Plin5
entrez
66968
canonical
uniprot
Q8BVZ1
canonical
ensembl
ENSMUSG00000011305
resolver
ensp
ENSMUSP00000019808
resolver
ensp
ENSMUSP00000108695
resolver
ensp
ENSMUSP00000174370
resolver
genesymbol
Plin5
resolver
genesymbol_syn
Lsdp5
resolver
genesymbol_syn
Mldp
resolver
genesymbol_syn
Oxpat
resolver
genesymbol_syn
Pat1
resolver
uniprot
Q78IK8
resolver
uniprot_entry
PLIN5_MOUSE
resolver
uniprot_sec
Q78IK8
resolver
amino_acid_sequence
MDQRGEDTTLAPHSRMSGDQTAQDPGSSLGELDQQNVVNRVVALPLVKATCTAVSSAYNSAKDRHPLLGSACRLAEHCVCSVTTCALDHAQPLLEHLQPQLATVNDLACRGLDKLEEKLPFLQQPSDMVVTSAKDTVAKSVTGMVDLAQRGRRWSGELRRSMSQAMDMVLGKSEKLVDRFLPMTEAELAVLAAEAEGPEVGTVEEQRQQQGYFVRLGSLSARLRHLAYEHSLGKLRQSKHRTQEMLAQLQETLELIQHMQRGASPSPTFHPPKTQELWGSWSPCLENGRSHSEVELETLALSRSLTLELQNAVDALAGCVRGLPPSAQAKVAEVQRSVDALQATFADAHCLGDVAPTALAEGRGSVARAHACVDEFLDLVLRAMPLPWLVGPFAPILVEQSEPLINLATCVDEVVGDPDPRWAHMDWPAQKRAWEAESADPGGQEAEPPRGQGKHTMMPELDF
uniprot
proteins
function
FUNCTION: Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE. {ECO:0000269|PubMed:17130488, ECO:0000269|PubMed:19064991, ECO:0000269|PubMed:21393244, ECO:0000269|PubMed:21885430, ECO:0000269|PubMed:22532565, ECO:0000269|PubMed:22675471, ECO:0000269|PubMed:23345411}.
uniprot
proteins
mass_dalton
50474
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PKA. Phosphorylated on serine in skeletal muscle at rest or with lipolytic stimulation. {ECO:0000269|PubMed:21393244}.
uniprot
proteins
protein_family
Perilipin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16571721
uniprot
proteins
pubmed
17130488
uniprot
proteins
pubmed
17234449
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19064991
uniprot
proteins
pubmed
19717842
uniprot
proteins
pubmed
21148142
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21393244
uniprot
proteins
pubmed
21885430
uniprot
proteins
pubmed
22532565
uniprot
proteins
pubmed
22675471
uniprot
proteins
pubmed
23345411
uniprot
proteins
pubmed
23423172
uniprot
proteins
pubmed
23606724
uniprot
proteins
sequence_length
463
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:16571721, ECO:0000269|PubMed:17130488, ECO:0000269|PubMed:17234449, ECO:0000269|PubMed:19717842, ECO:0000269|PubMed:23345411}. Cytoplasm {ECO:0000269|PubMed:17234449, ECO:0000269|PubMed:19717842}. Mitochondrion {ECO:0000250|UniProtKB:M0R7Z9}. Note=Lipid droplet surface-associated (PubMed:16571721, PubMed:17130488, PubMed:17234449). Exchanges between lipid droplets and the cytoplasm (PubMed:19717842). {ECO:0000269|PubMed:16571721, ECO:0000269|PubMed:17130488, ECO:0000269|PubMed:17234449, ECO:0000269|PubMed:19717842}.
uniprot
proteins