PLIN1_HUMAN
ID PLIN1_HUMAN Reviewed; 522 AA.
AC O60240; Q8N5Y6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Perilipin-1;
DE AltName: Full=Lipid droplet-associated protein;
GN Name=PLIN1; Synonyms=PERI, PLIN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT ALA-194.
RC TISSUE=Adipocyte;
RX PubMed=9521880; DOI=10.1006/geno.1997.5179;
RA Nishiu J., Tanaka T., Nakamura Y.;
RT "Isolation and chromosomal mapping of the human homolog of perilipin
RT (PLIN), a rat adipose tissue-specific gene, by differential display
RT method.";
RL Genomics 48:254-257(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-194 AND GLU-210.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INVOLVEMENT IN FPLD4.
RX PubMed=21345103; DOI=10.1056/nejmoa1007487;
RA Gandotra S., Le Dour C., Bottomley W., Cervera P., Giral P., Reznik Y.,
RA Charpentier G., Auclair M., Delepine M., Barroso I., Semple R.K.,
RA Lathrop M., Lascols O., Capeau J., O'Rahilly S., Magre J., Savage D.B.,
RA Vigouroux C.;
RT "Perilipin deficiency and autosomal dominant partial lipodystrophy.";
RL N. Engl. J. Med. 364:740-748(2011).
RN [5]
RP FUNCTION IN UNILOCULAR LIPID DROPLET FORMATION AND LIPOLYSIS, INTERACTION
RP WITH CIDEC, AND SUBCELLULAR LOCATION.
RX PubMed=23399566; DOI=10.1016/j.bbrc.2013.01.113;
RA Grahn T.H., Zhang Y., Lee M.J., Sommer A.G., Mostoslavsky G., Fried S.K.,
RA Greenberg A.S., Puri V.;
RT "FSP27 and PLIN1 interaction promotes the formation of large lipid droplets
RT in human adipocytes.";
RL Biochem. Biophys. Res. Commun. 432:296-301(2013).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-130; SER-174;
RP SER-382; SER-436 AND SER-497, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=26357594; DOI=10.7717/peerj.1213;
RA Chughtai A.A., Kassak F., Kostrouchova M., Novotny J.P., Krause M.W.,
RA Saudek V., Kostrouch Z., Kostrouchova M.;
RT "Perilipin-related protein regulates lipid metabolism in C. elegans.";
RL PeerJ 3:E1213-E1213(2015).
RN [8]
RP INTERACTION WITH AQP7, IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE
RP SPECIFICITY.
RX PubMed=27832861; DOI=10.1016/j.metabol.2016.09.004;
RA Hansen J.S., Krintel C., Hernebring M., Haataja T.J., de Mare S.,
RA Wasserstrom S., Kosinska-Eriksson U., Palmgren M., Holm C., Stenkula K.G.,
RA Jones H.A., Lindkvist-Petersson K.;
RT "Perilipin 1 binds to aquaporin 7 in human adipocytes and controls its
RT mobility via protein kinase A mediated phosphorylation.";
RL Metabolism 65:1731-1742(2016).
CC -!- FUNCTION: Modulator of adipocyte lipid metabolism. Coats lipid storage
CC droplets to protect them from breakdown by hormone-sensitive lipase
CC (HSL). Its absence may result in leanness. Plays a role in unilocular
CC lipid droplet formation by activating CIDEC. Their interaction promotes
CC lipid droplet enlargement and directional net neutral lipid transfer.
CC May modulate lipolysis and triglyceride levels.
CC {ECO:0000269|PubMed:23399566}.
CC -!- SUBUNIT: Interacts with ABHD5 (By similarity). Interacts with CIDEC
CC (PubMed:23399566). Interacts with AQP7 (PubMed:27832861).
CC {ECO:0000250|UniProtKB:Q8CGN5, ECO:0000269|PubMed:23399566,
CC ECO:0000269|PubMed:27832861}.
CC -!- INTERACTION:
CC O60240; O14520: AQP7; NbExp=4; IntAct=EBI-26906001, EBI-20765950;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:23399566}. Lipid droplet
CC {ECO:0000269|PubMed:23399566, ECO:0000305|PubMed:26357594}. Note=Lipid
CC droplet surface-associated. {ECO:0000269|PubMed:23399566}.
CC -!- TISSUE SPECIFICITY: Detected in adipocytes from white adipose tissue
CC (at protein level) (PubMed:27832861). Detected in visceral adipose
CC tissue and mammary gland (PubMed:9521880).
CC {ECO:0000269|PubMed:27832861, ECO:0000269|PubMed:9521880}.
CC -!- PTM: Major cAMP-dependent protein kinase-substrate in adipocytes, also
CC dephosphorylated by PP1. When phosphorylated, may be maximally
CC sensitive to HSL and when unphosphorylated, may play a role in the
CC inhibition of lipolysis, by acting as a barrier in lipid droplet (By
CC similarity). {ECO:0000250}.
CC -!- DISEASE: Lipodystrophy, familial partial, 4 (FPLD4) [MIM:613877]: A
CC form of lipodystrophy characterized by loss of subcutaneous adipose
CC tissue primarily affecting the lower limbs, insulin-resistant diabetes
CC mellitus, hypertriglyceridemia, and hypertension.
CC {ECO:0000269|PubMed:21345103}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Fat, wonderful fat - Issue
CC 10 of May 2001;
CC URL="https://web.expasy.org/spotlight/back_issues/010";
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DR EMBL; AB005293; BAA25420.1; -; mRNA.
DR EMBL; AC013787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031084; AAH31084.1; -; mRNA.
DR CCDS; CCDS10353.1; -.
DR RefSeq; NP_001138783.1; NM_001145311.1.
DR RefSeq; NP_002657.3; NM_002666.4.
DR RefSeq; XP_005254991.1; XM_005254934.4.
DR AlphaFoldDB; O60240; -.
DR BioGRID; 111361; 6.
DR IntAct; O60240; 1.
DR STRING; 9606.ENSP00000300055; -.
DR BindingDB; O60240; -.
DR ChEMBL; CHEMBL1741164; -.
DR GlyGen; O60240; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60240; -.
DR PhosphoSitePlus; O60240; -.
DR BioMuta; PLIN1; -.
DR jPOST; O60240; -.
DR MassIVE; O60240; -.
DR PaxDb; O60240; -.
DR PeptideAtlas; O60240; -.
DR PRIDE; O60240; -.
DR ProteomicsDB; 49270; -.
DR Antibodypedia; 15811; 388 antibodies from 37 providers.
DR DNASU; 5346; -.
DR Ensembl; ENST00000300055.10; ENSP00000300055.5; ENSG00000166819.12.
DR Ensembl; ENST00000430628.2; ENSP00000402167.2; ENSG00000166819.12.
DR GeneID; 5346; -.
DR KEGG; hsa:5346; -.
DR MANE-Select; ENST00000300055.10; ENSP00000300055.5; NM_002666.5; NP_002657.3.
DR UCSC; uc002boh.4; human.
DR CTD; 5346; -.
DR DisGeNET; 5346; -.
DR GeneCards; PLIN1; -.
DR HGNC; HGNC:9076; PLIN1.
DR HPA; ENSG00000166819; Group enriched (adipose tissue, breast).
DR MalaCards; PLIN1; -.
DR MIM; 170290; gene.
DR MIM; 613877; phenotype.
DR neXtProt; NX_O60240; -.
DR OpenTargets; ENSG00000166819; -.
DR Orphanet; 280356; PLIN1-related familial partial lipodystrophy.
DR PharmGKB; PA33409; -.
DR VEuPathDB; HostDB:ENSG00000166819; -.
DR eggNOG; ENOG502RY3Q; Eukaryota.
DR GeneTree; ENSGT00950000182920; -.
DR HOGENOM; CLU_037212_1_0_1; -.
DR InParanoid; O60240; -.
DR OMA; KDTISCP; -.
DR OrthoDB; 1437332at2759; -.
DR PhylomeDB; O60240; -.
DR TreeFam; TF325901; -.
DR PathwayCommons; O60240; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-9031528; NR1H2 & NR1H3 regulate gene expression linked to triglyceride lipolysis in adipose.
DR SignaLink; O60240; -.
DR SIGNOR; O60240; -.
DR BioGRID-ORCS; 5346; 14 hits in 1068 CRISPR screens.
DR ChiTaRS; PLIN1; human.
DR GeneWiki; Perilipin; -.
DR GenomeRNAi; 5346; -.
DR Pharos; O60240; Tbio.
DR PRO; PR:O60240; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O60240; protein.
DR Bgee; ENSG00000166819; Expressed in subcutaneous adipose tissue and 114 other tissues.
DR ExpressionAtlas; O60240; baseline and differential.
DR Genevisible; O60240; HS.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; TAS:Reactome.
DR GO; GO:0008289; F:lipid binding; NAS:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; NAS:UniProtKB.
DR InterPro; IPR004279; Perilipin.
DR InterPro; IPR042998; PLIN1.
DR PANTHER; PTHR47138; PTHR47138; 1.
DR Pfam; PF03036; Perilipin; 1.
DR PIRSF; PIRSF036881; PAT; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid droplet; Lipid metabolism; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..522
FT /note="Perilipin-1"
FT /id="PRO_0000099884"
FT REGION 195..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..319
FT /note="Required for interaction with CIDEC"
FT /evidence="ECO:0000250"
FT REGION 413..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..316
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGN5"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGN5"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGN5"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGN5"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43884"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43884"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43884"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGN5"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGN5"
FT VARIANT 194
FT /note="P -> A (in dbSNP:rs6496589)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9521880"
FT /id="VAR_055046"
FT VARIANT 210
FT /note="K -> E (in dbSNP:rs17852910)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055047"
FT VARIANT 271
FT /note="A -> V (in dbSNP:rs58361219)"
FT /id="VAR_061505"
FT VARIANT 348
FT /note="S -> L (in dbSNP:rs8179071)"
FT /id="VAR_055048"
FT CONFLICT 510
FT /note="L -> V (in Ref. 1; BAA25420)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 55990 MW; 394FC14388EB5DCC CRC64;
MAVNKGLTLL DGDLPEQENV LQRVLQLPVV SGTCECFQKT YTSTKEAHPL VASVCNAYEK
GVQSASSLAA WSMEPVVRRL STQFTAANEL ACRGLDHLEE KIPALQYPPE KIASELKDTI
STRLRSARNS ISVPIASTSD KVLGAALAGC ELAWGVARDT AEFAANTRAG RLASGGADLA
LGSIEKVVEY LLPPDKEESA PAPGHQQAQK SPKAKPSLLS RVGALTNTLS RYTVQTMARA
LEQGHTVAMW IPGVVPLSSL AQWGASVAMQ AVSRRRSEVR VPWLHSLAAA QEEDHEDQTD
TEGEDTEEEE ELETEENKFS EVAALPGPRG LLGGVAHTLQ KTLQTTISAV TWAPAAVLGM
AGRVLHLTPA PAVSSTKGRA MSLSDALKGV TDNVVDTVVH YVPLPRLSLM EPESEFRDID
NPPAEVERRE AERRASGAPS AGPEPAPRLA QPRRSLRSAQ SPGAPPGPGL EDEVATPAAP
RPGFPAVPRE KPKRRVSDSF FRPSVMEPIL GRTHYSQLRK KS
