ID   PLIN3_PIG               Reviewed;         439 AA.
AC   Q5BLZ2;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 67.
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   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].
RA   Zhang P., Yang Z., Duan L., Xia T., Yang Z.;
RL   Submitted (FEB-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. Required for
CC       the transport of mannose 6-phosphate receptors (MPR) from endosomes to
CC       the trans-Golgi network. {ECO:0000250|UniProtKB:O60664}.
CC   -!- SUBUNIT: Homooligomer. Interacts with M6PR (via the cytoplasmic
CC       domain). Interacts with IGF2R (via the cytoplasmic domain).
CC       {ECO:0000250|UniProtKB:O60664}.
CC   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:O60664}.
CC       Endosome membrane {ECO:0000250|UniProtKB:O60664}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:O60664}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:O60664}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O60664}. Note=Membrane associated on endosomes.
CC       Detected in the envelope and the core of lipid bodies and in lipid
CC       sails. {ECO:0000250|UniProtKB:O60664}.
CC   -!- PTM: Phosphorylation at Tyr-256 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:O60664}.
CC   -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
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DR   EMBL; AY939831; AAX31659.1; -; mRNA.
DR   RefSeq; NP_001026948.1; NM_001031778.1.
DR   AlphaFoldDB; Q5BLZ2; -.
DR   SMR; Q5BLZ2; -.
DR   STRING; 9823.ENSSSCP00000021684; -.
DR   PeptideAtlas; Q5BLZ2; -.
DR   PRIDE; Q5BLZ2; -.
DR   GeneID; 595103; -.
DR   KEGG; ssc:595103; -.
DR   CTD; 10226; -.
DR   eggNOG; ENOG502R7TG; Eukaryota.
DR   InParanoid; Q5BLZ2; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
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; Coiled coil; Cytoplasm; Endosome; Isopeptide bond;
KW   Lipid droplet; Membrane; Phosphoprotein; Reference proteome; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..439
FT                   /note="Perilipin-3"
FT                   /id="PRO_0000099892"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          254..282
FT                   /evidence="ECO:0000255"
FT   COILED          358..381
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         66
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
FT   MOD_RES         175
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
FT   MOD_RES         180
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
FT   MOD_RES         221
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
FT   MOD_RES         256
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
FT   CROSSLNK        123
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:O60664"
SQ   SEQUENCE   439 AA;  47900 MW;  FF38F6AD431F9C38 CRC64;
     MFASETEASA SSTQVTTEEP VQQPSVVDRV AGMPLISSTC HMVSAAYTST KESHPHVKTV
     CDVAEKGVKT LTAAAVSGAQ PILSKLEPQL TSASEYAHRG LDKLEENLPI LQQPSEKVLA
     DTKELVSSKV SEAREAVSNT VSSAKDTVAS RVTEAVVVTR GAVQSGVDLT KSMVTSSVHS
     VMGSRVGQMV LSGVDTVLGK SEEWVDNHLP MTDAELAHLA TSLEGFDMAS VAQQRQDQSY
     FVRLGSLSER LRQRAYEHSL GKLQHTRQRA QEALLQLSQA LSLMETVKQG VDQKLVEGQE
     KLHQMWLSWN QKRLQGGEED PAKPEQVESQ TFTMFRDVTQ QLQTTCASLG ASLQGLPAHV
     KEQALQARRQ VEDLQATFSG MHSFQDLSSN VLMQSREQVA RAREALDHVV DYVAQNTPVM
     WLVGPFAPGV VEKAPEEKK