PLIN2_HUMAN
ID PLIN2_HUMAN Reviewed; 437 AA.
AC Q99541; Q9BSC3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Perilipin-2;
DE AltName: Full=Adipophilin;
DE AltName: Full=Adipose differentiation-related protein {ECO:0000303|PubMed:9003395};
DE Short=ADRP {ECO:0000303|PubMed:9003395};
GN Name=PLIN2; Synonyms=ADFP;
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], TISSUE SPECIFICITY, AND ACYLATION.
RX PubMed=9003395; DOI=10.1042/bj3201025;
RA Heid H.W., Schnolzer M., Keenan T.W.;
RT "Adipocyte differentiation-related protein is secreted into milk as a
RT constituent of milk lipid globule membrane.";
RL Biochem. J. 320:1025-1030(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tangkeangsirisin W., Serrero G.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
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 [9]
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-232, AND MUTAGENESIS
RP OF TYR-232.
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 {ECO:0000269|PubMed:34077757}.
CC -!- INTERACTION:
CC Q99541; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-2115275, EBI-2813554;
CC Q99541; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-2115275, EBI-12878374;
CC Q99541; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-2115275, EBI-12937691;
CC Q99541; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2115275, EBI-10975473;
CC Q99541; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-2115275, EBI-1389308;
CC Q99541; O95562: SFT2D2; NbExp=3; IntAct=EBI-2115275, EBI-4402330;
CC Q99541; O76024: WFS1; NbExp=3; IntAct=EBI-2115275, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P43883};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P43883}. Lipid
CC droplet {ECO:0000269|PubMed:34077757, ECO:0000305|PubMed:26357594}.
CC -!- TISSUE SPECIFICITY: Milk lipid globules. {ECO:0000269|PubMed:9003395}.
CC -!- PTM: Acylated; primarily with C14, C16 and C18 fatty acids.
CC {ECO:0000269|PubMed:9003395}.
CC -!- PTM: Phosphorylation at Tyr-232 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; X97324; CAA65989.1; -; mRNA.
DR EMBL; AF443203; AAL35614.1; -; mRNA.
DR EMBL; BC005127; AAH05127.1; -; mRNA.
DR CCDS; CCDS6490.1; -.
DR RefSeq; NP_001113.2; NM_001122.3.
DR AlphaFoldDB; Q99541; -.
DR SMR; Q99541; -.
DR BioGRID; 106635; 21.
DR IntAct; Q99541; 14.
DR STRING; 9606.ENSP00000276914; -.
DR GlyGen; Q99541; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99541; -.
DR PhosphoSitePlus; Q99541; -.
DR BioMuta; PLIN2; -.
DR DMDM; 21264409; -.
DR EPD; Q99541; -.
DR jPOST; Q99541; -.
DR MassIVE; Q99541; -.
DR MaxQB; Q99541; -.
DR PaxDb; Q99541; -.
DR PeptideAtlas; Q99541; -.
DR PRIDE; Q99541; -.
DR ProteomicsDB; 78314; -.
DR Antibodypedia; 24726; 951 antibodies from 38 providers.
DR DNASU; 123; -.
DR Ensembl; ENST00000276914.7; ENSP00000276914.2; ENSG00000147872.10.
DR GeneID; 123; -.
DR KEGG; hsa:123; -.
DR MANE-Select; ENST00000276914.7; ENSP00000276914.2; NM_001122.4; NP_001113.2.
DR UCSC; uc003zno.4; human.
DR CTD; 123; -.
DR DisGeNET; 123; -.
DR GeneCards; PLIN2; -.
DR HGNC; HGNC:248; PLIN2.
DR HPA; ENSG00000147872; Tissue enhanced (adipose tissue, liver).
DR MIM; 103195; gene.
DR neXtProt; NX_Q99541; -.
DR OpenTargets; ENSG00000147872; -.
DR PharmGKB; PA24569; -.
DR VEuPathDB; HostDB:ENSG00000147872; -.
DR eggNOG; ENOG502QRYF; Eukaryota.
DR GeneTree; ENSGT00950000182920; -.
DR HOGENOM; CLU_035133_0_1_1; -.
DR InParanoid; Q99541; -.
DR OMA; QGKMLNN; -.
DR OrthoDB; 1437332at2759; -.
DR PhylomeDB; Q99541; -.
DR TreeFam; TF328397; -.
DR PathwayCommons; Q99541; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-9613354; Lipophagy.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR SignaLink; Q99541; -.
DR SIGNOR; Q99541; -.
DR BioGRID-ORCS; 123; 14 hits in 1082 CRISPR screens.
DR ChiTaRS; PLIN2; human.
DR GeneWiki; Adipose_differentiation-related_protein; -.
DR GenomeRNAi; 123; -.
DR Pharos; Q99541; Tbio.
DR PRO; PR:Q99541; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q99541; protein.
DR Bgee; ENSG00000147872; Expressed in pericardium and 197 other tissues.
DR ExpressionAtlas; Q99541; baseline and differential.
DR Genevisible; Q99541; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0015909; P:long-chain fatty acid transport; IEA:Ensembl.
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; Lipoprotein; Membrane; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..437
FT /note="Perilipin-2"
FT /id="PRO_0000099888"
FT REGION 412..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 232
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:34077757"
FT VARIANT 251
FT /note="S -> P (in dbSNP:rs35568725)"
FT /id="VAR_061506"
FT MUTAGEN 232
FT /note="Y->F: Abolished phosphorylation at Tyr-232 by
FT isoform 1 of CHKA (CHKalpha2)."
FT /evidence="ECO:0000269|PubMed:34077757"
FT CONFLICT 305..306
FT /note="HI -> QF (in Ref. 1; CAA65989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 48075 MW; 36411341619E53BF CRC64;
MASVAVDPQP SVVTRVVNLP LVSSTYDLMS SAYLSTKDQY PYLKSVCEMA ENGVKTITSV
AMTSALPIIQ KLEPQIAVAN TYACKGLDRI EERLPILNQP STQIVANAKG AVTGAKDAVT
TTVTGAKDSV ASTITGVMDK TKGAVTGSVE KTKSVVSGSI NTVLGSRMMQ LVSSGVENAL
TKSELLVEQY LPLTEEELEK EAKKVEGFDL VQKPSYYVRL GSLSTKLHSR AYQQALSRVK
EAKQKSQQTI SQLHSTVHLI EFARKNVYSA NQKIQDAQDK LYLSWVEWKR SIGYDDTDES
HCAEHIESRT LAIARNLTQQ LQTTCHTLLS NIQGVPQNIQ DQAKHMGVMA GDIYSVFRNA
ASFKEVSDSL LTSSKGQLQK MKESLDDVMD YLVNNTPLNW LVGPFYPQLT ESQNAQDQGA
EMDKSSQETQ RSEHKTH
