB:Q8BGN3};
DE Short=GPC-Cpde;
DE EC=3.1.4.- {ECO:0000250|UniProtKB:Q8BGN3};
DE EC=3.1.4.38 {ECO:0000250|UniProtKB:Q8BGN3};
DE AltName: Full=Choline-specific glycerophosphodiester phosphodiesterase {ECO:0000250|UniProtKB:Q8BGN3};
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:0000250|UniProtKB:Q6UWR7};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15679890; DOI=10.1186/1741-7007-3-2;
RA Jorgensen F.G., Hobolth A., Hornshoj H., Bendixen C., Fredholm M.,
RA Schierup M.H.;
RT "Comparative analysis of protein coding sequences from human, mouse and the
RT domesticated pig.";
RL BMC Biol. 3:2-2(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
RX PubMed=17145712; DOI=10.1093/nar/gkl954;
RA Uenishi H., Eguchi-Ogawa T., Shinkai H., Okumura N., Suzuki K., Toki D.,
RA Hamasima N., Awata T.;
RT "PEDE (Pig EST Data Explorer) has been expanded into Pig Expression Data
RT Explorer, including 10 147 porcine full-length cDNA sequences.";
RL Nucleic Acids Res. 35:D650-D653(2007).
CC -!- FUNCTION: Choline-specific glycerophosphodiesterase that hydrolyzes
CC glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and
CC contributes to supplying choline to the cells. Has a preference for LPC
CC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty
CC acids. In vitro, hydrolyzes only choline-containing lysophospholipids,
CC such as sphingosylphosphorylcholine (SPC), platelet-activating factor
CC (PAF) and lysoPAF, but not other lysophospholipids.
CC {ECO:0000250|UniProtKB:Q8BGN3}.
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:0000250|UniProtKB:Q8BGN3};
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:0000250|UniProtKB:Q8BGN3};
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:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homotetramer. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q8BGN3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
CC -!- CAUTION: This sequence was originally thought to derive from Bos taurus
CC (PubMed:16305752). In fact it derives from Sus scrofa (PubMed:15679890
CC and PubMed:17145712). {ECO:0000305|PubMed:16305752}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46576.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BT021729; AAX46576.1; ALT_INIT; mRNA.
DR EMBL; AY609869; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK236257; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK345705; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK347685; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q58D68; -.
DR SMR; Q58D68; -.
DR STRING; 9823.ENSSSCP00000022663; -.
DR PaxDb; Q58D68; -.
DR PeptideAtlas; Q58D68; -.
DR PRIDE; Q58D68; -.
DR eggNOG; KOG2645; Eukaryota.
DR InParanoid; Q58D68; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0047390; F:glycerophosphocholine cholinephosphodiesterase activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0019695; P:choline metabolic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; ISS: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 2: Evidence at transcript 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_0000239359"
FT PROPEP 420..440
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420892"
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 CONFLICT 127
FT /note="L -> P (in Ref. 3; AK345705)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="F -> L (in Ref. 3; AK236257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 50356 MW; 9ABBC7EEDF20A701 CRC64;
MAMKFGALLL VLVLSLAQPA SGRRKLLVFL LDGFRSDYIS DEALESLPGF KEIVSRGVKV
DYLTPDFPSL SYPNYYTLMT GRHCEVHQMI GNYMWDPATN KSFDIGVNRD SLMPLWWNGS
EPLWITLTKA KRKVYMYYWP GCEVEILGVR PTYCLEYKNV PTDINFANAV SDALDFFKSG
QADLAAIYHE RIDVEGHHFG PSSPQRRDAL KAVDTVLKYM TEWIQERELQ DDLNVIIFSD
HGMTDIFWMD KVIELNKYIS LNDLQQVKDR GPVVSLWPAP GKHSEIYNKL RRVEHMTVYE
KEAIPSRFYY KKGKFVSPLT LVADEGWFIT ENRELLPFWM NSTGKREGWQ RGWHGYDNEL
RDMRGIFLAF GPDFKSNFRA APIRSVDVYN VMCSVAGITP LPNNGSWSRV VCMLKDPVSS
APAALPSACV LALILLWLLA
