Lpin1
entrez
14245
canonical
uniprot
Q91ZP3
canonical
ensembl
ENSMUSG00000020593
resolver
ensp
ENSMUSP00000070583
resolver
ensp
ENSMUSP00000106696
resolver
ensp
ENSMUSP00000152276
resolver
ensp
ENSMUSP00000152285
resolver
ensp
ENSMUSP00000152466
resolver
ensp
ENSMUSP00000158955
resolver
ensp
ENSMUSP00000159076
resolver
ensp
ENSMUSP00000211572
resolver
ensp
ENSMUSP00000211573
resolver
ensp
ENSMUSP00000211577
resolver
enst
ENSMUST00000067124
resolver
enst
ENSMUST00000111067
resolver
enst
ENSMUST00000221230
resolver
enst
ENSMUST00000221297
resolver
enst
ENSMUST00000222989
resolver
enst
ENSMUST00000239165
resolver
genesymbol
Lpin1
resolver
genesymbol_syn
Flde
resolver
uniprot
A0A0R4J0V3
resolver
uniprot
A0A1Y7VLN4
resolver
uniprot
A0A5F8MQ53
resolver
uniprot
E9QKQ5
resolver
uniprot
Q8CD95
resolver
uniprot
Q9CQI2
resolver
uniprot
Q9JLG6
resolver
uniprot_entry
A0A1Y7VLN4_MOUSE
resolver
uniprot_entry
A0A5F8MQ53_MOUSE
resolver
uniprot_entry
E9QKQ5_MOUSE
resolver
uniprot_entry
LPIN1_MOUSE
resolver
uniprot_entry
Q8CD95_MOUSE
resolver
uniprot_sec
A0A0R4J0V3
resolver
uniprot_sec
Q9CQI2
resolver
uniprot_sec
Q9JLG6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by N-ethylmaleimide treatment. {ECO:0000269|PubMed:17158099}.
uniprot
proteins
amino_acid_sequence
MNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVIRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKLGDNGEAFFVQETDNDQEIIPMYLATSPILSEGAARMESQLKRNSVDRIRCLDPTTAAQGLPPSDTPSTGSLGKKRRKRRRKAQLDNLKRDDNVNSSEDEDMFPIEMSSDEDTAPMDGSRTLPNDVPPFQDDIPKENFPSISTHPQSASYPSSDREWSPSPSSLVDCQRTPPHLAEGVLSSSCPLQSCHFHASESPSGSRPSTPKSDSELVSKSADRLTPKNNLEMLWLWGELPQAAKSSSPHKMKESSPLGSRKTPDKMNFQAIHSESSDTFSDQSPTMARGLLIHQSKAQTEMQFVNEEDLESLGAAAPPSPVAEELKAPYPNTAQSSSKTDSPSRKKDKRSRHLGADGVYLDDLTDMDPEVAALYFPKNGDPGGLPKQASDNGARSANQSPQSVGGSGIDSGVESTSDSLRDLPSIAISLCGGLSDHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKVGNKYYNWTTAAPLLLAMQAFQKPLPKATVESIMRDKMPKKGGRWWFSWRGRNATIKEESKPEQCLTGKGHNTGEQPAQLGLATRIKHESSSSDEEHAAAKPSGSSHLSLLSNVSYKKTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFPLLKRSHSCDFPCSDTFSNFTFWREPLPPFENQDMHSASA
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Lpin1 are the cause of the fatty liver dystrophy phenotype (fld). Fld mutant mice are characterized by neonatal fatty liver and hypertriglyceridemia that resolve at weaning, and neuropathy affecting peripheral nerve in adulthood. Adipose tissue deficiency, glucose intolerance and increased susceptibility to atherosclerosis are associated with this mutation too. Two independent mutant alleles are characterized in this phenotype, fld and fld2j. {ECO:0000269|PubMed:11138012}.
uniprot
proteins
ec_number
3.1.3.4
uniprot
proteins
function
FUNCTION: Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis and therefore controls the metabolism of fatty acids at different levels (PubMed:17158099). Is involved in adipocyte differentiation (PubMed:16049017). Also acts as nuclear transcriptional coactivator for PPARGC1A/PPARA regulatory pathway to modulate lipid metabolism gene expression (PubMed:16950137). {ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:16950137, ECO:0000269|PubMed:17158099}.; FUNCTION: [Isoform 1]: Recruited at the mitochondrion outer membrane and is involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol. {ECO:0000269|PubMed:21397848}.
uniprot
proteins
mass_dalton
102002
uniprot
proteins
mutagenesis
MUTAGEN 106; /note="S->A: Abolishes phosphorylation in response to insulin but has no effect on cellular location."; /evidence="ECO:0000269|PubMed:19717560"; MUTAGEN 599; /note="K->R: Reduces sumoylation. Abolishes sumoylation and nuclear localization; when associated with R-629."; /evidence="ECO:0000269|PubMed:19753306"; MUTAGEN 629; /note="K->R: Reduces sumoylation. Abolishes sumoylation and nuclear localization; when associated with R-599."; /evidence="ECO:0000269|PubMed:19753306"; MUTAGEN 712; /note="D->A,E: Abolishes phosphatidate phosphatase activity. No effect on interaction or coactivation with PPARA."; /evidence="ECO:0000269|PubMed:16950137, ECO:0000269|PubMed:21397848"; MUTAGEN 726; /note="I->F: Diminishes significantly the interaction and coactivation OFPPARA; when associated with F-727."; /evidence="ECO:0000269|PubMed:16950137"; MUTAGEN 727; /note="L->F: Diminishes significantly the interaction and coactivation OFPPARA; when associated with F-726."; /evidence="ECO:0000269|PubMed:16950137"; MUTAGEN Q91ZP3-2:724; /note="S->L: Abolishes phosphatidate phosphatase activity but does not prevent membrane association."; /evidence="ECO:0000269|PubMed:19717560
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at multiple sites in response to insulin. Phosphorylation is controlled by the mTOR signaling pathway. Phosphorylation is decreased by epinephrine. Phosphorylation may not directly affect the catalytic activity but may regulate the localization. Dephosphorylated by the CTDNEP1-CNEP1R1 complex. {ECO:0000269|PubMed:17105729}.; PTM: Phosphorylated at multiple sites by mTOR in response to insulin, leading to its inactivation (PubMed:17105729). Phosphorylation does not affect the catalytic activity but regulates the localization (PubMed:17105729). Phosphorylation is decreased by epinephrine (PubMed:17105729). Dephosphorylated by the CTDNEP1-CNEP1R1 complex (PubMed:17105729). Dephosphorylation following mTOR inhibition promotes its activity (By similarity). {ECO:0000250|UniProtKB:Q14693, ECO:0000269|PubMed:17105729}.; PTM: Sumoylation is important in brain and is marginal in other tissues. Sumoylation facilitates nuclear localization of isoform 2 in neuronals cells and its transcriptional coactivator activity. {ECO:0000269|PubMed:19753306}.; PTM: Acetylation at Lys-459 and Lys-629 by KAT5 in response to fatty acids promotes translocation to the endoplasmic reticulum and synthesis of diacylglycerol. {ECO:0000250|UniProtKB:Q14693}.
uniprot
proteins
protein_family
Lipin family
uniprot
proteins
pubmed
11138012
uniprot
proteins
pubmed
11792863
uniprot
proteins
pubmed
16049017
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16950137
uniprot
proteins
pubmed
17105729
uniprot
proteins
pubmed
17158099
uniprot
proteins
pubmed
19717560
uniprot
proteins
pubmed
19753306
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21397848
uniprot
proteins
pubmed
22134922
uniprot
proteins
pubmed
23426360
uniprot
proteins
sequence_length
924
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion outer membrane {ECO:0000269|PubMed:21397848}. Cytoplasm {ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:21397848}. Nucleus membrane {ECO:0000269|PubMed:21397848}. Note=Recruited at the mitochondrion outer membrane following phosphatidic acid formation mediated by PLD6. In neuronals cells, isoform 1 is exclusively cytoplasmic (PubMed:21397848). In 3T3-L1 pre-adipocytes, it primarily located in the cytoplasm (PubMed:16049017). {ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:21397848}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:11138012, ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:17105729, ECO:0000269|PubMed:19753306, ECO:0000269|PubMed:22134922}. Cytoplasm {ECO:0000269|PubMed:19753306}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14693}. Note=Nuclear localization requires both CNEP1R1 and CTDNEP1 (PubMed:22134922). In neuronals cells, localized in both the cytoplasm and the nucleus (PubMed:19753306). In 3T3-L1 pre-adipocytes, it is predominantly nuclear (PubMed:16049017). Translocates from the cytosol to the endoplasmic reticulum following acetylation by KAT5 (By similarity). {ECO:0000250|UniProtKB:Q14693, ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:19753306, ECO:0000269|PubMed:22134922}.
uniprot
proteins