PLIN3_PONAB
ID PLIN3_PONAB Reviewed; 434 AA.
AC Q5RAV8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Perilipin-3;
DE AltName: Full=Mannose-6-phosphate receptor-binding protein 1;
GN Name=PLIN3; Synonyms=M6PRBP1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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-251 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; CR858903; CAH91102.1; -; mRNA.
DR RefSeq; NP_001125642.1; NM_001132170.1.
DR AlphaFoldDB; Q5RAV8; -.
DR SMR; Q5RAV8; -.
DR STRING; 9601.ENSPPYP00000010562; -.
DR GeneID; 100172561; -.
DR CTD; 10226; -.
DR eggNOG; ENOG502R7TG; Eukaryota.
DR InParanoid; Q5RAV8; -.
DR Proteomes; UP000001595; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT CHAIN 2..434
FT /note="Perilipin-3"
FT /id="PRO_0000099893"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 252..280
FT /evidence="ECO:0000255"
FT COILED 353..377
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 65
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT MOD_RES 251
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60664"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:O60664"
SQ SEQUENCE 434 AA; 46990 MW; B4FCC9D5F423F4EC CRC64;
MSADGAEADG STQVTVEEPV QQPSVVDRVA SMPLISSTCD MVSAAYASTK ESYPHVKTVC
DAAEKGVRTL TAAAVSGAQP ILSKLEPQIA SASEYAHRGL DKLEENLPIL QQPTERVLAD
TKELVSSKVS GAQEMVSSAK DTVATQLSEA VDATRGAVQS GVDKTKSVVT GGVQSVMGSR
LGQMVLSGVD TVLGKSGEWA DNHLPLTDAE LARIATSLDG FDVASVQQQR QEQSYFVRLG
SLSERLRQHA YEHSLGKLRA TKQRAQEALL QLSQALSLME TVKEGVDQKL VEGQEKLHQM
WLSWNQKQLQ GPEKEPPKPE QVESRALTMF RDIAQQLQAT CTSLGSSIQG LPTNVKDQVQ
QARRQVEDLQ ATFSSIHSFQ DLSSSILAQS RERVASAREA LDHMVEYVAQ NTPVTWLVGP
FAPGITEKAP EEKK
