ID   PLIN_HUMAN              Reviewed;         522 AA.
AC   O60240; Q8N5Y6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   07-JUL-2009, entry version 75.
DE   RecName: Full=Perilipin;
DE            Short=PERI;
DE   AltName: Full=Lipid droplet-associated protein;
GN   Name=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   MEDLINE=98190526; 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).
CC   -!- FUNCTION: Modulator of adipocyte lipid metabolism, it coats lipid
CC       storage droplets to protect them to be broken down by hormone-
CC       sensitive lipase (HSL). Its absence may result in leanness.
CC   -!- SUBUNIT: Interacts with ABHD5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Lipid droplet (By similarity). Note=Lipid
CC       droplet surface-associated (By similarity).
CC   -!- TISSUE SPECIFICITY: Adipocytes.
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).
CC   -!- SIMILARITY: Belongs to the perilipin family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Fat, wonderful fat -
CC       Issue 10 of May 2001;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt010.shtml";
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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   IPI; IPI00028444; -.
DR   RefSeq; NP_001138783.1; -.
DR   RefSeq; NP_002657.3; -.
DR   UniGene; Hs.103253; -.
DR   PhosphoSite; O60240; -.
DR   PRIDE; O60240; -.
DR   Ensembl; ENSG00000166819; Homo sapiens.
DR   GeneID; 5346; -.
DR   KEGG; hsa:5346; -.
DR   UCSC; uc002boh.1; human.
DR   GeneCards; GC15M088008; -.
DR   H-InvDB; HIX0012568; -.
DR   HGNC; HGNC:9076; PLIN.
DR   MIM; 170290; gene.
DR   PharmGKB; PA33409; -.
DR   HOGENOM; O60240; -.
DR   HOVERGEN; O60240; -.
DR   Reactome; REACT_602; Metabolism of lipids and lipoproteins.
DR   NextBio; 20718; -.
DR   ArrayExpress; O60240; -.
DR   Bgee; O60240; -.
DR   CleanEx; HS_PLIN; -.
DR   GermOnline; ENSG00000166819; Homo sapiens.
DR   GO; GO:0012511; C:monolayer-surrounded lipid storage body; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; NAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; ISS:UniProtKB.
DR   InterPro; IPR004279; Perilipin.
DR   PANTHER; PTHR14024; Perilipin; 1.
DR   Pfam; PF03036; Perilipin; 1.
DR   PIRSF; PIRSF036881; PAT; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Lipid droplet; Lipid metabolism; Phosphoprotein;
KW   Polymorphism.
FT   CHAIN         1    522       Perilipin.
FT                                /FTId=PRO_0000099884.
FT   COMPBIAS    307    316       Poly-Glu.
FT   VARIANT     194    194       P -> A (in dbSNP:rs6496589).
FT                                /FTId=VAR_055046.
FT   VARIANT     210    210       K -> E (in dbSNP:rs17852910).
FT                                /FTId=VAR_055047.
FT   VARIANT     348    348       S -> L (in dbSNP:rs8179071).
FT                                /FTId=VAR_055048.
FT   CONFLICT    510    510       L -> V (in Ref. 1; BAA25420).
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
//