Lipe
entrez
25330
canonical
uniprot
P15304
canonical
ensembl
ENSRNOG00000020546
resolver
ensp
ENSRNOP00000027911
resolver
ensp
ENSRNOP00000096661
resolver
genesymbol
Lipe
resolver
uniprot
Q6LCQ2
resolver
uniprot_entry
LIPS_RAT
resolver
uniprot_sec
Q6LCQ2
resolver
activity_regulation
ACTIVITY REGULATION: Rapidly activated by cAMP-dependent phosphorylation under the influence of catecholamines (PubMed:6374655). Dephosphorylation and inactivation are controlled by insulin (PubMed:6374655). cAMP stimulates its retinyl ester hydrolase activity (PubMed:9162045). {ECO:0000269|PubMed:6374655, ECO:0000269|PubMed:9162045}.
uniprot
proteins
amino_acid_sequence
MKPRRPISFTREITAMEPSSTSVSRPEWRPEAQQTLTDYPGSRELQEFGIPQKQSLPNEATAQQGAEFQQEQGVQQSTLLQKLLTPLAFPVPQQSFPSHKVHSDQQEATSQNGPGAGKVHTTQKELEHRDEHVGTAESGPAEPPPATEVEATSIAQAVSGPDKKLPTQTDLVSQERAEQSDPTAQQTPLVQGVKSDQGSLIESGILARLQKLAIQQPSQEWKTFLDCVTESDMEKYLNSSSKSNPPEPSGGTVIPGTLPSKQKPDCGKMSGYGGKLPHGKKGILQKHKHYWDTASAFSHSMDLRTMTQSLVALAEDNMAFFSSQGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRASHNLAELEAYLAALTQLRALAYYAQRLLTINRPGVLFFEGDEGLSADFLQDYVTLHKGCFYGRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNITEIEVLSSLANMASTTVRVSRLLSLPPEAFEMPLTSDPKLTVTISPPLAHTGPGPVLARLISYDLREGQDSKMLNSLAKSEGPRLELRPRPQQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLGSTGERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLQSSASPSRLLSLMDPLLPLSVLSKCVSAYSGTETEDHFDSDQKALGVMGLVQRDTSLFLRDLRLGASSWLNSFLELSGRKPHKTPLPATETLRPTDSGRLTESMRRSVSEAALAQPEGLLGTDSLKKLTIKDLSFKGNSEPSDSPEMSQSMETLGPSTPSDVNFFLRSGNSQEEAETRDDISPMDGIPRVRAAFPDGFHPRRSSQGVLHMPLYSSPIVKNPFMSPLLAPDVMLKTLPPVHLVACALDPMLDDSVMFARRLKDLGQPVTLKVVEDLPHGFLSLAALCRETRQAAELCVQRIRLILTPPAAPLT
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:10694408, PubMed:6643478, PubMed:9162045). Shows a preferential hydrolysis of DAGs over TAGs and MAGs and preferentially hydrolyzes the fatty acid (FA) esters at the sn-3 position of DAGs (By similarity). Preferentially hydrolyzes fatty acids at the sn-1 and sn-2 positions of TAGs (PubMed:6643478). 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 (PubMed:1770312). {ECO:0000250|UniProtKB:P54310, ECO:0000269|PubMed:10694408, ECO:0000269|PubMed:6643478, ECO:0000269|PubMed:9162045, ECO:0000303|PubMed:1770312}.
uniprot
proteins
mass_dalton
116812
uniprot
proteins
mutagenesis
MUTAGEN 863; /note="S->A,E: No effect on activation by PKA."; /evidence="ECO:0000269|PubMed:9417067"; MUTAGEN 865; /note="S->A: Increases activation by PKA."; /evidence="ECO:0000269|PubMed:9417067"; MUTAGEN 865; /note="S->E: No effect on activation by PKA."; /evidence="ECO:0000269|PubMed:9417067"; MUTAGEN 959; /note="S->A: Slightly decreases activation by PKA. Abolishes activation by PKA; when associated with A-960."; /evidence="ECO:0000269|PubMed:9417067"; MUTAGEN 960; /note="S->A: No effect on activation by PKA. Abolishes activation by PKA; when associated with A-959."; /evidence="ECO:0000269|PubMed:9417067
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:0000269|PubMed:15878856}.
uniprot
proteins
protein_family
'GDXG' lipolytic enzyme family
uniprot
proteins
pubmed
10694408
uniprot
proteins
pubmed
15878856
uniprot
proteins
pubmed
1770312
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24303154
uniprot
proteins
pubmed
3186461
uniprot
proteins
pubmed
3420405
uniprot
proteins
pubmed
6374655
uniprot
proteins
pubmed
6643478
uniprot
proteins
pubmed
8812477
uniprot
proteins
pubmed
9162045
uniprot
proteins
pubmed
9417067
uniprot
proteins
sequence_length
1068
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05469}. Membrane, caveola {ECO:0000250|UniProtKB:Q05469}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q05469}. Lipid droplet {ECO:0000269|PubMed:15878856}. Note=Found in the high-density caveolae (By similarity). Translocates to the cytoplasm from the caveolae upon insulin stimulation (By similarity). Phosphorylation by AMPK reduces its translocation towards the lipid droplets. {ECO:0000250|UniProtKB:Q05469, ECO:0000269|PubMed:15878856}.
uniprot
proteins