ID PLIN1_RAT Reviewed; 517 AA. AC P43884; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 24-JAN-2024, entry version 144. DE RecName: Full=Perilipin-1; DE AltName: Full=Lipid droplet-associated protein; GN Name=Plin1; Synonyms=Peri, Plin; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND PARTIAL PROTEIN RP SEQUENCE. RC STRAIN=Sprague-Dawley; TISSUE=Adipocyte; RX PubMed=7505452; DOI=10.1073/pnas.90.24.12035; RA Greenberg A.S., Egan J.J., Wek S.A., Moos M.C. Jr., Londos C., Kimmel A.R.; RT "Isolation of cDNAs for perilipins A and B: sequence and expression of RT lipid droplet-associated proteins of adipocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 90:12035-12039(1993). RN [2] RP PHOSPHORYLATION. RX PubMed=9755872; DOI=10.1016/s0014-5793(98)01052-7; RA Clifford G.M., McCormick D.K., Londos C., Vernon R.G., Yeaman S.J.; RT "Dephosphorylation of perilipin by protein phosphatases present in rat RT adipocytes."; RL FEBS Lett. 435:125-129(1998). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-174; THR-299; RP THR-301; SER-315; SER-385; SER-387; SER-411; SER-436; SER-440 AND SER-460, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 (ISOFORM B), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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 (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with ABHD5 (By similarity). Interacts with CIDEC. CC Interacts with AQP7 (By similarity). {ECO:0000250|UniProtKB:O60240, CC ECO:0000250|UniProtKB:Q8CGN5}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000250|UniProtKB:O60240}. Lipid droplet CC {ECO:0000250|UniProtKB:O60240}. Note=Lipid droplet surface-associated. CC {ECO:0000250|UniProtKB:O60240}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=PERIA; CC IsoId=P43884-1; Sequence=Displayed; CC Name=B; Synonyms=PERIB; CC IsoId=P43884-2; Sequence=VSP_004662, VSP_004663; CC -!- TISSUE SPECIFICITY: Adipocytes. CC -!- PTM: Major cAMP-dependent protein kinase substrate in adipocytes, also CC dephosphorylated by PP1. When phosphorylated, may be maximally CC sensitive to HSL. When unphosphorylated, may play a role in the CC inhibition of lipolysis, by acting as a barrier in lipid droplet. CC {ECO:0000269|PubMed:9755872}. CC -!- PTM: The N-terminus is blocked. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L26043; AAA41830.1; -; mRNA. DR EMBL; L26044; AAA41831.1; -; mRNA. DR PIR; A49413; A49413. DR AlphaFoldDB; P43884; -. DR STRING; 10116.ENSRNOP00000068793; -. DR GlyGen; P43884; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P43884; -. DR PhosphoSitePlus; P43884; -. DR PaxDb; 10116-ENSRNOP00000061809; -. DR UCSC; RGD:3351; rat. [P43884-1] DR AGR; RGD:3351; -. DR RGD; 3351; Plin1. DR eggNOG; ENOG502RY3Q; Eukaryota. DR InParanoid; P43884; -. DR PRO; PR:P43884; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005811; C:lipid droplet; IDA:RGD. DR GO; GO:0070417; P:cellular response to cold; ISO:RGD. DR GO; GO:0016042; P:lipid catabolic process; ISO:RGD. DR InterPro; IPR004279; Perilipin. DR InterPro; IPR042998; PLIN1. DR PANTHER; PTHR47138; PERILIPIN-1; 1. DR PANTHER; PTHR47138:SF1; PERILIPIN-1; 1. DR Pfam; PF03036; Perilipin; 1. DR PIRSF; PIRSF036881; PAT; 1. PE 1: Evidence at protein level; KW Alternative splicing; Direct protein sequencing; Endoplasmic reticulum; KW Lipid droplet; Lipid metabolism; Phosphoprotein; Reference proteome. FT CHAIN 1..517 FT /note="Perilipin-1" FT /id="PRO_0000099886" FT REGION 197..217 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 285..321 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 291..322 FT /note="Required for interaction with CIDEC" FT /evidence="ECO:0000250" FT REGION 415..495 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 298..319 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 81 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O60240" 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:22673903" 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:22673903" FT MOD_RES 224 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8CGN5" FT MOD_RES 299 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 301 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 315 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 385 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 387 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 411 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O60240" FT MOD_RES 436 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 440 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 460 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 492 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O60240" FT MOD_RES 494 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CGN5" FT VAR_SEQ 407..422 FT /note="LPRLSLMEPESEFQDI -> VSPAPGPPSDSQGRFD (in isoform B)" FT /evidence="ECO:0000303|PubMed:7505452" FT /id="VSP_004662" FT VAR_SEQ 423..517 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|PubMed:7505452" FT /id="VSP_004663" FT MOD_RES P43884-2:408 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" SQ SEQUENCE 517 AA; 55614 MW; 1041F76DC2F55A25 CRC64; MSMNKGPTLL DGDLPEQENV LQRVLQLPVV SGTCECFQKT YNSTKEAHPL VASVCNAYEK GVQGASNLAA WSMEPVVRRL STQFTAANEL ACRGLDHLEE KIPALQYPPE KIASELKGTI STRLRSARNS ISVPIASTSD KVLGATLAGC ELALGMAKET AEYAANTRVG RLASGGADLA LGSIEKVVEY LLPPDKVESA PSSGRQKTQK APKAKPSLLR RVSTLANTLS RHTMQTTARA LKRGHSLAMW IPGVAPLSSL AQWGASAAMQ VVSRRQSEVR VPWLHNLAAS KDENHEDQTD TEGEETDEEE EEEESEAEEN VLREVTALPT PLGFLGGVVH TVQKTLQNTI SAVTWAPAAV LGTVGRILHL TPAQAVSSTK GRAMSLSDAL KGVTDNVVDT VVHYVPLPRL SLMEPESEFQ DIDNPPAEVE RKGSGSRPAS PESTARPGQP RAACAVRGLS APSCPDLDDK TETSARPGLL AMPREKPARR VSDSFFRPSV MEPILGRTQY SQLRKKS //