PLIN3_MOUSE
ID PLIN3_MOUSE Reviewed; 437 AA.
AC Q9DBG5; Q3TK05; Q8BKV9; Q9CZK1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Perilipin-3;
DE AltName: Full=Cargo selection protein TIP47 {ECO:0000303|PubMed:15242596};
DE AltName: Full=Mannose-6-phosphate receptor-binding protein 1;
GN Name=Plin3; Synonyms=M6prbp1, Tip47 {ECO:0000303|PubMed:15242596};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 191-437.
RX PubMed=15242596; DOI=10.1016/j.str.2004.04.021;
RA Hickenbottom S.J., Kimmel A.R., Londos C., Hurley J.H.;
RT "Structure of a lipid droplet protein; the PAT family member TIP47.";
RL Structure 12:1199-1207(2004).
CC -!- FUNCTION: Structural component of lipid droplets, which is required for
CC the formation and maintenance of lipid storage droplets. Required for
CC the transport of mannose 6-phosphate receptors (MPR) from endosomes to
CC the trans-Golgi network. {ECO:0000250|UniProtKB:O60664}.
CC -!- SUBUNIT: Homooligomer. Interacts with M6PR (via the cytoplasmic
CC domain). Interacts with IGF2R (via the cytoplasmic domain).
CC {ECO:0000250|UniProtKB:O60664}.
CC -!- INTERACTION:
CC Q9DBG5; P63017: Hspa8; NbExp=2; IntAct=EBI-643495, EBI-433443;
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:O60664}.
CC Endosome membrane {ECO:0000250|UniProtKB:O60664}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:O60664}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O60664}. Cytoplasm
CC {ECO:0000250|UniProtKB:O60664}. Note=Membrane associated on endosomes.
CC Detected in the envelope and the core of lipid bodies and in lipid
CC sails. {ECO:0000250|UniProtKB:O60664}.
CC -!- PTM: Phosphorylation at Tyr-255 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:0000250|UniProtKB:O60664}.
CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33798.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK004970; BAB23708.1; -; mRNA.
DR EMBL; AK012517; BAB28291.1; -; mRNA.
DR EMBL; AK049537; BAC33798.1; ALT_FRAME; mRNA.
DR EMBL; AK050140; BAC34089.1; -; mRNA.
DR EMBL; AK132313; BAE21098.1; -; mRNA.
DR EMBL; AK167214; BAE39340.1; -; mRNA.
DR EMBL; BC011116; AAH11116.1; -; mRNA.
DR CCDS; CCDS28901.1; -.
DR RefSeq; NP_080112.1; NM_025836.3.
DR PDB; 1SZI; X-ray; 2.80 A; A=191-437.
DR PDBsum; 1SZI; -.
DR AlphaFoldDB; Q9DBG5; -.
DR SMR; Q9DBG5; -.
DR BioGRID; 211801; 3.
DR DIP; DIP-49514N; -.
DR IntAct; Q9DBG5; 2.
DR STRING; 10090.ENSMUSP00000019726; -.
DR iPTMnet; Q9DBG5; -.
DR PhosphoSitePlus; Q9DBG5; -.
DR REPRODUCTION-2DPAGE; IPI00319270; -.
DR CPTAC; non-CPTAC-3862; -.
DR EPD; Q9DBG5; -.
DR jPOST; Q9DBG5; -.
DR MaxQB; Q9DBG5; -.
DR PaxDb; Q9DBG5; -.
DR PeptideAtlas; Q9DBG5; -.
DR PRIDE; Q9DBG5; -.
DR ProteomicsDB; 289931; -.
DR Antibodypedia; 1639; 599 antibodies from 39 providers.
DR DNASU; 66905; -.
DR Ensembl; ENSMUST00000019726; ENSMUSP00000019726; ENSMUSG00000024197.
DR GeneID; 66905; -.
DR KEGG; mmu:66905; -.
DR UCSC; uc008dbn.1; mouse.
DR CTD; 10226; -.
DR MGI; MGI:1914155; Plin3.
DR VEuPathDB; HostDB:ENSMUSG00000024197; -.
DR eggNOG; ENOG502R7TG; Eukaryota.
DR GeneTree; ENSGT00950000182920; -.
DR HOGENOM; CLU_035133_0_1_1; -.
DR InParanoid; Q9DBG5; -.
DR OMA; STVMSTR; -.
DR OrthoDB; 1437332at2759; -.
DR PhylomeDB; Q9DBG5; -.
DR TreeFam; TF328397; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-MMU-9706019; RHOBTB3 ATPase cycle.
DR BioGRID-ORCS; 66905; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Plin3; mouse.
DR EvolutionaryTrace; Q9DBG5; -.
DR PRO; PR:Q9DBG5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9DBG5; protein.
DR Bgee; ENSMUSG00000024197; Expressed in epithelium of small intestine and 232 other tissues.
DR ExpressionAtlas; Q9DBG5; baseline and differential.
DR Genevisible; Q9DBG5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:1905691; P:lipid droplet disassembly; ISS:UniProtKB.
DR GO; GO:0019915; P:lipid storage; ISS:UniProtKB.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IBA:GO_Central.
DR DisProt; DP02683; -.
DR InterPro; IPR004279; Perilipin.
DR Pfam; PF03036; Perilipin; 1.
DR PIRSF; PIRSF036881; PAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; 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:0000250|UniProtKB:O60664"
FT CHAIN 2..437
FT /note="Perilipin-3"
FT /id="PRO_0000099891"
FT COILED 251..284
FT /evidence="ECO:0000255"
FT COILED 357..410
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 65
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 255
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1SZI"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:1SZI"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:1SZI"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1SZI"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1SZI"
FT HELIX 248..287
FT /evidence="ECO:0007829|PDB:1SZI"
FT HELIX 324..350
FT /evidence="ECO:0007829|PDB:1SZI"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:1SZI"
FT HELIX 357..376
FT /evidence="ECO:0007829|PDB:1SZI"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:1SZI"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:1SZI"
FT HELIX 388..413
FT /evidence="ECO:0007829|PDB:1SZI"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:1SZI"
SQ SEQUENCE 437 AA; 47262 MW; F7CDD3A754A5C04D CRC64;
MSSNGTDAPA EAQAAMEEPV VQPSVVDRVA GLPLISSTYG MVSAAYTSTK ENYPHVRTVC
DVAEKGVKTL TTAAVSTAQP ILSKLEPQIA TASEYAHRGL DRLQESLPIL QQPTEKVLAD
TKELVSSTVS GAQEMVSSSV SSAKETVATR VTGAVDVTLG AVQNSVDKTK SAMTSGVQSV
MGSRVGQMVI SGVDRVLVKS EAWADNRLPL TEAELALIAT PPEDSDMASL QQQRQEQNYF
VRLGSLSERL RNHAYEHSLG KLQNARQKAQ ETLQQLTSVL GLMESVKQGV DQRLGEGQEK
LHQMWLSWNQ KTPQDAEKDP AKPEQVEARA LSMFRDITQQ LQSMCVALGA SIQGLPSHVR
EQAQQARSQV NDLQATFSGI HSFQDLSAGV LAQTRERIAR AREALDNTVE YVAQNTPAMW
LVGPFAPGIT EKTPEGK
