PLIN5_HUMAN
ID PLIN5_HUMAN Reviewed; 463 AA.
AC Q00G26; A2RRC1; Q6ZS68;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Perilipin-5;
DE AltName: Full=Lipid storage droplet protein 5;
GN Name=PLIN5; Synonyms=LSDP5, OXPAT, PAT-1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND VARIANTS ARG-255 AND TRP-306.
RC TISSUE=Heart;
RX PubMed=17234449; DOI=10.1016/j.bbalip.2006.11.011;
RA Dalen K.T., Dahl T., Holter E., Arntsen B., Londos C., Sztalryd C.,
RA Nebb H.I.;
RT "LSDP5 is a PAT protein specifically expressed in fatty acid oxidizing
RT tissues.";
RL Biochim. Biophys. Acta 1771:210-227(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-255.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-114.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP INDUCTION.
RX PubMed=23129790; DOI=10.1113/jphysiol.2012.240952;
RA Shepherd S.O., Cocks M., Tipton K.D., Ranasinghe A.M., Barker T.A.,
RA Burniston J.G., Wagenmakers A.J., Shaw C.S.;
RT "Sprint interval and traditional endurance training increase net
RT intramuscular triglyceride breakdown and expression of perilipin 2 and 5.";
RL J. Physiol. (Lond.) 591:657-675(2013).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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, ECO:0000269|PubMed:17234449}.
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 -!- INTERACTION:
CC Q00G26; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-21732470, EBI-2813554;
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:17234449}.
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 -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, liver, heart and
CC kidney. {ECO:0000269|PubMed:17234449}.
CC -!- INDUCTION: Increased by endurance and sprint interval training.
CC {ECO:0000269|PubMed:23129790}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC87086.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; DQ839131; ABH07519.1; -; mRNA.
DR EMBL; AC011498; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC131524; AAI31525.1; -; mRNA.
DR EMBL; AK127689; BAC87086.1; ALT_SEQ; mRNA.
DR CCDS; CCDS42473.1; -.
DR RefSeq; NP_001013728.2; NM_001013706.2.
DR AlphaFoldDB; Q00G26; -.
DR SMR; Q00G26; -.
DR BioGRID; 136635; 13.
DR IntAct; Q00G26; 7.
DR STRING; 9606.ENSP00000371272; -.
DR BindingDB; Q00G26; -.
DR iPTMnet; Q00G26; -.
DR PhosphoSitePlus; Q00G26; -.
DR BioMuta; PLIN5; -.
DR DMDM; 292495026; -.
DR jPOST; Q00G26; -.
DR MassIVE; Q00G26; -.
DR PaxDb; Q00G26; -.
DR PeptideAtlas; Q00G26; -.
DR PRIDE; Q00G26; -.
DR ProteomicsDB; 57901; -.
DR Antibodypedia; 23670; 174 antibodies from 15 providers.
DR DNASU; 440503; -.
DR Ensembl; ENST00000381848.7; ENSP00000371272.2; ENSG00000214456.8.
DR GeneID; 440503; -.
DR KEGG; hsa:440503; -.
DR MANE-Select; ENST00000381848.7; ENSP00000371272.2; NM_001013706.3; NP_001013728.2.
DR UCSC; uc002mas.5; human.
DR CTD; 440503; -.
DR DisGeNET; 440503; -.
DR GeneCards; PLIN5; -.
DR HGNC; HGNC:33196; PLIN5.
DR HPA; ENSG00000214456; Tissue enhanced (liver, pancreas, skeletal muscle).
DR MIM; 613248; gene.
DR neXtProt; NX_Q00G26; -.
DR OpenTargets; ENSG00000214456; -.
DR PharmGKB; PA165394043; -.
DR VEuPathDB; HostDB:ENSG00000214456; -.
DR eggNOG; KOG4790; Eukaryota.
DR GeneTree; ENSGT00950000182920; -.
DR HOGENOM; CLU_035133_1_0_1; -.
DR InParanoid; Q00G26; -.
DR OMA; ISTDQDQ; -.
DR OrthoDB; 1437332at2759; -.
DR PhylomeDB; Q00G26; -.
DR TreeFam; TF328397; -.
DR PathwayCommons; Q00G26; -.
DR SignaLink; Q00G26; -.
DR BioGRID-ORCS; 440503; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; PLIN5; human.
DR GenomeRNAi; 440503; -.
DR Pharos; Q00G26; Tbio.
DR PRO; PR:Q00G26; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q00G26; protein.
DR Bgee; ENSG00000214456; Expressed in right lobe of liver and 169 other tissues.
DR ExpressionAtlas; Q00G26; baseline and differential.
DR Genevisible; Q00G26; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005811; C:lipid droplet; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0035473; F:lipase binding; IEA:Ensembl.
DR GO; GO:0034389; P:lipid droplet organization; ISS:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR GO; GO:0051646; P:mitochondrion localization; IEA:Ensembl.
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 1: Evidence at protein level;
KW Cytoplasm; Lipid droplet; Mitochondrion; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..463
FT /note="Perilipin-5"
FT /id="PRO_0000338982"
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 185..463
FT /note="Interaction with PNPLA2 and ABHD5"
FT /evidence="ECO:0000250"
FT REGION 444..463
FT /note="Recruits mitochondria at the lipid droplet surface"
FT /evidence="ECO:0000250"
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 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 6
FT /note="A -> V (in dbSNP:rs10407239)"
FT /id="VAR_043850"
FT VARIANT 255
FT /note="C -> R (in dbSNP:rs1610090)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17234449"
FT /id="VAR_043851"
FT VARIANT 306
FT /note="R -> W (in dbSNP:rs1062223)"
FT /evidence="ECO:0000269|PubMed:17234449"
FT /id="VAR_043852"
SQ SEQUENCE 463 AA; 50791 MW; B9747E905DFB56E2 CRC64;
MSEEEAAQIP RSSVWEQDQQ NVVQRVVALP LVRATCTAVC DVYSAAKDRH PLLGSACRLA
ENCVCGLTTR ALDHAQPLLE HLQPQLATMN SLACRGLDKL EEKLPFLQQP SETVVTSAKD
VVASSVTGVV DLARRGRRWS VELKRSVSHA VDVVLEKSEE LVDHFLPMTE EELAALAAEA
EGPEVGSVED QRRQQGYFVR LGSLSARIRH LAYEHSVGKL RQSKHRAQDT LAQLQETLEL
IDHMQCGVTP TAPACPGKVH ELWGEWGQRP PESRRRSQAE LETLVLSRSL TQELQGTVEA
LESSVRGLPA GAQEKVAEVR RSVDALQTAF ADARCFRDVP AAALAEGRGR VAHAHACVDE
LLELVVQAVP LPWLVGPFAP ILVERPEPLP DLADLVDEVI GGPDPRWAHL DWPAQQRAWE
AEHRDGSGNG DGDRMGVAGD ICEQEPETPS CPVKHTLMPE LDF
