ENPP6_MOUSE
ID ENPP6_MOUSE Reviewed; 440 AA.
AC Q8BGN3; Q4VAH5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glycerophosphocholine cholinephosphodiesterase ENPP6 {ECO:0000305};
DE Short=GPC-Cpde;
DE EC=3.1.4.- {ECO:0000269|PubMed:15788404};
DE EC=3.1.4.38 {ECO:0000269|PubMed:15788404, ECO:0000269|PubMed:26888014};
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|MGI:MGI:2445171};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP TISSUE SPECIFICITY, FUNCTION, AND CATALYTIC ACTIVITY.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-421 IN COMPLEX WITH
RP PHOSPHOCHOLINE AND ZINC, GLYCOSYLATION AT ASN-100; ASN-118; ASN-341 AND
RP ASN-404, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION
RP PHENOTYPE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DISULFIDE BOND, AND
RP MUTAGENESIS OF SER-71; TYR-72; TYR-75; CYS-154; TYR-188; GLU-190; CYS-393
RP AND CYS-412.
RX PubMed=26888014; DOI=10.1038/srep20995;
RA Morita J., Kano K., Kato K., Takita H., Sakagami H., Yamamoto Y.,
RA Mihara E., Ueda H., Sato T., Tokuyama H., Arai H., Asou H., Takagi J.,
RA Ishitani R., Nishimasu H., Nureki O., Aoki J.;
RT "Structure and biological function of ENPP6, a choline-specific
RT glycerophosphodiester-phosphodiesterase.";
RL Sci. Rep. 6:20995-20995(2016).
CC -!- FUNCTION: Choline-specific glycerophosphodiesterase that hydrolyzes
CC glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and
CC contributes to supplying choline to the cells (PubMed:15788404,
CC PubMed:26888014). Has a preference for LPC with short (12:0 and 14:0)
CC or polyunsaturated (18:2 and 20:4) fatty acids (PubMed:15788404). In
CC vitro, hydrolyzes only choline-containing lysophospholipids, such as
CC sphingosylphosphorylcholine (SPC), platelet-activating factor (PAF) and
CC lysoPAF, but not other lysophospholipids (PubMed:15788404).
CC {ECO:0000269|PubMed:15788404, ECO:0000269|PubMed:26888014}.
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, ECO:0000269|PubMed:26888014};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19546;
CC Evidence={ECO:0000269|PubMed:26888014};
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:0000305|PubMed:15788404};
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:0000269|PubMed:15788404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36084;
CC Evidence={ECO:0000305|PubMed:15788404};
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:0000269|PubMed:15788404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41128;
CC Evidence={ECO:0000305|PubMed:15788404};
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:0000269|PubMed:15788404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41120;
CC Evidence={ECO:0000305|PubMed:15788404};
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:0000269|PubMed:15788404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41004;
CC Evidence={ECO:0000305|PubMed:15788404};
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:0000269|PubMed:15788404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41000;
CC Evidence={ECO:0000305|PubMed:15788404};
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:0000269|PubMed:15788404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41096;
CC Evidence={ECO:0000305|PubMed:15788404};
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:0000269|PubMed:15788404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41092;
CC Evidence={ECO:0000305|PubMed:15788404};
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:0000269|PubMed:15788404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41116;
CC Evidence={ECO:0000305|PubMed:15788404};
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:0000269|PubMed:26888014};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61685;
CC Evidence={ECO:0000269|PubMed:26888014};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:26888014};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:26888014};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and EGTA in vitro.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:26888014). Homotetramer
CC (PubMed:26888014). {ECO:0000250, ECO:0000269|PubMed:26888014}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in kidney with a lesser
CC expression in brain and heart (PubMed:15788404, PubMed:26888014). In
CC the brain and spinal cord, mainly expressed in the white matter. In
CC oligodendrocytes, is predominantly detected in the myelin sheath. In
CC the kidney, is predominantly expressed in the luminal side of the renal
CC tubule in the cortex and in the proximal renal tubules. It is expressed
CC in liver sinusoidal endothelial cells (PubMed:26888014).
CC {ECO:0000269|PubMed:15788404, ECO:0000269|PubMed:26888014}.
CC -!- DEVELOPMENTAL STAGE: At postnatal day 2 (P2) and P4, is detected in
CC immature oligodendrocytes, where it was predominantly found both in the
CC processes and cell bodies. In contrast, at P12 and P14, it is found
CC mainly in myelin sheaths. {ECO:0000269|PubMed:26888014}.
CC -!- DISRUPTION PHENOTYPE: Enpp6 knockout mice give birth according to the
CC Mendelian rule and are apparently normal. Mice exhibit mild symptoms of
CC fatty liver and are more susceptible to a choline-deficient diet and
CC exhibit severe fatty liver phenotypes at the early stage.
CC {ECO:0000269|PubMed:26888014}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; AK046797; BAC32873.1; -; mRNA.
DR EMBL; AK046881; BAC32906.1; -; mRNA.
DR EMBL; BC096376; AAH96376.1; -; mRNA.
DR CCDS; CCDS40335.1; -.
DR RefSeq; NP_796278.1; NM_177304.4.
DR PDB; 5EGE; X-ray; 2.00 A; A/B/C/D=1-421.
DR PDB; 5EGH; X-ray; 1.80 A; A/B=1-421.
DR PDBsum; 5EGE; -.
DR PDBsum; 5EGH; -.
DR AlphaFoldDB; Q8BGN3; -.
DR SMR; Q8BGN3; -.
DR IntAct; Q8BGN3; 2.
DR MINT; Q8BGN3; -.
DR STRING; 10090.ENSMUSP00000044608; -.
DR SwissLipids; SLP:000000637; -.
DR GlyConnect; 2277; 5 N-Linked glycans (4 sites).
DR GlyGen; Q8BGN3; 5 sites, 5 N-linked glycans (4 sites).
DR iPTMnet; Q8BGN3; -.
DR PhosphoSitePlus; Q8BGN3; -.
DR jPOST; Q8BGN3; -.
DR MaxQB; Q8BGN3; -.
DR PaxDb; Q8BGN3; -.
DR PeptideAtlas; Q8BGN3; -.
DR PRIDE; Q8BGN3; -.
DR ProteomicsDB; 275912; -.
DR Antibodypedia; 28837; 207 antibodies from 21 providers.
DR DNASU; 320981; -.
DR Ensembl; ENSMUST00000039840; ENSMUSP00000044608; ENSMUSG00000038173.
DR GeneID; 320981; -.
DR KEGG; mmu:320981; -.
DR UCSC; uc009lqr.1; mouse.
DR CTD; 133121; -.
DR MGI; MGI:2445171; Enpp6.
DR VEuPathDB; HostDB:ENSMUSG00000038173; -.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000158457; -.
DR HOGENOM; CLU_017594_2_0_1; -.
DR InParanoid; Q8BGN3; -.
DR OMA; KEAWQNG; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; Q8BGN3; -.
DR TreeFam; TF330032; -.
DR BRENDA; 3.1.4.2; 3474.
DR BRENDA; 3.1.4.3; 3474.
DR BRENDA; 3.1.4.38; 3474.
DR Reactome; R-MMU-6814848; Glycerophospholipid catabolism.
DR BioGRID-ORCS; 320981; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Enpp6; mouse.
DR PRO; PR:Q8BGN3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BGN3; protein.
DR Bgee; ENSMUSG00000038173; Expressed in lumbar subsegment of spinal cord and 105 other tissues.
DR ExpressionAtlas; Q8BGN3; baseline and differential.
DR Genevisible; Q8BGN3; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0047390; F:glycerophosphocholine cholinephosphodiesterase activity; IMP:UniProtKB.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IDA:MGI.
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; IDA:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; 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:0000250"
FT CHAIN 23..419
FT /note="Glycerophosphocholine cholinephosphodiesterase
FT ENPP6"
FT /id="PRO_0000239363"
FT PROPEP 420..440
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420891"
FT ACT_SITE 71
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGH"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGH"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGH"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGH"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGH"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGH"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
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:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
FT DISULFID 142..154
FT /evidence="ECO:0000269|PubMed:26888014,
FT ECO:0007744|PDB:5EGE, ECO:0007744|PDB:5EGH"
FT DISULFID 412
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT MUTAGEN 71
FT /note="S->A: Almost loss of glycerophosphocholine
FT cholinephosphodiesterase activity. Loss of choline
FT metabolism."
FT /evidence="ECO:0000269|PubMed:26888014"
FT MUTAGEN 71
FT /note="S->T: Almost loss of glycerophosphocholine
FT cholinephosphodiesterase activity. Loss of choline
FT metabolism."
FT /evidence="ECO:0000269|PubMed:26888014"
FT MUTAGEN 72
FT /note="Y->A: Highly decreases glycerophosphocholine
FT cholinephosphodiesterase activity. Loss of choline
FT metabolism."
FT /evidence="ECO:0000269|PubMed:26888014"
FT MUTAGEN 75
FT /note="Y->A: Highly decreases glycerophosphocholine
FT cholinephosphodiesterase activity. Loss of choline
FT metabolism."
FT /evidence="ECO:0000269|PubMed:26888014"
FT MUTAGEN 154
FT /note="C->A: Highly decreases glycerophosphocholine
FT cholinephosphodiesterase activity. Loss of choline
FT metabolism."
FT /evidence="ECO:0000269|PubMed:26888014"
FT MUTAGEN 188
FT /note="Y->A: Highly decreases glycerophosphocholine
FT cholinephosphodiesterase activity. Loss of choline
FT metabolism."
FT /evidence="ECO:0000269|PubMed:26888014"
FT MUTAGEN 190
FT /note="E->A: Highly decreases glycerophosphocholine
FT cholinephosphodiesterase activity. Loss of choline
FT metabolism."
FT /evidence="ECO:0000269|PubMed:26888014"
FT MUTAGEN 393
FT /note="C->A: Does not affect glycerophosphocholine
FT cholinephosphodiesterase activity; when associated with S-
FT 412. Does not affect choline metabolism; when associated
FT with S-412."
FT /evidence="ECO:0000269|PubMed:26888014"
FT MUTAGEN 412
FT /note="C->S: Does not affect Glycerophosphocholine
FT cholinephosphodiesterase activity; when associated withA-
FT 393. Does not affect choline metabolism; when associated
FT with A-393."
FT /evidence="ECO:0000269|PubMed:26888014"
FT CONFLICT 384
FT /note="R -> K (in Ref. 2; AAH96376)"
FT /evidence="ECO:0000305"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:5EGH"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:5EGH"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:5EGH"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5EGH"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 163..178
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 204..226
FT /evidence="ECO:0007829|PDB:5EGH"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:5EGH"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:5EGH"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 388..396
FT /evidence="ECO:0007829|PDB:5EGH"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:5EGH"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:5EGH"
SQ SEQUENCE 440 AA; 50618 MW; 837B050E93EB7492 CRC64;
MAAKLWTFLL GFGLSWVWPA SAHRKLLVLL LDGFRSDYIS EDALASLPGF REIVNRGVKV
DYLTPDFPSL SYPNYYTLMT GRHCEVHQMI GNYMWDPRTN KSFDIGVNRD SLMPLWWNGS
EPLWITLMKA RRKVYMYYWP GCEVEILGVR PTYCLEYKTV PTDINFANAV SDALDSLKSG
RADLAAIYHE RIDVEGHHYG PSSPQRKDAL RAVDTVLKYM IQWIQDRGLQ QDLNVILFSD
HGMTDIFWMD KVIELSNYIS LDDLQQVKDR GPVVSLWPVP GKHSEIYHKL RTVEHMTVYE
KESIPNRFYY KKGKFVSPLT LVADEGWFIA ESREMLPFWM NSTGKREGWQ RGWHGYDNEL
MDMRGIFLAI GPDFKSNFRA APIRSVDVYN IMCHVAGITP LPNNGSWSRV VCMLKGQTSS
APPTPLNSCA LVLILLLYFV
