ID A0A1S3FQ05_DIPOR Unreviewed; 297 AA.
AC A0A1S3FQ05;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Perilipin-5 {ECO:0000256|ARBA:ARBA00039212};
DE AltName: Full=Lipid storage droplet protein 5 {ECO:0000256|ARBA:ARBA00041242};
GN Name=Plin5 {ECO:0000313|RefSeq:XP_012878104.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012878104.1};
RN [1] {ECO:0000313|RefSeq:XP_012878104.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012878104.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00037149}.
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. {ECO:0000256|ARBA:ARBA00038796}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the perilipin family.
CC {ECO:0000256|ARBA:ARBA00006311}.
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DR RefSeq; XP_012878104.1; XM_013022650.1.
DR AlphaFoldDB; A0A1S3FQ05; -.
DR GeneID; 105990286; -.
DR KEGG; dord:105990286; -.
DR CTD; 440503; -.
DR InParanoid; A0A1S3FQ05; -.
DR OrthoDB; 3026676at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProt.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR Gene3D; 1.20.120.340; Flagellar protein FliS; 1.
DR Gene3D; 3.30.720.170; Perilipin, alpha-beta domain; 1.
DR InterPro; IPR004279; Perilipin.
DR PANTHER; PTHR14024; PERILIPIN; 1.
DR PANTHER; PTHR14024:SF9; PERILIPIN-5; 1.
DR Pfam; PF03036; Perilipin; 1.
DR SUPFAM; SSF109775; Mannose-6-phosphate receptor binding protein 1 (Tip47), C-terminal domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT REGION 169..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 32181 MW; 89AD253098EDF1AD CRC64;
MSDHAAATQD PRPSSEQEQQ NVVQRVAALP LVRAVSDAYC STKDRHGVLG SACRLAEHCV
CGLTTRALDH AQPLLDHLQP QLATVNHLAC RGLDKLEEKL PFLQQPSDTV LTSARDTVVS
GVSGVTGLAQ RGRRWSVELR RSVSHALDVV LGKSEELVDH LLPPTSEALE AKAQGPAVAE
AEAAEAASTE EQRRQQGYLV RLASLSSRIR HLAYEHSIGK LRQSKHCAQE MLVQLQEMLE
LIHRVQDRAA LPAKAQEPGG DRSPSPLQNG RCGQVELERL AAELARAVEG SVELGVS
//
