ID   PLIN2_PIG               Reviewed;         459 AA.
AC   Q4PLW0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Perilipin-2;
DE   AltName: Full=Adipophilin;
DE   AltName: Full=Adipose differentiation-related protein;
DE            Short=ADRP;
GN   Name=PLIN2; Synonyms=ADFP, ADRP;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Meishan;
RX   PubMed=16167998; DOI=10.1111/j.1365-2052.2005.01344.x;
RA   Nie T., Zhao X.L., Qiu H., Xia T., Chen X.D., Gan L., Feng S.Q., Lei T.,
RA   Dai M.H., Yang Z.Q.;
RT   "Sequence analysis and map assignment of pig SREBF2 and ADFP.";
RL   Anim. Genet. 36:455-457(2005).
CC   -!- FUNCTION: Structural component of lipid droplets, which is required for
CC       the formation and maintenance of lipid storage droplets.
CC       {ECO:0000250|UniProtKB:Q99541}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P43883};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P43883}. Lipid
CC       droplet {ECO:0000250|UniProtKB:P43883}.
CC   -!- PTM: Acylated; primarily with C14, C16 and C18 fatty acids.
CC       {ECO:0000250|UniProtKB:Q99541}.
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:0000250|UniProtKB:Q99541}.
CC   -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
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DR   EMBL; DQ066659; AAY68481.1; -; mRNA.
DR   AlphaFoldDB; Q4PLW0; -.
DR   SMR; Q4PLW0; -.
DR   STRING; 9823.ENSSSCP00000005560; -.
DR   PaxDb; Q4PLW0; -.
DR   PeptideAtlas; Q4PLW0; -.
DR   PRIDE; Q4PLW0; -.
DR   eggNOG; ENOG502QRYF; Eukaryota.
DR   InParanoid; Q4PLW0; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005622; C:intracellular anatomical structure; IDA:AgBase.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   InterPro; IPR004279; Perilipin.
DR   Pfam; PF03036; Perilipin; 1.
DR   PIRSF; PIRSF036881; PAT; 1.
PE   2: Evidence at transcript 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..459
FT                   /note="Perilipin-2"
FT                   /id="PRO_0000252362"
FT   REGION          412..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99541"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99541"
FT   MOD_RES         232
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99541"
SQ   SEQUENCE   459 AA;  50196 MW;  B26E168539B606F1 CRC64;
     MASVAVESQP SVVTRVANLP LVSSTYDLVS SAYISTKDQY PYLKSLCEMA EKGVKTITSV
     AMSGALPIIQ KLEPQIAIAN TYACKGLDRI EEKLPILNQP TNQVVANAKG AVTGAKDAMT
     TTVTGAKDCV ASTITEVVDK TKEAVTGSVE KTKSVVNGSI NTVLGGRMMQ LVSSGVEKAF
     TKSELLVDQY LPLTEEELEK EAKKVEGFDM VQKPSYYIRL GSLSTKLRSR AYQQALTRVK
     EVKQKSQETI SQLHSTVNLI EFARKNVHNA NQKIQGTQDK LYLSWVEWKR SIGYDDTDES
     HCAEHIESRT LAIARNLTQQ LQTTCHTLVS NIQGLPQNIH DQANHLGVMA GDIYSVFHNA
     SSFKEMSDGL LSSSKGQLQK MKESLDDVMD YLVNNTPLNW LVGPFYPQLT ESQDAQSRGA
     ENTTSPETQQ PETKRIKPAP ASSAWGSQSG DTSCTVATC