PLIN2_MOUSE
ID PLIN2_MOUSE Reviewed; 425 AA.
AC P43883; Q8K3Q8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Perilipin-2;
DE AltName: Full=Adipophilin {ECO:0000303|PubMed:12562852};
DE AltName: Full=Adipose differentiation-related protein {ECO:0000303|PubMed:1518805, ECO:0000303|PubMed:9392423};
DE Short=ADRP {ECO:0000303|PubMed:9392423};
GN Name=Plin2; Synonyms=Adfp, Adrp {ECO:0000303|PubMed:9392423};
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 [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC TISSUE=Adipocyte;
RX PubMed=1518805; DOI=10.1073/pnas.89.17.7856;
RA Jiang H.P., Serrero G.;
RT "Isolation and characterization of a full-length cDNA coding for an adipose
RT differentiation-related protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7856-7860(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C3H/HeJ; TISSUE=Adipose tissue;
RX PubMed=8325636; DOI=10.1006/geno.1993.1241;
RA Eisinger D.P., Serrero G.;
RT "Structure of the gene encoding mouse adipose differentiation-related
RT protein (ADRP).";
RL Genomics 16:638-644(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11978849; DOI=10.1523/jneurosci.22-09-03730.2002;
RA Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.;
RT "Congenic mapping of alcohol and pentobarbital withdrawal liability loci to
RT a <1 centimorgan interval of murine chromosome 4: identification of Mpdz as
RT a candidate gene.";
RL J. Neurosci. 22:3730-3738(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9392423;
RA Brasaemle D.L., Barber T., Wolins N.E., Serrero G., Blanchette-Mackie E.J.,
RA Londos C.;
RT "Adipose differentiation-related protein is an ubiquitously expressed lipid
RT storage droplet-associated protein.";
RL J. Lipid Res. 38:2249-2263(1997).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12562852; DOI=10.1194/jlr.c200021-jlr200;
RA McManaman J.L., Zabaronick W., Schaack J., Orlicky D.J.;
RT "Lipid droplet targeting domains of adipophilin.";
RL J. Lipid Res. 44:668-673(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, and Lung;
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).
CC -!- FUNCTION: Structural component of lipid droplets, which is required for
CC the formation and maintenance of lipid storage droplets.
CC {ECO:0000269|PubMed:12562852, ECO:0000305|PubMed:1518805}.
CC -!- INTERACTION:
CC P43883; P63017: Hspa8; NbExp=3; IntAct=EBI-16156700, EBI-433443;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:1518805}; Peripheral
CC membrane protein {ECO:0000305|PubMed:1518805}. Lipid droplet
CC {ECO:0000269|PubMed:12562852, ECO:0000269|PubMed:9392423}.
CC -!- TISSUE SPECIFICITY: Adipose tissue specific. Expressed abundantly and
CC preferentially in fat pads. {ECO:0000269|PubMed:1518805}.
CC -!- INDUCTION: By dexamethasone. {ECO:0000269|PubMed:1518805}.
CC -!- PTM: Acylated; primarily with C14, C16 and C18 fatty acids.
CC {ECO:0000250|UniProtKB:Q99541}.
CC -!- PTM: Phosphorylation at Tyr-230 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:Q99541}.
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; M93275; AAA37176.1; -; mRNA.
DR EMBL; L09734; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; AY035850; AAK63075.1; -; mRNA.
DR EMBL; AK150177; BAE29361.1; -; mRNA.
DR EMBL; AK152081; BAE30931.1; -; mRNA.
DR EMBL; AK152263; BAE31081.1; -; mRNA.
DR EMBL; AK153222; BAE31815.1; -; mRNA.
DR EMBL; AK154582; BAE32690.1; -; mRNA.
DR EMBL; AK167140; BAE39285.1; -; mRNA.
DR EMBL; AL824707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054766; AAH54766.1; -; mRNA.
DR CCDS; CCDS18308.1; -.
DR PIR; A46251; A46251.
DR RefSeq; NP_031434.3; NM_007408.3.
DR RefSeq; XP_006537620.1; XM_006537557.1.
DR AlphaFoldDB; P43883; -.
DR SMR; P43883; -.
DR BioGRID; 197983; 1.
DR DIP; DIP-61639N; -.
DR IntAct; P43883; 1.
DR STRING; 10090.ENSMUSP00000000466; -.
DR iPTMnet; P43883; -.
DR PhosphoSitePlus; P43883; -.
DR SwissPalm; P43883; -.
DR EPD; P43883; -.
DR MaxQB; P43883; -.
DR PaxDb; P43883; -.
DR PeptideAtlas; P43883; -.
DR PRIDE; P43883; -.
DR ProteomicsDB; 289686; -.
DR Antibodypedia; 24726; 951 antibodies from 38 providers.
DR DNASU; 11520; -.
DR Ensembl; ENSMUST00000000466; ENSMUSP00000000466; ENSMUSG00000028494.
DR GeneID; 11520; -.
DR KEGG; mmu:11520; -.
DR UCSC; uc008tlz.1; mouse.
DR CTD; 123; -.
DR MGI; MGI:87920; Plin2.
DR VEuPathDB; HostDB:ENSMUSG00000028494; -.
DR eggNOG; ENOG502QRYF; Eukaryota.
DR GeneTree; ENSGT00950000182920; -.
DR HOGENOM; CLU_035133_0_1_1; -.
DR InParanoid; P43883; -.
DR OMA; QGKMLNN; -.
DR OrthoDB; 1437332at2759; -.
DR PhylomeDB; P43883; -.
DR TreeFam; TF328397; -.
DR BioGRID-ORCS; 11520; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Plin2; mouse.
DR PRO; PR:P43883; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P43883; protein.
DR Bgee; ENSMUSG00000028494; Expressed in thoracic mammary gland and 260 other tissues.
DR ExpressionAtlas; P43883; baseline and differential.
DR Genevisible; P43883; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005811; C:lipid droplet; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0015909; P:long-chain fatty acid transport; IDA:MGI.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IBA:GO_Central.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR InterPro; IPR004279; Perilipin.
DR Pfam; PF03036; Perilipin; 1.
DR PIRSF; PIRSF036881; PAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Lipid droplet; Membrane; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99541"
FT CHAIN 2..425
FT /note="Perilipin-2"
FT /id="PRO_0000099889"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99541"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99541"
FT MOD_RES 230
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99541"
FT CONFLICT 183
FT /note="L -> M (in Ref. 1; AAA37176 and 2; L09734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 46646 MW; D2624E1BFF335BF9 CRC64;
MAAAVVDPQQ SVVMRVANLP LVSSTYDLVS SAYVSTKDQY PYLRSVCEMA EKGVKTVTSA
AMTSALPIIQ KLEPQIAVAN TYACKGLDRM EERLPILNQP TSEIVASARG AVTGAKDVVT
TTMAGAKDSV ASTVSGVVDK TKGAVTGSVE RTKSVVNGSI NTVLGMVQFM NSGVDNAITK
SELLVDQYFP LTQEELEMEA KKVEGFDMVQ KPSNYERLES LSTKLCSRAY HQALSRVKEA
KQKSQETISQ LHSTVHLIEF ARKNMHSANQ KIQGAQDKLY VSWVEWKRSI GYDDTDESHC
VEHIESRTLA IARNLTQQLQ TTCQTVLVNA QGLPQNIQDQ AKHLGVMAGD IYSVFRNAAS
FKEVSDGVLT SSKGQLQKMK ESLDEVMDYF VNNTPLNWLV GPFYPQSTEV NKASLKVQQS
EVKAQ
