ENPP6_DANRE
ID ENPP6_DANRE Reviewed; 438 AA.
AC Q5BKW7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Glycerophosphocholine cholinephosphodiesterase ENPP6 {ECO:0000250|UniProtKB:Q6UWR7};
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}; ORFNames=zgc:103605;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Liver;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; BC090903; AAH90903.1; -; mRNA.
DR RefSeq; NP_001013545.1; NM_001013527.1.
DR AlphaFoldDB; Q5BKW7; -.
DR SMR; Q5BKW7; -.
DR STRING; 7955.ENSDARP00000059230; -.
DR PaxDb; Q5BKW7; -.
DR GeneID; 791915; -.
DR KEGG; dre:791915; -.
DR CTD; 133121; -.
DR ZFIN; ZDB-GENE-031205-1; enpp6.
DR eggNOG; KOG2645; Eukaryota.
DR InParanoid; Q5BKW7; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; Q5BKW7; -.
DR Reactome; R-DRE-6814848; Glycerophospholipid catabolism.
DR PRO; PR:Q5BKW7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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; Coiled coil; Disulfide bond; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipid degradation; Lipid metabolism; Lipoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..415
FT /note="Glycerophosphocholine cholinephosphodiesterase
FT ENPP6"
FT /id="PRO_0000239365"
FT PROPEP 416..438
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420895"
FT COILED 162..226
FT /evidence="ECO:0000255"
FT ACT_SITE 69
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 69
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 69
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 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 191
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 195
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 238
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 239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 239
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 352
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT BINDING 352
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 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B0BND0"
FT LIPID 415
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
FT DISULFID 140..152
FT /evidence="ECO:0000250|UniProtKB:Q8BGN3"
SQ SEQUENCE 438 AA; 50694 MW; 8E5DCD7BF71D56DC CRC64;
MTRTLLKIYT LFILLLCRQR DANRKLLVFL IDGFRHDYMD DLHNLPGFRE IVENGVKVDY
LTPDFPSLSY PNYYSLMTGR HCEVHQMTGN YMWDTDTQKE FLIGTNPDSR LPMWWDGSEP
LWVTMQKLGK KVYMYYWPGC EVTILGVRPT FCEEYVYNPS EKNLTDSMEN ALNALKSSKA
DMAGIYYEKI DVEGHHFGPR SPEIQRAIRS LDQAFQILNQ KIREKNMRDT INVVLFSDHG
MTQLKWMEKI IELDNYINMS HIIKMMDRGP VVSLWPKQDK FEEIYQNLST ADNMNVYKKH
EIPDRFHYKN GQFVSTLTLV AEPGWFITEN KAKLPFWNNG TEAAGGWQHG WHGYDNEFVD
MRGSFLAQGP DFKSNYRAGP IRTVDVYNVL CKTLGMNPLP NNGSWSRVEC MMRSSAATAG
ASLISCCFLL LLTLTGVC
