LIPE
entrez
3991
canonical
uniprot
Q05469
canonical
ensembl
ENSG00000079435
resolver
ensp
ENSP00000244289
resolver
ensp
ENSP00000469545
resolver
enst
ENST00000597620
resolver
genesymbol
LIPE
resolver
hgnc
HGNC:6621
resolver
uniprot
A8K8W7
resolver
uniprot
M0QY29
resolver
uniprot
Q3LRT2
resolver
uniprot
Q6NSL7
resolver
uniprot_entry
A8K8W7_HUMAN
resolver
uniprot_entry
LIPS_HUMAN
resolver
uniprot_entry
M0QY29_HUMAN
resolver
uniprot_sec
Q3LRT2
resolver
uniprot_sec
Q6NSL7
resolver
activity_regulation
ACTIVITY REGULATION: Retinyl ester hydrolase is inhibited by bis-p-nitrophenyl phosphate. {ECO:0000269|PubMed:15955102}.
uniprot
proteins
amino_acid_sequence
MEPGSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPLTQQETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLGKESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQETPEQSDKQTTPVQGAKSKQGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVGSSSDTDSPATMGGMVAQGVKLGFKGKSGYKVMSGYSGTSPHEKTSARNHRHYQDTASRLIHNMDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAHLFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWKAFWNITEMEVLSSLANMASATVRVSRLLSLPPEAFEMPLTADPTLTVTISPPLAHTGPGPVLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPRPQQAPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERICLAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLQPAASPSRLLSLMDPLLPLSVLSKCVSAYAGAKTEDHSNSDQKALGMMGLVRRDTALLLRDFRLGASSWLNSFLELSGRKSQKMSEPIAEPMRRSVSEAALAQPQGPLGTDSLKNLTLRDLSLRGNSETSSDTPEMSLSAETLSPSTPSDVNFLLPPEDAGEEAEAKNELSPMDRGLGVRAAFPEGFHPRRSSQGATQMPLYSSPIVKNPFMSPLLAPDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVEDLPHGFLTLAALCRETRQAAELCVERIRLVLTPPAGAGPSGETGAAGVDGGCGGRH
uniprot
proteins
disease_involvement
DISEASE: Lipodystrophy, familial partial, 6 (FPLD6) [MIM:615980]: An autosomal recessive form of lipodystrophy characterized by abnormal subcutaneous fat distribution. Affected individuals have increased visceral fat, impaired lipolysis, dyslipidemia, hepatic steatosis, systemic insulin resistance, and diabetes. Some patients manifest muscular dystrophy. {ECO:0000269|PubMed:24848981}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.1.23
uniprot
proteins
ec_number
3.1.1.79
uniprot
proteins
function
FUNCTION: Lipase with broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters (PubMed:15716583, PubMed:15955102, PubMed:19800417, PubMed:8812477). Shows a preferential hydrolysis of DAGs over TAGs and MAGs and preferentially hydrolyzes the fatty acid (FA) esters at the sn-3 position of the glycerol backbone in DAGs (PubMed:19800417). Preferentially hydrolyzes FA esters at the sn-1 and sn-2 positions of the glycerol backbone in TAGs (By similarity). Catalyzes the hydrolysis of 2-arachidonoylglycerol, an endocannabinoid and of 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor (By similarity). In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production (By similarity). {ECO:0000250|UniProtKB:P15304, ECO:0000250|UniProtKB:P54310, ECO:0000269|PubMed:15716583, ECO:0000269|PubMed:15955102, ECO:0000269|PubMed:19800417, ECO:0000269|PubMed:8812477}.
uniprot
proteins
mass_dalton
116598
uniprot
proteins
pathway_participation
PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by AMPK reduces its translocation towards the lipid droplets. {ECO:0000250|UniProtKB:P54310}.
uniprot
proteins
protein_family
'GDXG' lipolytic enzyme family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15716583
uniprot
proteins
pubmed
15955102
uniprot
proteins
pubmed
16803459
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17026959
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19800417
uniprot
proteins
pubmed
24848981
uniprot
proteins
pubmed
8506334
uniprot
proteins
pubmed
8812477
uniprot
proteins
sequence_length
1076
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17026959}. Membrane, caveola {ECO:0000269|PubMed:16803459, ECO:0000269|PubMed:17026959}. Cytoplasm, cytosol {ECO:0000269|PubMed:17026959}. Lipid droplet {ECO:0000250|UniProtKB:P54310}. Note=Found in the high-density caveolae. Translocates to the cytoplasm from the caveolae upon insulin stimulation (PubMed:17026959). Phosphorylation by AMPK reduces its translocation towards the lipid droplets (By similarity). {ECO:0000250|UniProtKB:P54310, ECO:0000269|PubMed:17026959}.
uniprot
proteins