PLIN5_RAT
ID PLIN5_RAT Reviewed; 475 AA.
AC M0R7Z9;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Perilipin-5;
DE AltName: Full=Lipid storage droplet protein 5;
GN Name=Plin5; Synonyms=Lsdp5, Oxpat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION IN LIPID HOMEOSTASIS, ASSOCIATION WITH MITOCHONDRIA, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=21885430; DOI=10.1194/jlr.m017939;
RA Wang H., Sreenivasan U., Sreenevasan U., Hu H., Saladino A., Polster B.M.,
RA Lund L.M., Gong D.W., Stanley W.C., Sztalryd C.;
RT "Perilipin 5, a lipid droplet-associated protein, provides physical and
RT metabolic linkage to mitochondria.";
RL J. Lipid Res. 52:2159-2168(2011).
RN [4]
RP FUNCTION IN LIPID OXIDATION, AND SUBCELLULAR LOCATION.
RX PubMed=22127648; DOI=10.1007/s00418-011-0888-x;
RA Bosma M., Minnaard R., Sparks L.M., Schaart G., Losen M., de Baets M.H.,
RA Duimel H., Kersten S., Bickel P.E., Schrauwen P., Hesselink M.K.;
RT "The lipid droplet coat protein perilipin 5 also localizes to muscle
RT mitochondria.";
RL Histochem. Cell Biol. 137:205-216(2012).
RN [5]
RP INTERACTION WITH ABHD5 AND PNPLA2.
RX PubMed=23408028; DOI=10.1152/ajpregu.00418.2012;
RA MacPherson R.E., Ramos S.V., Vandenboom R., Roy B.D., Peters S.J.;
RT "Skeletal muscle PLIN proteins, ATGL and CGI-58, interactions at rest and
RT following stimulated contraction.";
RL Am. J. Physiol. 304:R644-R650(2013).
RN [6]
RP FUNCTION IN LIPID STORAGE.
RX PubMed=23353597; DOI=10.1016/j.bbalip.2013.01.007;
RA Bosma M., Sparks L.M., Hooiveld G.J., Jorgensen J.A., Houten S.M.,
RA Schrauwen P., Kersten S., Hesselink M.K.;
RT "Overexpression of PLIN5 in skeletal muscle promotes oxidative gene
RT expression and intramyocellular lipid content without compromising insulin
RT sensitivity.";
RL Biochim. Biophys. Acta 1831:844-852(2013).
RN [7]
RP INTERACTION WITH LIPE AND PNPLA2, AND PHOSPHORYLATION.
RX PubMed=24303154; DOI=10.1002/phy2.84;
RA Macpherson R.E., Vandenboom R., Roy B.D., Peters S.J.;
RT "Skeletal muscle PLIN3 and PLIN5 are serine phosphorylated at rest and
RT following lipolysis during adrenergic or contractile stimulation.";
RL Physiol. Rep. 1:E00084-E00084(2013).
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:0000269|PubMed:21885430, ECO:0000269|PubMed:22127648,
CC ECO:0000269|PubMed:23353597}.
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:0000269|PubMed:23408028, ECO:0000269|PubMed:24303154}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:21885430,
CC ECO:0000269|PubMed:22127648}. Cytoplasm {ECO:0000250|UniProtKB:Q8BVZ1}.
CC Mitochondrion {ECO:0000269|PubMed:21885430,
CC ECO:0000269|PubMed:22127648}. 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. {ECO:0000269|PubMed:24303154}.
CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
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DR EMBL; AABR06058419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474092; EDL83657.1; -; Genomic_DNA.
DR RefSeq; NP_001128109.1; NM_001134637.1.
DR AlphaFoldDB; M0R7Z9; -.
DR SMR; M0R7Z9; -.
DR STRING; 10116.ENSRNOP00000065588; -.
DR iPTMnet; M0R7Z9; -.
DR PhosphoSitePlus; M0R7Z9; -.
DR PaxDb; M0R7Z9; -.
DR PRIDE; M0R7Z9; -.
DR Ensembl; ENSRNOT00000073930; ENSRNOP00000065588; ENSRNOG00000047860.
DR GeneID; 501283; -.
DR KEGG; rno:501283; -.
DR CTD; 440503; -.
DR RGD; 1589602; Plin5.
DR eggNOG; KOG4790; Eukaryota.
DR GeneTree; ENSGT00950000182920; -.
DR HOGENOM; CLU_035133_1_0_1; -.
DR InParanoid; M0R7Z9; -.
DR OMA; ISTDQDQ; -.
DR OrthoDB; 1437332at2759; -.
DR PRO; PR:M0R7Z9; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Proteomes; UP000234681; Chromosome 9.
DR Bgee; ENSRNOG00000047860; Expressed in heart and 10 other tissues.
DR Genevisible; M0R7Z9; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0035473; F:lipase binding; IPI:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; ISS:UniProtKB.
DR GO; GO:0019915; P:lipid storage; ISO:RGD.
DR GO; GO:0051646; P:mitochondrion localization; ISO:RGD.
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:0050995; P:negative regulation of lipid catabolic process; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0060193; P:positive regulation of lipase activity; IDA:UniProtKB.
DR GO; GO:0010884; P:positive regulation of lipid storage; IDA:UniProtKB.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IDA: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 1: Evidence at protein level;
KW Cytoplasm; Lipid droplet; Mitochondrion; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..475
FT /note="Perilipin-5"
FT /id="PRO_0000429266"
FT REGION 1..200
FT /note="Essential for lipid droplet targeting"
FT /evidence="ECO:0000250"
FT REGION 1..123
FT /note="Interaction with LIPE"
FT /evidence="ECO:0000250"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..475
FT /note="Interaction with PNPLA2 and ABHD5"
FT /evidence="ECO:0000250"
FT REGION 447..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..475
FT /note="Recruits mitochondria at the lipid droplet surface"
FT /evidence="ECO:0000250"
FT COMPBIAS 13..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BVZ1"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BVZ1"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00G26"
SQ SEQUENCE 475 AA; 51805 MW; CE68632C467811A9 CRC64;
MDQRGKDTTL ALHSRMSGDQ TAQDPGSSLG ELDQHNVVKR VVALPLVRAT CTAVSGAYNS
AKDRHPLLGS ACRFAEHCVC SVATCALDHA QPLLEHLQPK LATVNDLACR GLDKLEEKLP
FLQQPSDTVV TSAKDAVAKS VTGVVDLAQR GRRWSGELRR SVSQAMDTVL RRSVSQAMDT
VLGKSEELVD HFLPMTEAEL VALATESQGP EVGSVEEQRQ KQGYFVRLGS LSARLRHLAY
QHSLGKLRES KHRTQEMLAQ LQKTLELIQH MQSRASPTPT FHHPKVQELC GDWSPCLENG
YRHSQVELET LALSRSLTLE LQSAVDALAG CVRGLPPSAQ AKVAEVQRSV DALQATFADA
HCLGDVAPTA LAEGQDSVAQ AHACVDEFLD LVLRAMPLAW LVGPFAPILV ERSEPLINLA
TCVDEVVGDP DPRWAHMDWP AQQRAWEAEP ADPGGQEAEP PLGQVKHTMM PELDF
