ID   PLIN2_BOVIN             Reviewed;         450 AA.
AC   Q9TUM6; Q3T0Y0;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 93.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Mammary gland;
RX   PubMed=10629799; DOI=10.3168/jds.s0022-0302(99)75508-6;
RA   Nielsen R.L., Andersen M.H., Mabhout P., Berglund L., Petersen T.E.,
RA   Rasmussen J.T.;
RT   "Isolation of adipophilin and butyrophilin from bovine milk and
RT   characterization of a cDNA encoding adipophilin.";
RL   J. Dairy Sci. 82:2543-2549(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9TUM6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9TUM6-2; Sequence=VSP_019867;
CC   -!- TISSUE SPECIFICITY: Milk lipid globules. {ECO:0000269|PubMed:10629799}.
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; AJ011680; CAB53860.1; -; mRNA.
DR   EMBL; BC102211; AAI02212.1; -; mRNA.
DR   RefSeq; NP_776405.1; NM_173980.2. [Q9TUM6-1]
DR   AlphaFoldDB; Q9TUM6; -.
DR   SMR; Q9TUM6; -.
DR   STRING; 9913.ENSBTAP00000007519; -.
DR   PaxDb; Q9TUM6; -.
DR   PeptideAtlas; Q9TUM6; -.
DR   PRIDE; Q9TUM6; -.
DR   GeneID; 280981; -.
DR   KEGG; bta:280981; -.
DR   CTD; 123; -.
DR   eggNOG; ENOG502QRYF; Eukaryota.
DR   InParanoid; Q9TUM6; -.
DR   OrthoDB; 1437332at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   InterPro; IPR004279; Perilipin.
DR   Pfam; PF03036; Perilipin; 1.
DR   PIRSF; PIRSF036881; PAT; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Lipid droplet; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q99541"
FT   CHAIN           2..450
FT                   /note="Perilipin-2"
FT                   /id="PRO_0000099887"
FT   REGION          411..450
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"
FT   VAR_SEQ         402..450
FT                   /note="VGPFYPQVTESESAQAPGTTRRPGRWSRKHPKPVPVSNAEGSQPDDSSS ->
FT                   ALDFSITDFTSETDEIPDIIALEEEDGPNHSHANGPEPSQGKMLNN (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_019867"
FT   CONFLICT        54
FT                   /note="M -> T (in Ref. 2; AAI02212)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  49368 MW;  A5026FF11969A885 CRC64;
     MASVAVEPQL SVVTRVANLP LVSSTYDLVS SAYISRKDQY PYLKSLCEMA EKGMKTITSV
     AVTSALPIIQ KLEPQIAVAN TYACKGLDRI EEKLPILNQP TNQVVANAKG AMTGAKDAVT
     TTVTGAKDSV ASTITGVVDR TKGAVTGSVE KTKSVVSGSI NTVLRSRVMQ LMSSGVENAL
     TKSELLVDQY LPLTKDELEK EAKKVEGFDM VQKPSYYVRL GSLSTKLRSR AYQQALCRVE
     EAKRKGQETI SQLHSAFNLS ELARKNVHNA NQKIQDAQDK LYLSWLEWKR SIGYDDTDES
     HCAEHIESRT LAIARNLTQQ LQTMCHTLLS NIQGLPQNIQ DRANHLGVMA GDIYSVFRNA
     ASFKEVSDGL LASSKGQLQK MKESLDDVMD YLVNNTPLNW LVGPFYPQVT ESESAQAPGT
     TRRPGRWSRK HPKPVPVSNA EGSQPDDSSS