ENPP7
entrez
339221
canonical
uniprot
Q6UWV6
canonical
ensembl
ENSG00000182156
resolver
ensp
ENSP00000332656
resolver
ensp
ENSP00000534539
resolver
ensp
ENSP00000534540
resolver
enst
ENST00000328313
resolver
enst
ENST00000864480
resolver
genesymbol
ENPP7
resolver
hgnc
HGNC:23764
resolver
uniprot
Q6ZTS5
resolver
uniprot
Q8IUS8
resolver
uniprot_entry
ENPP7_HUMAN
resolver
uniprot_sec
Q6ZTS5
resolver
uniprot_sec
Q8IUS8
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited in a dose dependent manner by ATP, imidazole, orthovanadate and zinc ion. Not inhibited by ADP, AMP and EDTA. {ECO:0000269|PubMed:12885774}.
uniprot
proteins
amino_acid_sequence
MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA
uniprot
proteins
ec_number
3.1.4.12
uniprot
proteins
function
FUNCTION: Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract (PubMed:12671034, PubMed:12885774, PubMed:15205117, PubMed:16255717, PubMed:28292932). Also has phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation (PubMed:12885774, PubMed:16255717). Does not have nucleotide pyrophosphatase activity (PubMed:12885774). May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen (By similarity). {ECO:0000250|UniProtKB:Q3TIW9, ECO:0000269|PubMed:12671034, ECO:0000269|PubMed:12885774, ECO:0000269|PubMed:15205117, ECO:0000269|PubMed:16255717, ECO:0000269|PubMed:28292932}.
uniprot
proteins
mass_dalton
51478
uniprot
proteins
mutagenesis
MUTAGEN 76; /note="S->F: Loss of activity."; /evidence="ECO:0000269|PubMed:15458386"; MUTAGEN 78; /note="C->N: Strongly reduces activity."; /evidence="ECO:0000269|PubMed:15458386"; MUTAGEN 100; /note="N->Q: Strongly reduces N-glycosylation and enzyme activity; when associated with Q-121; Q-146; Q-168 and Q-267."; /evidence="ECO:0000269|PubMed:15458386"; MUTAGEN 109; /note="Y->L: Decreased enzyme activity with sphingomyelin and para-nitrophenylphosphorylcholine."; /evidence="ECO:0000269|PubMed:28292932"; MUTAGEN 121; /note="N->Q: Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-146; Q-168 and Q-267."; /evidence="ECO:0000269|PubMed:15458386"; MUTAGEN 146; /note="N->Q: Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-146; Q-168 and Q-267."; /evidence="ECO:0000269|PubMed:15458386"; MUTAGEN 166; /note="Y->L: Decreased enzyme activity with sphingomyelin and para-nitrophenylphosphorylcholine."; /evidence="ECO:0000269|PubMed:28292932"; MUTAGEN 168; /note="N->Q: Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-121; Q-168 and Q-267."; /evidence="ECO:0000269|PubMed:15458386"; MUTAGEN 267; /note="N->Q: Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-121; Q-146 and Q-168."; /evidence="ECO:0000269|PubMed:15458386"; MUTAGEN 271; /note="R->E: Decreased enzyme activity; when associated with E-343."; /evidence="ECO:0000269|PubMed:28292932"; MUTAGEN 343; /note="R->E: Decreased enzyme activity; when associated with E-271."; /evidence="ECO:0000269|PubMed:28292932"; MUTAGEN 344..348; /note="INVQF->ENEQE: Loss of enzyme activity with sphingomyelin."; /evidence="ECO:0000269|PubMed:28292932"; MUTAGEN 344..348; /note="INVQF->NNNQN: Loss of enzyme activity with sphingomyelin."; /evidence="ECO:0000269|PubMed:28292932"; MUTAGEN 353; /note="H->A: Loss of activity."; /evidence="ECO:0000269|PubMed:15016655
uniprot
proteins
post_translational_modification
PTM: N-glycosylated; required for activity and transport to the plasma membrane. {ECO:0000269|PubMed:15458386, ECO:0000269|PubMed:19159218}.
uniprot
proteins
protein_family
Nucleotide pyrophosphatase/phosphodiesterase family
uniprot
proteins
pubmed
12671034
uniprot
proteins
pubmed
12885774
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15016655
uniprot
proteins
pubmed
15205117
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15458386
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16255717
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
28292932
uniprot
proteins
sequence_length
458
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12671034, ECO:0000269|PubMed:15205117}; Single-pass type I membrane protein {ECO:0000269|PubMed:12671034, ECO:0000269|PubMed:15205117}. Note=The catalytic domain is released into the extracellular medium when cells are treated with trypsin (PubMed:15205117). Localized at the surface of the microvillar membrane in small intestine enterocytes, and in endosome-like structures situated beneath the microvillar membrane, and in Golgi complex (PubMed:12671034, PubMed:12885774). {ECO:0000269|PubMed:12671034, ECO:0000269|PubMed:12885774, ECO:0000269|PubMed:15205117}.
uniprot
proteins
transmembrane_region
TRANSMEM 434..454; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins