PLIN1_RAT
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 25-MAY-2022, entry version 139.
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";
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DR EMBL; L26043; AAA41830.1; -; mRNA.
DR EMBL; L26044; AAA41831.1; -; mRNA.
DR PIR; A49413; A49413.
DR AlphaFoldDB; P43884; -.
DR STRING; 10116.ENSRNOP00000061809; -.
DR iPTMnet; P43884; -.
DR PhosphoSitePlus; P43884; -.
DR PaxDb; P43884; -.
DR UCSC; RGD:3351; rat. [P43884-1]
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; PTHR47138; 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
