PLIN1_MOUSE
ID PLIN1_MOUSE Reviewed; 517 AA.
AC Q8CGN5; Q4V9U2; Q8C0F5;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Perilipin-1;
DE AltName: Full=Lipid droplet-associated protein;
DE AltName: Full=Perilipin A;
GN Name=Plin1; Synonyms=Peri, Plin;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=11641724; DOI=10.1007/s00335-01-2055-5;
RA Lu X., Gruia-Gray J., Copeland N.G., Gilbert D.J., Jenkins N.A., Londos C.,
RA Kimmel A.R.;
RT "The murine perilipin gene: the lipid droplet-associated perilipins derive
RT from tissue-specific, mRNA splice variants and define a gene family of
RT ancient origin.";
RL Mamm. Genome 12:741-749(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Tansey J.T., Lu X., Londos C., Kimmel A.R.;
RT "Mouse perilipin.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [6]
RP INTERACTION WITH ABHD5.
RX PubMed=15292255; DOI=10.1074/jbc.m407462200;
RA Subramanian V., Rothenberg A., Gomez C., Cohen A.W., Garcia A.,
RA Bhattacharyya S., Shapiro L., Dolios G., Wang R., Lisanti M.P.,
RA Brasaemle D.L.;
RT "Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in
RT 3T3-L1 adipocytes.";
RL J. Biol. Chem. 279:42062-42071(2004).
RN [7]
RP PHOSPHORYLATION AT SER-410 AND SER-460.
RX PubMed=19921680; DOI=10.1002/pmic.200800861;
RA Kanshin E., Wang S., Ashmarina L., Fedjaev M., Nifant'ev I., Mitchell G.A.,
RA Pshezhetsky A.V.;
RT "The stoichiometry of protein phosphorylation in adipocyte lipid droplets:
RT analysis by N-terminal isotope tagging and enzymatic dephosphorylation.";
RL Proteomics 9:5067-5077(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; THR-85; SER-126; SER-130;
RP SER-132; SER-137; SER-174; THR-223; SER-384; SER-410; SER-492 AND SER-494,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION IN UNILOCULAR LIPID DROPLET FORMATION AND LIPOLYSIS, INTERACTION
RP WITH CIDEC, AND SUBCELLULAR LOCATION.
RX PubMed=23481402; DOI=10.1038/ncomms2581;
RA Sun Z., Gong J., Wu H., Xu W., Wu L., Xu D., Gao J., Wu J.W., Yang H.,
RA Yang M., Li P.;
RT "Perilipin1 promotes unilocular lipid droplet formation through the
RT activation of Fsp27 in adipocytes.";
RL Nat. Commun. 4:1594-1594(2013).
RN [10]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-492.
RX PubMed=24945349; DOI=10.1371/journal.pone.0100559;
RA Okumura T., Harada K., Oue K., Zhang J., Asano S., Hayashiuchi M.,
RA Mizokami A., Tanaka H., Irifune M., Kamata N., Hirata M., Kanematsu T.;
RT "Phospholipase C-related catalytically inactive protein (PRIP) regulates
RT lipolysis in adipose tissue by modulating the phosphorylation of hormone-
RT sensitive lipase.";
RL PLoS ONE 9:E100559-E100559(2014).
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 (By similarity). Plays a role
CC in unilocular lipid droplet formation by activating CIDEC. Their
CC interaction promotes lipid droplet enlargement and directional net
CC neutral lipid transfer. May modulate lipolysis and triglyceride levels.
CC {ECO:0000250, ECO:0000269|PubMed:23481402}.
CC -!- SUBUNIT: Interacts with ABHD5 (PubMed:15292255). Interacts with CIDEC
CC (PubMed:23481402). Interacts with AQP7 (By similarity).
CC {ECO:0000250|UniProtKB:O60240, ECO:0000269|PubMed:15292255,
CC ECO:0000269|PubMed:23481402}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O60240}. Lipid droplet
CC {ECO:0000269|PubMed:23481402, ECO:0000269|PubMed:24945349}. Note=Lipid
CC droplet surface-associated. {ECO:0000250|UniProtKB:O60240}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Peri A;
CC IsoId=Q8CGN5-1; Sequence=Displayed;
CC Name=2; Synonyms=Peri B;
CC IsoId=Q8CGN5-2; Sequence=VSP_038208, VSP_038209;
CC Name=3; Synonyms=Peri C;
CC IsoId=Q8CGN5-3; Sequence=VSP_038206, VSP_038207;
CC Name=4; Synonyms=Peri D;
CC IsoId=Q8CGN5-4; Sequence=VSP_038204, VSP_038205;
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 -!- 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; AY161165; AAN77870.1; -; mRNA.
DR EMBL; AK031445; BAC27409.1; -; mRNA.
DR EMBL; CH466543; EDL07055.1; -; Genomic_DNA.
DR EMBL; BC096685; AAH96685.1; -; mRNA.
DR CCDS; CCDS21385.1; -. [Q8CGN5-1]
DR RefSeq; NP_001106942.1; NM_001113471.1. [Q8CGN5-1]
DR RefSeq; NP_783571.2; NM_175640.2. [Q8CGN5-1]
DR RefSeq; XP_011249078.1; XM_011250776.2. [Q8CGN5-1]
DR AlphaFoldDB; Q8CGN5; -.
DR BioGRID; 222244; 1.
DR STRING; 10090.ENSMUSP00000032762; -.
DR iPTMnet; Q8CGN5; -.
DR PhosphoSitePlus; Q8CGN5; -.
DR jPOST; Q8CGN5; -.
DR MaxQB; Q8CGN5; -.
DR PaxDb; Q8CGN5; -.
DR PeptideAtlas; Q8CGN5; -.
DR PRIDE; Q8CGN5; -.
DR ProteomicsDB; 289682; -. [Q8CGN5-1]
DR ProteomicsDB; 289683; -. [Q8CGN5-2]
DR ProteomicsDB; 289684; -. [Q8CGN5-3]
DR ProteomicsDB; 289685; -. [Q8CGN5-4]
DR Antibodypedia; 15811; 388 antibodies from 37 providers.
DR DNASU; 103968; -.
DR Ensembl; ENSMUST00000032762; ENSMUSP00000032762; ENSMUSG00000030546. [Q8CGN5-1]
DR Ensembl; ENSMUST00000178257; ENSMUSP00000136996; ENSMUSG00000030546. [Q8CGN5-1]
DR Ensembl; ENSMUST00000205915; ENSMUSP00000146028; ENSMUSG00000030546. [Q8CGN5-1]
DR GeneID; 103968; -.
DR KEGG; mmu:103968; -.
DR UCSC; uc009hyu.2; mouse. [Q8CGN5-1]
DR UCSC; uc009hyw.1; mouse. [Q8CGN5-3]
DR CTD; 5346; -.
DR MGI; MGI:1890505; Plin1.
DR VEuPathDB; HostDB:ENSMUSG00000030546; -.
DR eggNOG; ENOG502RY3Q; Eukaryota.
DR GeneTree; ENSGT00950000182920; -.
DR HOGENOM; CLU_037212_1_0_1; -.
DR InParanoid; Q8CGN5; -.
DR OMA; KDTISCP; -.
DR OrthoDB; 1437332at2759; -.
DR PhylomeDB; Q8CGN5; -.
DR TreeFam; TF325901; -.
DR BioGRID-ORCS; 103968; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q8CGN5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8CGN5; protein.
DR Bgee; ENSMUSG00000030546; Expressed in epididymal fat pad and 79 other tissues.
DR ExpressionAtlas; Q8CGN5; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IDA:MGI.
DR GO; GO:0070417; P:cellular response to cold; IDA:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IMP:MGI.
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; Endoplasmic reticulum; Lipid droplet;
KW Lipid metabolism; Phosphoprotein; Reference proteome.
FT CHAIN 1..517
FT /note="Perilipin-1"
FT /id="PRO_0000099885"
FT REGION 195..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..321
FT /note="Required for interaction with CIDEC"
FT /evidence="ECO:0000269|PubMed:23481402"
FT REGION 425..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..318
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43884"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43884"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43884"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43884"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19921680,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60240"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43884"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19921680"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24945349,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 199..244
FT /note="APSSGRQRTQKAPKAKPSLVRRVSTLANTLSRHTMQTTAWALKQGH -> GI
FT CHPDWLAILGARWPLSTRGSVGGIQVLLALLWDRGYPSASSGNS (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:11641724"
FT /id="VSP_038204"
FT VAR_SEQ 245..517
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11641724"
FT /id="VSP_038205"
FT VAR_SEQ 326..347
FT /note="ALPNPRGLLGGVVHTVQNTLRN -> KTESPRPHSPRLGGEKEGNGIE (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11641724"
FT /id="VSP_038206"
FT VAR_SEQ 348..517
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11641724"
FT /id="VSP_038207"
FT VAR_SEQ 406..421
FT /note="LPRLSLMEPESEFRDI -> VSPAPGAPSDSQGFRD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11641724"
FT /id="VSP_038208"
FT VAR_SEQ 422..517
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11641724"
FT /id="VSP_038209"
FT CONFLICT 3
FT /note="M -> I (in Ref. 2; AAN77870)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="E -> D (in Ref. 3; BAC27409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 55596 MW; 906AE1CC5AFD65AE CRC64;
MSMNKGPTLL DGDLPEQENV LQRVLQLPVV SGTCECFQKT YNSTKEAHPL VASVCNAYEK
GVQGASNLAA WSMEPVVRRL STQFTAANEL ACRGLDHLEE KIPALQYPPE KIASELKGTI
STRLRSARNS ISVPIASTSD KVLGATLAGC ELALGMAKET AEYAANTRVG RLASGGADLA
LGSIEKVVEF LLPPDKESAP SSGRQRTQKA PKAKPSLVRR VSTLANTLSR HTMQTTAWAL
KQGHSLAMWI PGVAPLSSLA QWGASAAMQV VSRRQSEVRV PWLHNLAASQ DESHDDQTDT
EGEETDDEEE EEESEAEENV LREVTALPNP RGLLGGVVHT VQNTLRNTIS AVTWAPAAVL
GTVGRILHLT PAQAVSSTKG RAMSLSDALK GVTDNVVDTV VHYVPLPRLS LMEPESEFRD
IDNPSAEAER KGSGARPASP ESTPRPGQPR GSLRSVRGLS APSCPGLDDK TEASARPGFL
AMPREKPARR VSDSFFRPSV MEPILGRAQY SQLRKKS
