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 16-SEP-2015, entry version 103. DE RecName: Full=Perilipin-3; DE AltName: Full=Cargo selection protein TIP47; DE AltName: Full=Mannose-6-phosphate receptor-binding protein 1; GN Name=Plin3; Synonyms=M6prbp1, Tip47; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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, RC Pancreas, 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 RT expression."; RL Cell 143:1174-1189(2010). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, AND IDENTIFICATION BY RP MASS 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., RA Zhang Y., 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: Required for the transport of mannose 6-phosphate CC receptors (MPR) from endosomes to the trans-Golgi network. CC {ECO:0000250}. CC -!- SUBUNIT: Homooligomer. Interacts with M6PR (via the cytoplasmic CC domain). Interacts with IGF2R (via the cytoplasmic domain) (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; CC Cytoplasmic side {ECO:0000250}. Lipid droplet {ECO:0000250}. CC Note=Membrane associated on endosomes. Detected in the envelope CC and the core of lipid bodies and in lipid sails (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC33798.1; Type=Frameshift; Positions=400; Evidence={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; 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 UniGene; Mm.311696; -. DR PDB; 1SZI; X-ray; 2.80 A; A=191-437. DR PDBsum; 1SZI; -. DR ProteinModelPortal; Q9DBG5; -. DR SMR; Q9DBG5; 206-431. DR BioGrid; 211801; 1. DR IntAct; Q9DBG5; 2. DR MINT; MINT-1748486; -. DR STRING; 10090.ENSMUSP00000019726; -. DR PhosphoSite; Q9DBG5; -. DR REPRODUCTION-2DPAGE; IPI00319270; -. DR MaxQB; Q9DBG5; -. DR PaxDb; Q9DBG5; -. DR PRIDE; Q9DBG5; -. 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 eggNOG; NOG81115; -. DR GeneTree; ENSGT00500000044795; -. DR HOGENOM; HOG000033816; -. DR HOVERGEN; HBG002935; -. DR InParanoid; Q9DBG5; -. DR OMA; WADNHLP; -. DR OrthoDB; EOG7SN8CD; -. DR PhylomeDB; Q9DBG5; -. DR TreeFam; TF328397; -. DR EvolutionaryTrace; Q9DBG5; -. DR NextBio; 322981; -. DR PRO; PR:Q9DBG5; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; Q9DBG5; -. DR CleanEx; MM_M6PRBP1; -. DR Genevisible; Q9DBG5; MM. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005811; C:lipid particle; ISO:MGI. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR004279; Perilipin. DR PANTHER; PTHR14024; PTHR14024; 1. DR Pfam; PF03036; Perilipin; 1. DR PIRSF; PIRSF036881; PAT; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Coiled coil; Complete proteome; Cytoplasm; KW Endosome; Lipid droplet; Membrane; Phosphoprotein; Reference proteome; KW Transport. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O60664}. FT CHAIN 2 437 Perilipin-3. FT /FTId=PRO_0000099891. FT COILED 251 284 {ECO:0000255}. FT COILED 357 410 {ECO:0000255}. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000250|UniProtKB:O60664}. FT MOD_RES 65 65 N6-acetyllysine. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 130 130 Phosphoserine. FT {ECO:0000250|UniProtKB:O60664}. FT MOD_RES 174 174 Phosphothreonine. FT {ECO:0000250|UniProtKB:O60664}. FT MOD_RES 179 179 Phosphoserine. FT {ECO:0000250|UniProtKB:O60664}. FT MOD_RES 183 183 Phosphoserine. FT {ECO:0000250|UniProtKB:O60664}. FT STRAND 207 210 {ECO:0000244|PDB:1SZI}. FT HELIX 212 216 {ECO:0000244|PDB:1SZI}. FT HELIX 227 235 {ECO:0000244|PDB:1SZI}. FT STRAND 239 242 {ECO:0000244|PDB:1SZI}. FT HELIX 243 245 {ECO:0000244|PDB:1SZI}. FT HELIX 248 287 {ECO:0000244|PDB:1SZI}. FT HELIX 324 350 {ECO:0000244|PDB:1SZI}. FT TURN 351 354 {ECO:0000244|PDB:1SZI}. FT HELIX 357 376 {ECO:0000244|PDB:1SZI}. FT HELIX 377 379 {ECO:0000244|PDB:1SZI}. FT HELIX 383 385 {ECO:0000244|PDB:1SZI}. FT HELIX 388 413 {ECO:0000244|PDB:1SZI}. FT STRAND 421 427 {ECO:0000244|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 //