ID PLIN3_HUMAN Reviewed; 434 AA. AC O60664; A8K4Y9; K7EQF4; Q53G77; Q9BS03; Q9UBD7; Q9UP92; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 27-MAR-2024, entry version 205. DE RecName: Full=Perilipin-3; DE AltName: Full=47 kDa mannose 6-phosphate receptor-binding protein {ECO:0000303|PubMed:9590177}; DE Short=47 kDa MPR-binding protein {ECO:0000303|PubMed:9590177}; DE AltName: Full=Cargo selection protein TIP47 {ECO:0000303|PubMed:9590177}; DE AltName: Full=Mannose-6-phosphate receptor-binding protein 1; DE AltName: Full=Placental protein 17 {ECO:0000303|PubMed:9874244}; DE Short=PP17 {ECO:0000303|PubMed:9874244}; GN Name=PLIN3; Synonyms=M6PRBP1, TIP47 {ECO:0000303|PubMed:9590177}; 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] (ISOFORM 1), VARIANTS VAL-56 AND ALA-275, RP FUNCTION, INTERACTION WITH M6PR AND IGF2R, HOMOOLIGOMERIZATION, AND RP SUBCELLULAR LOCATION. RX PubMed=9590177; DOI=10.1016/s0092-8674(00)81171-x; RA Diaz E., Pfeffer S.R.; RT "TIP47: a cargo selection device for mannose 6-phosphate receptor RT trafficking."; RL Cell 93:433-443(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS VAL-56 AND RP ALA-275. RC TISSUE=Placenta; RX PubMed=9874244; DOI=10.1046/j.1432-1327.1998.2580752.x; RA Than N.G., Sumegi B., Than G.N., Kispal G., Bohn H.; RT "Cloning and sequence analysis of cDNAs encoding human placental tissue RT protein 17 (PP17) variants."; RL Eur. J. Biochem. 258:752-757(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBUNIT (ISOFORM 2), AND RP VARIANTS VAL-56 AND ALA-275. RC TISSUE=Placenta; RX PubMed=10393528; DOI=10.1159/000030062; RA Than N.G., Sumegi B., Than G.N., Kispal G., Bohn H.; RT "Cloning and sequencing of human oncodevelopmental soluble placental tissue RT protein 17 (PP17): homology with adipophilin and the mouse adipose RT differentiation-related protein."; RL Tumor Biol. 20:184-192(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-275. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-275. 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ALA-275. RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-56 AND RP ALA-275. RC TISSUE=Colon, and Muscle; 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 [9] RP CHARACTERIZATION. RC TISSUE=Placenta; RX PubMed=6856484; RA Bohn H., Kraus W., Winckler W.; RT "Purification and characterization of two new soluble placental tissue RT proteins (PP13 and PP17)."; RL Oncodev. Biol. Med. 4:343-350(1983). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=15545278; DOI=10.1074/jbc.m407194200; RA Robenek H., Lorkowski S., Schnoor M., Troyer D.; RT "Spatial integration of TIP47 and adipophilin in macrophage lipid bodies."; RL J. Biol. Chem. 280:5789-5794(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; THR-170; SER-175 AND RP SER-179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-91; SER-130; SER-148; RP THR-216; SER-217 AND SER-241, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP IDENTIFICATION BY 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). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=26357594; DOI=10.7717/peerj.1213; RA Chughtai A.A., Kassak F., Kostrouchova M., Novotny J.P., Krause M.W., RA Saudek V., Kostrouch Z., Kostrouchova M.; RT "Perilipin-related protein regulates lipid metabolism in C. elegans."; RL PeerJ 3:E1213-E1213(2015). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [23] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-251, AND MUTAGENESIS RP OF TYR-251. RX PubMed=34077757; DOI=10.1016/j.molcel.2021.05.005; RA Liu R., Lee J.H., Li J., Yu R., Tan L., Xia Y., Zheng Y., Bian X.L., RA Lorenzi P.L., Chen Q., Lu Z.; RT "Choline kinase alpha 2 acts as a protein kinase to promote lipolysis of RT lipid droplets."; RL Mol. Cell 81:2722-2735(2021). CC -!- FUNCTION: Structural component of lipid droplets, which is required for CC the formation and maintenance of lipid storage droplets CC (PubMed:34077757). Required for the transport of mannose 6-phosphate CC receptors (MPR) from endosomes to the trans-Golgi network CC (PubMed:9590177). {ECO:0000269|PubMed:34077757, CC ECO:0000269|PubMed:9590177}. CC -!- SUBUNIT: Homooligomer (PubMed:9590177). Interacts with M6PR (via the CC cytoplasmic domain) (PubMed:9590177). Interacts with IGF2R (via the CC cytoplasmic domain) (PubMed:9590177). {ECO:0000269|PubMed:9590177}. CC -!- SUBUNIT: [Isoform 2]: May exist as a homodimer. CC {ECO:0000269|PubMed:9874244}. CC -!- INTERACTION: CC O60664; Q8TB40: ABHD4; NbExp=3; IntAct=EBI-725795, EBI-7131019; CC O60664; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-725795, EBI-2813554; CC O60664; P55212: CASP6; NbExp=3; IntAct=EBI-725795, EBI-718729; CC O60664; P24863: CCNC; NbExp=3; IntAct=EBI-725795, EBI-395261; CC O60664; Q9H444: CHMP4B; NbExp=3; IntAct=EBI-725795, EBI-749627; CC O60664; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-725795, EBI-2548702; CC O60664; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-725795, EBI-11522780; CC O60664; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-725795, EBI-2680384; CC O60664; Q05329: GAD2; NbExp=3; IntAct=EBI-725795, EBI-9304251; CC O60664; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-725795, EBI-18053395; CC O60664; P13473-2: LAMP2; NbExp=3; IntAct=EBI-725795, EBI-21591415; CC O60664; Q9C0E8-2: LNPK; NbExp=3; IntAct=EBI-725795, EBI-11024283; CC O60664; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-725795, EBI-740987; CC O60664; Q9HB07: MYG1; NbExp=3; IntAct=EBI-725795, EBI-709754; CC O60664; Q96AL5: PBX3; NbExp=3; IntAct=EBI-725795, EBI-741171; CC O60664; Q9Y6X2: PIAS3; NbExp=3; IntAct=EBI-725795, EBI-2803703; CC O60664; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-725795, EBI-5280197; CC O60664; P43378: PTPN9; NbExp=3; IntAct=EBI-725795, EBI-742898; CC O60664; O95562: SFT2D2; NbExp=3; IntAct=EBI-725795, EBI-4402330; CC O60664; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-725795, EBI-2623095; CC O60664; Q13596: SNX1; NbExp=4; IntAct=EBI-725795, EBI-2822329; CC O60664; O60749: SNX2; NbExp=3; IntAct=EBI-725795, EBI-1046690; CC O60664; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-725795, EBI-12187159; CC O60664; O43761: SYNGR3; NbExp=3; IntAct=EBI-725795, EBI-11321949; CC O60664; P08247: SYP; NbExp=3; IntAct=EBI-725795, EBI-9071725; CC O60664; Q9BW92: TARS2; NbExp=3; IntAct=EBI-725795, EBI-1045099; CC O60664; Q9NVG8: TBC1D13; NbExp=3; IntAct=EBI-725795, EBI-12264956; CC O60664; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-725795, EBI-2339195; CC O60664; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=5; IntAct=EBI-725795, EBI-6863748; CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:15545278, CC ECO:0000269|PubMed:34077757}. Endosome membrane CC {ECO:0000269|PubMed:15545278}; Peripheral membrane protein CC {ECO:0000269|PubMed:15545278}; Cytoplasmic side CC {ECO:0000269|PubMed:15545278}. Cytoplasm {ECO:0000269|PubMed:15545278, CC ECO:0000269|PubMed:26357594, ECO:0000269|PubMed:9590177}. Note=Membrane CC associated on endosomes (PubMed:15545278). Detected in the envelope and CC the core of lipid bodies and in lipid sails (PubMed:15545278). CC {ECO:0000269|PubMed:15545278}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=PP17b {ECO:0000303|PubMed:9874244}; CC IsoId=O60664-1; Sequence=Displayed; CC Name=2; Synonyms=PP17a {ECO:0000303|PubMed:9874244}; CC IsoId=O60664-2; Sequence=VSP_004664; CC Name=3; CC IsoId=O60664-3; Sequence=VSP_040325; CC Name=4; CC IsoId=O60664-4; Sequence=VSP_047038; CC -!- PTM: Phosphorylation at Tyr-251 by isoform 1 of CHKA (CHKalpha2) CC promotes dissociation from lipid droplets: dissociation is followed by CC recruitment of autophagosome machinery to lipid droplets and subsequent CC lipid droplet lipolysis. {ECO:0000269|PubMed:34077757}. CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF057140; AAC39751.1; -; mRNA. DR EMBL; AF055574; AAD11622.1; -; mRNA. DR EMBL; AF051314; AAD11619.1; -; mRNA. DR EMBL; AF051315; AAD11620.1; -; mRNA. DR EMBL; BT007235; AAP35899.1; -; mRNA. DR EMBL; AK291104; BAF83793.1; -; mRNA. DR EMBL; AK223054; BAD96774.1; -; mRNA. DR EMBL; AK225045; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC027319; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001590; AAH01590.1; -; mRNA. DR EMBL; BC005818; AAH05818.1; -; mRNA. DR EMBL; BC007566; AAH07566.1; -; mRNA. DR EMBL; BC019278; AAH19278.1; -; mRNA. DR CCDS; CCDS12137.1; -. [O60664-1] DR CCDS; CCDS59337.1; -. [O60664-4] DR CCDS; CCDS59338.1; -. [O60664-3] DR RefSeq; NP_001157661.1; NM_001164189.1. [O60664-3] DR RefSeq; NP_001157666.1; NM_001164194.1. [O60664-4] DR RefSeq; NP_005808.3; NM_005817.4. [O60664-1] DR AlphaFoldDB; O60664; -. DR SMR; O60664; -. DR BioGRID; 115520; 131. DR CORUM; O60664; -. DR IntAct; O60664; 53. DR MINT; O60664; -. DR STRING; 9606.ENSP00000221957; -. DR ChEMBL; CHEMBL4523145; -. DR DrugBank; DB01279; Galsulfase. DR DrugBank; DB01271; Idursulfase. DR GlyCosmos; O60664; 3 sites, 1 glycan. DR GlyGen; O60664; 8 sites, 1 O-linked glycan (8 sites). DR iPTMnet; O60664; -. DR MetOSite; O60664; -. DR PhosphoSitePlus; O60664; -. DR SwissPalm; O60664; -. DR BioMuta; PLIN3; -. DR REPRODUCTION-2DPAGE; IPI00303882; -. DR CPTAC; CPTAC-111; -. DR CPTAC; CPTAC-112; -. DR EPD; O60664; -. DR jPOST; O60664; -. DR MassIVE; O60664; -. DR MaxQB; O60664; -. DR PaxDb; 9606-ENSP00000221957; -. DR PeptideAtlas; O60664; -. DR PRIDE; O60664; -. DR ProteomicsDB; 49508; -. [O60664-1] DR ProteomicsDB; 49509; -. [O60664-2] DR ProteomicsDB; 49510; -. [O60664-3] DR Pumba; O60664; -. DR TopDownProteomics; O60664-1; -. [O60664-1] DR TopDownProteomics; O60664-2; -. [O60664-2] DR TopDownProteomics; O60664-3; -. [O60664-3] DR Antibodypedia; 1639; 682 antibodies from 39 providers. DR DNASU; 10226; -. DR Ensembl; ENST00000221957.9; ENSP00000221957.3; ENSG00000105355.9. [O60664-1] DR Ensembl; ENST00000585479.5; ENSP00000465596.1; ENSG00000105355.9. [O60664-3] DR Ensembl; ENST00000592528.5; ENSP00000467803.1; ENSG00000105355.9. [O60664-4] DR GeneID; 10226; -. DR KEGG; hsa:10226; -. DR MANE-Select; ENST00000221957.9; ENSP00000221957.3; NM_005817.5; NP_005808.3. DR UCSC; uc002mbj.3; human. [O60664-1] DR AGR; HGNC:16893; -. DR CTD; 10226; -. DR DisGeNET; 10226; -. DR GeneCards; PLIN3; -. DR HGNC; HGNC:16893; PLIN3. DR HPA; ENSG00000105355; Low tissue specificity. DR MIM; 602702; gene. DR neXtProt; NX_O60664; -. DR OpenTargets; ENSG00000105355; -. DR PharmGKB; PA165394001; -. DR VEuPathDB; HostDB:ENSG00000105355; -. DR eggNOG; ENOG502R7TG; Eukaryota. DR GeneTree; ENSGT00950000182920; -. DR HOGENOM; CLU_035133_0_1_1; -. DR InParanoid; O60664; -. DR OMA; STVMSTR; -. DR OrthoDB; 3026676at2759; -. DR PhylomeDB; O60664; -. DR TreeFam; TF328397; -. DR PathwayCommons; O60664; -. DR Reactome; R-HSA-163560; Triglyceride catabolism. DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network. DR Reactome; R-HSA-9613354; Lipophagy. DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy. DR Reactome; R-HSA-9615710; Late endosomal microautophagy. DR Reactome; R-HSA-9706019; RHOBTB3 ATPase cycle. DR SignaLink; O60664; -. DR SIGNOR; O60664; -. DR BioGRID-ORCS; 10226; 12 hits in 1169 CRISPR screens. DR ChiTaRS; PLIN3; human. DR GeneWiki; M6PRBP1; -. DR GenomeRNAi; 10226; -. DR Pharos; O60664; Tbio. DR PRO; PR:O60664; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; O60664; Protein. DR Bgee; ENSG00000105355; Expressed in pharyngeal mucosa and 206 other cell types or tissues. DR ExpressionAtlas; O60664; baseline and differential. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005768; C:endosome; TAS:ProtInc. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0005811; C:lipid droplet; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0030133; C:transport vesicle; TAS:Reactome. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB. DR GO; GO:1905691; P:lipid droplet disassembly; IDA:UniProtKB. DR GO; GO:0019915; P:lipid storage; IDA:UniProtKB. DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IBA:GO_Central. DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc. 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:SF11; PERILIPIN-3; 1. DR Pfam; PF03036; Perilipin; 1. DR PIRSF; PIRSF036881; PAT; 1. DR SUPFAM; SSF109775; Mannose-6-phosphate receptor binding protein 1 (Tip47), C-terminal domain; 1. DR Genevisible; O60664; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Endosome; KW Isopeptide bond; Lipid droplet; Membrane; Phosphoprotein; KW Reference proteome; Transport; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..434 FT /note="Perilipin-3" FT /id="PRO_0000099890" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 252..277 FT /evidence="ECO:0000255" FT COILED 353..377 FT /evidence="ECO:0000255" FT COMPBIAS 1..20 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 65 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 91 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 130 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 148 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 170 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 175 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 179 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 216 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 217 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 251 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:34077757" FT CROSSLNK 122 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0007744|PubMed:25114211" FT VAR_SEQ 1..183 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10393528, FT ECO:0000303|PubMed:9874244" FT /id="VSP_004664" FT VAR_SEQ 116..127 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_047038" FT VAR_SEQ 321 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_040325" FT VARIANT 56 FT /note="I -> V (in dbSNP:rs8289)" FT /evidence="ECO:0000269|PubMed:10393528, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9590177, FT ECO:0000269|PubMed:9874244" FT /id="VAR_022780" FT VARIANT 275 FT /note="V -> A (in dbSNP:rs9973235)" FT /evidence="ECO:0000269|PubMed:10393528, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9590177, ECO:0000269|PubMed:9874244, FT ECO:0000269|Ref.4, ECO:0000269|Ref.6" FT /id="VAR_024559" FT MUTAGEN 251 FT /note="Y->F: Abolished phosphorylation at Tyr-232 by FT isoform 1 of CHKA (CHKalpha2)." FT /evidence="ECO:0000269|PubMed:34077757" FT CONFLICT 77 FT /note="G -> W (in Ref. 2; AAD11622)" FT /evidence="ECO:0000305" FT CONFLICT 109..111 FT /note="ILQ -> MLR (in Ref. 2; AAD11622)" FT /evidence="ECO:0000305" SQ SEQUENCE 434 AA; 47075 MW; 67B2B9CDBC523043 CRC64; MSADGAEADG STQVTVEEPV QQPSVVDRVA SMPLISSTCD MVSAAYASTK ESYPHIKTVC DAAEKGVRTL TAAAVSGAQP ILSKLEPQIA SASEYAHRGL DKLEENLPIL QQPTEKVLAD TKELVSSKVS GAQEMVSSAK DTVATQLSEA VDATRGAVQS GVDKTKSVVT GGVQSVMGSR LGQMVLSGVD TVLGKSEEWA DNHLPLTDAE LARIATSLDG FDVASVQQQR QEQSYFVRLG SLSERLRQHA YEHSLGKLRA TKQRAQEALL QLSQVLSLME TVKQGVDQKL VEGQEKLHQM WLSWNQKQLQ GPEKEPPKPE QVESRALTMF RDIAQQLQAT CTSLGSSIQG LPTNVKDQVQ QARRQVEDLQ ATFSSIHSFQ DLSSSILAQS RERVASAREA LDHMVEYVAQ NTPVTWLVGP FAPGITEKAP EEKK //