PLIN5_SHEEP
ID PLIN5_SHEEP Reviewed; 456 AA.
AC B0FJL7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Perilipin-5;
DE AltName: Full=Lipid storage droplet protein 5;
GN Name=Plin5; Synonyms=Lsdp5;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang Y.-K., Wang Y.-L., Guo Y.-J., Lee H.-J., Zhong K., Zhu H.-S.,
RA Wang Y.-Y., Han L.-Q., Wang L.-F., Yang G.-Y.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipid droplet-associated protein that maintains the balance
CC between lipogenesis and lipolysis and also regulates fatty acid
CC oxidation in oxidative tissues. Recruits mitochondria to the surface of
CC lipid droplets and is involved in lipid droplet homeostasis by
CC regulating both the storage of fatty acids in the form of triglycerides
CC and the release of fatty acids for mitochondrial fatty acid oxidation.
CC In lipid droplet triacylglycerol hydrolysis, plays a role as a
CC scaffolding protein for three major key lipolytic players: ABHD5,
CC PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of
CC PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets.
CC Phosphorylation by PKA enables lipolysis probably by promoting release
CC of ABHD5 from the perilipin scaffold and by facilitating interaction of
CC ABHD5 with PNPLA2. Also increases lipolysis through interaction with
CC LIPE and upon PKA-mediated phosphorylation of LIPE (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Interacts with PNPLA2; prevents interaction of
CC PNPLA2 with ABHD5. Interacts with ABHD5; targets ABHD5 to lipid
CC droplets and promotes interaction of ABHD5 with PNPLA2. Interacts with
CC LIPE (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q8BVZ1}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q8BVZ1}. Mitochondrion
CC {ECO:0000250|UniProtKB:M0R7Z9}. Note=Lipid droplet surface-associated.
CC Exchanges between lipid droplets and the cytoplasm.
CC {ECO:0000250|UniProtKB:Q8BVZ1}.
CC -!- PTM: Phosphorylated by PKA. Phosphorylated on serine in skeletal muscle
CC at rest or upon lipolytic stimulation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
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DR EMBL; EU330921; ABY53496.1; -; mRNA.
DR RefSeq; NP_001107246.1; NM_001113774.1.
DR AlphaFoldDB; B0FJL7; -.
DR SMR; B0FJL7; -.
DR STRING; 9940.ENSOARP00000010012; -.
DR GeneID; 100135434; -.
DR KEGG; oas:100135434; -.
DR CTD; 440503; -.
DR eggNOG; KOG4790; Eukaryota.
DR OrthoDB; 1437332at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; ISS:UniProtKB.
DR GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0060192; P:negative regulation of lipase activity; ISS:UniProtKB.
DR GO; GO:0035359; P:negative regulation of peroxisome proliferator activated receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; ISS:UniProtKB.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0060193; P:positive regulation of lipase activity; ISS:UniProtKB.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISS:UniProtKB.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; ISS:UniProtKB.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR004279; Perilipin.
DR Pfam; PF03036; Perilipin; 1.
DR PIRSF; PIRSF036881; PAT; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Lipid droplet; Mitochondrion; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..456
FT /note="Perilipin-5"
FT /id="PRO_0000338984"
FT REGION 1..173
FT /note="Essential for lipid droplet targeting"
FT /evidence="ECO:0000250"
FT REGION 1..108
FT /note="Interaction with LIPE"
FT /evidence="ECO:0000250"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..456
FT /note="Interaction with PNPLA2 and ABHD5"
FT /evidence="ECO:0000250"
FT REGION 420..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..456
FT /note="Recruits mitochondria at the lipid droplet surface"
FT /evidence="ECO:0000250"
FT COMPBIAS 440..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BVZ1"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BVZ1"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00G26"
SQ SEQUENCE 456 AA; 50229 MW; 11FDAB6717C1E77B CRC64;
MSEDEAAQAP GPSLSEQDQQ SAVQRVAALP LIRATCTAVS EAYSAAKDRH PLLGSACRLA
EHCVCDLTTR ALDHAQPLLS HLQPQLATVN DLACRGLDKL EEKLPFLQQP SETVVTSAKG
VVASSVTGMV GLARQGRRWS VELKRSVSHA MDVVLEKSEE LVDHFLPMTE EELAALAAEA
EGPEVGSVEE QRKHQGYFVR LGSLSTRLRH LAYEHSLGKL RQKKHHAQDT LAQLQETLEL
IHRMQCGVTP ITPARPGKVH ELWEDWSQRP LENGRRRHSQ AELETLVLSR NLMRELQSTV
DALETSVRGL PPSAQEKVAE VRRSVDALQA AFADARRFGD LPAAVLAEGR GSMARAHACV
DELLELVVQA MPLPWLVGPF APILVERPEP PPDLEALVDE VIGGPDPRWA HLDWPAQQRA
WQAQHGEGTV LSGNIPEEEP EPPSRPKHTL MPELDF
