LOCUS NP_005808 434 aa linear PRI 20-SEP-2024
DEFINITION perilipin-3 isoform 1 [Homo sapiens].
ACCESSION NP_005808
VERSION NP_005808.3
DBSOURCE REFSEQ: accession NM_005817.5
KEYWORDS RefSeq; MANE Select.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 434)
AUTHORS Liang,W., Zhou,Z., Gao,Q., Zhu,Z., Zhu,J., Lin,J., Wen,Y., Qian,F.,
Wang,L., Zhai,Y., Lv,J., Zhang,H., Zhong,F. and Du,H.
TITLE Tumor-derived Prevotella intermedia aggravates gastric cancer by
enhancing Perilipin 3 expression
JOURNAL Cancer Sci 115 (4), 1141-1153 (2024)
PUBMED 38287724
REMARK GeneRIF: Tumor-derived Prevotella intermedia aggravates gastric
cancer by enhancing Perilipin 3 expression.
REFERENCE 2 (residues 1 to 434)
AUTHORS He,Y., Liu,L., Dong,Y., Zhang,X., Song,Y., Jing,Y., Ni,Y., Wang,Y.,
Wang,Z. and Ding,L.
TITLE Lipid droplets-related Perilipin-3: potential immune checkpoint and
oncogene in oral squamous cell carcinoma
JOURNAL Cancer Immunol Immunother 73 (5), 78 (2024)
PUBMED 38554152
REMARK GeneRIF: Lipid droplets-related Perilipin-3: potential immune
checkpoint and oncogene in oral squamous cell carcinoma.
Publication Status: Online-Only
REFERENCE 3 (residues 1 to 434)
AUTHORS Stribny,J. and Schneiter,R.
TITLE Binding of perilipin 3 to membranes containing diacylglycerol is
mediated by conserved residues within its PAT domain
JOURNAL J Biol Chem 299 (12), 105384 (2023)
PUBMED 37898398
REMARK GeneRIF: Binding of perilipin 3 to membranes containing
diacylglycerol is mediated by conserved residues within its PAT
domain.
REFERENCE 4 (residues 1 to 434)
AUTHORS Men,X. and Zhu,W.
TITLE Silencing of Perilipin 3 Inhibits Lung Adenocarcinoma Cell Immune
Resistance by Regulating the Transcription of PD-L1 Through c-Myc
JOURNAL Immunol Invest 52 (7), 815-831 (2023)
PUBMED 37578465
REMARK GeneRIF: Silencing of Perilipin 3 Inhibits Lung Adenocarcinoma Cell
Immune Resistance by Regulating the Transcription of PD-L1 Through
c-Myc.
REFERENCE 5 (residues 1 to 434)
AUTHORS Chung,J., Park,J., Lai,Z.W., Lambert,T.J., Richards,R.C., Zhang,J.,
Walther,T.C. and Farese,R.V. Jr.
TITLE The Troyer syndrome protein spartin mediates selective autophagy of
lipid droplets
JOURNAL Nat Cell Biol 25 (8), 1101-1110 (2023)
PUBMED 37443287
REFERENCE 6 (residues 1 to 434)
AUTHORS Krise,J.P., Sincock,P.M., Orsel,J.G. and Pfeffer,S.R.
TITLE Quantitative analysis of TIP47-receptor cytoplasmic domain
interactions: implications for endosome-to-trans Golgi network
trafficking
JOURNAL J Biol Chem 275 (33), 25188-25193 (2000)
PUBMED 10829017
REFERENCE 7 (residues 1 to 434)
AUTHORS Than,N.G., Sumegi,B., Than,G.N., Kispal,G. and Bohn,H.
TITLE Cloning and sequencing of human oncodevelopmental soluble placental
tissue protein 17 (PP17): homology with adipophilin and the mouse
adipose differentiation-related protein
JOURNAL Tumour Biol 20 (4), 184-192 (1999)
PUBMED 10393528
REFERENCE 8 (residues 1 to 434)
AUTHORS Than,N.G., Sumegi,B., Than,G.N., Kispal,G. and Bohn,H.
TITLE Cloning and sequence analysis of cDNAs encoding human placental
tissue protein 17 (PP17) variants
JOURNAL Eur J Biochem 258 (2), 752-757 (1998)
PUBMED 9874244
REFERENCE 9 (residues 1 to 434)
AUTHORS Diaz,E. and Pfeffer,S.R.
TITLE TIP47: a cargo selection device for mannose 6-phosphate receptor
trafficking
JOURNAL Cell 93 (3), 433-443 (1998)
PUBMED 9590177
REFERENCE 10 (residues 1 to 434)
AUTHORS Bohn,H., Kraus,W. and Winckler,W.
TITLE Purification and characterization of two new soluble placental
tissue proteins (PP13 and PP17)
JOURNAL Oncodev Biol Med 4 (5), 343-350 (1983)
PUBMED 6856484
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AK312740.1, BQ057849.1,
AK225045.1 and BC019278.1.
This sequence is a reference standard in the RefSeqGene project.
On Aug 14, 2009 this sequence version replaced NP_005808.2.
Summary: Mannose 6-phophate receptors (MPRs) deliver lysosomal
hydrolase from the Golgi to endosomes and then return to the Golgi
complex. The protein encoded by this gene interacts with the
cytoplasmic domains of both cation-independent and cation-dependent
MPRs, and is required for endosome-to-Golgi transport. This protein
also binds directly to the GTPase RAB9 (RAB9A), a member of the RAS
oncogene family. The interaction with RAB9 has been shown to
increase the affinity of this protein for its cargo. Multiple
transcript variants encoding different isoforms have been found for
this gene.[provided by RefSeq, Aug 2009].
Transcript Variant: This variant (1) encodes the longest isoform
(1).
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: BC019278.1, AK226088.1 [ECO:0000332]
RNAseq introns :: mixed sample support SAMEA1965299,
SAMEA1966682 [ECO:0006172]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000221957.9/ ENSP00000221957.3
RefSeq Select criteria :: based on conservation, expression,
longest protein
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..434
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="19"
/map="19p13.3"
Protein 1..434
/product="perilipin-3 isoform 1"
/note="tail-interacting protein, 47 kD; testicular tissue
protein Li 114; cargo selection protein TIP47; placental
protein 17; 47 kDa MPR-binding protein;
mannose-6-phosphate receptor-binding protein 1"
/calculated_mol_wt=46944
Region 1..22
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (O60664.3)"
Site 2
/site_type="acetylation"
/note="N-acetylserine.
/evidence=ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
propagated from UniProtKB/Swiss-Prot (O60664.3)"
Region 18..425
/region_name="Perilipin"
/note="Perilipin family; pfam03036"
/db_xref="CDD:460784"
Site 31
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
Site 65
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0007744|PubMed:19608861; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
Site 91
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
Site 130
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
propagated from UniProtKB/Swiss-Prot (O60664.3)"
Site 148
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
Site 170
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0007744|PubMed:18669648; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
Site 175
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
Site 179
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
Site 216
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
Site 217
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
Site 241
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
Site 251
/site_type="phosphorylation"
/note="Phosphotyrosine.
/evidence=ECO:0000269|PubMed:34077757; propagated from
UniProtKB/Swiss-Prot (O60664.3)"
CDS 1..434
/gene="PLIN3"
/gene_synonym="M6PRBP1; PP17; TIP47"
/coded_by="NM_005817.5:77..1381"
/note="isoform 1 is encoded by transcript variant 1"
/db_xref="CCDS:CCDS12137.1"
/db_xref="GeneID:10226"
/db_xref="HGNC:HGNC:16893"
/db_xref="MIM:602702"
ORIGIN
1 msadgaeadg stqvtveepv qqpsvvdrva smplisstcd mvsaayastk esyphiktvc
61 daaekgvrtl taaavsgaqp ilsklepqia saseyahrgl dkleenlpil qqptekvlad
121 tkelvsskvs gaqemvssak dtvatqlsea vdatrgavqs gvdktksvvt ggvqsvmgsr
181 lgqmvlsgvd tvlgkseewa dnhlpltdae lariatsldg fdvasvqqqr qeqsyfvrlg
241 slserlrqha yehslgklra tkqraqeall qlsqvlslme tvkqgvdqkl vegqeklhqm
301 wlswnqkqlq gpekeppkpe qvesraltmf rdiaqqlqat ctslgssiqg lptnvkdqvq
361 qarrqvedlq atfssihsfq dlsssilaqs rervasarea ldhmveyvaq ntpvtwlvgp
421 fapgitekap eekk
//