PLIN3_HUMAN
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 03-AUG-2022, entry version 196.
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}.
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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; 116.
DR CORUM; O60664; -.
DR IntAct; O60664; 52.
DR MINT; O60664; -.
DR STRING; 9606.ENSP00000221957; -.
DR ChEMBL; CHEMBL4523145; -.
DR DrugBank; DB01279; Galsulfase.
DR DrugBank; DB01271; Idursulfase.
DR GlyGen; O60664; 3 sites, 1 O-linked glycan (3 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; O60664; -.
DR PeptideAtlas; O60664; -.
DR PRIDE; O60664; -.
DR ProteomicsDB; 49508; -. [O60664-1]
DR ProteomicsDB; 49509; -. [O60664-2]
DR ProteomicsDB; 49510; -. [O60664-3]
DR TopDownProteomics; O60664-1; -. [O60664-1]
DR TopDownProteomics; O60664-2; -. [O60664-2]
DR TopDownProteomics; O60664-3; -. [O60664-3]
DR Antibodypedia; 1639; 599 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 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; 1437332at2759; -.
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 1082 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 204 other tissues.
DR ExpressionAtlas; O60664; baseline and differential.
DR Genevisible; O60664; HS.
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:UniProtKB.
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 InterPro; IPR004279; Perilipin.
DR Pfam; PF03036; Perilipin; 1.
DR PIRSF; PIRSF036881; PAT; 1.
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
