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   11-NOV-2015, entry version 129.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA   Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA   Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA   Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA   Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA   Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA   Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human
RT   chromosome 15.";
RL   Nature 440:671-675(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-194 AND
RP   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
RT   project: 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.,
RA   Reznik Y., Charpentier G., Auclair M., Delepine M., Barroso I.,
RA   Semple R.K., Lathrop M., Lascols O., Capeau J., O'Rahilly S.,
RA   Magre J., Savage D.B., 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,
RP   INTERACTION 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.,
RA   Fried S.K., Greenberg A.S., Puri V.;
RT   "FSP27 and PLIN1 interaction promotes the formation of large lipid
RT   droplets 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Modulator of adipocyte lipid metabolism. Coats lipid
CC       storage droplets to protect them from breakdown by hormone-
CC       sensitive lipase (HSL). Its absence may result in leanness. Plays
CC       a role in unilocular lipid droplet formation by activating CIDEC.
CC       Their interaction promotes lipid droplet enlargement and
CC       directional net neutral lipid transfer. May modulate lipolysis and
CC       triglyceride levels. {ECO:0000269|PubMed:23399566}.
CC   -!- SUBUNIT: Interacts with ABHD5 (By similarity). Interacts with
CC       CIDEC. {ECO:0000250, ECO:0000269|PubMed:23399566}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:23399566}. Lipid droplet
CC       {ECO:0000269|PubMed:23399566}. Note=Lipid droplet surface-
CC       associated.
CC   -!- TISSUE SPECIFICITY: Adipocytes. {ECO:0000269|PubMed:9521880}.
CC   -!- PTM: Major cAMP-dependent protein kinase-substrate in adipocytes,
CC       also dephosphorylated by PP1. When phosphorylated, may be
CC       maximally sensitive to HSL and when unphosphorylated, may play a
CC       role in the inhibition of lipolysis, by acting as a barrier in
CC       lipid droplet (By similarity). {ECO:0000250}.
CC   -!- DISEASE: Lipodystrophy, familial partial, 4 (FPLD4) [MIM:613877]:
CC       A form of lipodystrophy characterized by loss of subcutaneous
CC       adipose tissue primarily affecting the lower limbs, insulin-
CC       resistant diabetes mellitus, hypertriglyceridemia, and
CC       hypertension. {ECO:0000269|PubMed:21345103}. Note=The disease is
CC       caused by mutations 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 -
CC       Issue 10 of May 2001;
CC       URL="http://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_005254934.3.
DR   UniGene; Hs.103253; -.
DR   ProteinModelPortal; O60240; -.
DR   BioGrid; 111361; 3.
DR   STRING; 9606.ENSP00000300055; -.
DR   BindingDB; O60240; -.
DR   ChEMBL; CHEMBL1741164; -.
DR   PhosphoSite; O60240; -.
DR   BioMuta; PLIN1; -.
DR   PaxDb; O60240; -.
DR   PRIDE; O60240; -.
DR   Ensembl; ENST00000300055; ENSP00000300055; ENSG00000166819.
DR   Ensembl; ENST00000430628; ENSP00000402167; ENSG00000166819.
DR   GeneID; 5346; -.
DR   KEGG; hsa:5346; -.
DR   UCSC; uc002boh.2; human.
DR   CTD; 5346; -.
DR   GeneCards; PLIN1; -.
DR   H-InvDB; HIX0202172; -.
DR   HGNC; HGNC:9076; PLIN1.
DR   HPA; CAB033821; -.
DR   HPA; CAB037333; -.
DR   HPA; HPA024299; -.
DR   MIM; 170290; gene.
DR   MIM; 613877; phenotype.
DR   neXtProt; NX_O60240; -.
DR   Orphanet; 280356; Familial partial lipodystrophy associated with PLIN1 mutations.
DR   PharmGKB; PA33409; -.
DR   eggNOG; ENOG410IGIT; Eukaryota.
DR   eggNOG; ENOG4111TBF; LUCA.
DR   GeneTree; ENSGT00500000044795; -.
DR   HOGENOM; HOG000261608; -.
DR   InParanoid; O60240; -.
DR   KO; K08768; -.
DR   OMA; ILGRAQY; -.
DR   OrthoDB; EOG7SN8CD; -.
DR   PhylomeDB; O60240; -.
DR   TreeFam; TF325901; -.
DR   Reactome; R-HSA-163560; Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
DR   Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR   GeneWiki; Perilipin; -.
DR   GenomeRNAi; 5346; -.
DR   NextBio; 20718; -.
DR   PRO; PR:O60240; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   Bgee; O60240; -.
DR   CleanEx; HS_PLIN; -.
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 particle; NAS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; NAS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; NAS:UniProtKB.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
DR   InterPro; IPR004279; Perilipin.
DR   PANTHER; PTHR14024; PTHR14024; 1.
DR   Pfam; PF03036; Perilipin; 1.
DR   PIRSF; PIRSF036881; PAT; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Endoplasmic reticulum; Lipid droplet;
KW   Lipid metabolism; Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN         1    522       Perilipin-1.
FT                                /FTId=PRO_0000099884.
FT   REGION      291    319       Required for interaction with CIDEC.
FT                                {ECO:0000250}.
FT   COMPBIAS    307    316       Poly-Glu.
FT   MOD_RES      81     81       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES      85     85       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q8CGN5}.
FT   MOD_RES     126    126       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CGN5}.
FT   MOD_RES     130    130       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     132    132       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CGN5}.
FT   MOD_RES     137    137       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CGN5}.
FT   MOD_RES     174    174       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     299    299       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P43884}.
FT   MOD_RES     301    301       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P43884}.
FT   MOD_RES     382    382       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     384    384       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P43884}.
FT   MOD_RES     408    408       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CGN5}.
FT   MOD_RES     436    436       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     497    497       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     499    499       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CGN5}.
FT   VARIANT     194    194       P -> A (in dbSNP:rs6496589).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9521880}.
FT                                /FTId=VAR_055046.
FT   VARIANT     210    210       K -> E (in dbSNP:rs17852910).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_055047.
FT   VARIANT     271    271       A -> V (in dbSNP:rs58361219).
FT                                /FTId=VAR_061505.
FT   VARIANT     348    348       S -> L (in dbSNP:rs8179071).
FT                                /FTId=VAR_055048.
FT   CONFLICT    510    510       L -> V (in Ref. 1; BAA25420).
FT                                {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
//