PLIN1_CAEEL
ID PLIN1_CAEEL Reviewed; 418 AA.
AC A8WHP8; Q23095; Q65ZB1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Perilipin-1 homolog {ECO:0000305};
DE AltName: Full=Lipid droplet-associated protein {ECO:0000305};
GN Name=plin-1 {ECO:0000303|PubMed:26357594, ECO:0000312|WormBase:W01A8.1c};
GN Synonyms=mdt-28 {ECO:0000303|PubMed:26025681,
GN ECO:0000312|WormBase:W01A8.1c};
GN ORFNames=W01A8.1 {ECO:0000312|WormBase:W01A8.1c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=26121959; DOI=10.1016/j.bbalip.2015.06.004;
RA Vrablik T.L., Petyuk V.A., Larson E.M., Smith R.D., Watts J.L.;
RT "Lipidomic and proteomic analysis of Caenorhabditis elegans lipid droplets
RT and identification of ACS-4 as a lipid droplet-associated protein.";
RL Biochim. Biophys. Acta 1851:1337-1345(2015).
RN [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26025681; DOI=10.1016/j.bbamcr.2015.05.020;
RA Na H., Zhang P., Chen Y., Zhu X., Liu Y., Liu Y., Xie K., Xu N., Yang F.,
RA Yu Y., Cichello S., Mak H.Y., Wang M.C., Zhang H., Liu P.;
RT "Identification of lipid droplet structure-like/resident proteins in
RT Caenorhabditis elegans.";
RL Biochim. Biophys. Acta 1853:2481-2491(2015).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=26357594; DOI=10.7717/peerj.1213;
RA Chughtai A.A., Kassak F., Kostrouchova M., Novotny J.P., Krause M.W.,
RA Saudek V., Kostrouch Z., Kostrouchova M.;
RT "Perilipin-related protein regulates lipid metabolism in C. elegans.";
RL PeerJ 3:E1213-E1213(2015).
CC -!- FUNCTION: Lipid droplet-associated protein which plays a role in lipid
CC droplet clustering (PubMed:26121959, PubMed:26025681, PubMed:26357594).
CC {ECO:0000269|PubMed:26025681, ECO:0000269|PubMed:26121959,
CC ECO:0000269|PubMed:26357594}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:26025681,
CC ECO:0000269|PubMed:26121959, ECO:0000269|PubMed:26357594}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|WormBase:W01A8.1c};
CC IsoId=A8WHP8-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:W01A8.1a};
CC IsoId=A8WHP8-2; Sequence=VSP_059202;
CC Name=b {ECO:0000312|WormBase:W01A8.1b};
CC IsoId=A8WHP8-3; Sequence=VSP_059202, VSP_059203, VSP_059204;
CC -!- TISSUE SPECIFICITY: Expressed in intestinal and epidermal cells
CC (PubMed:26357594). Expressed in the muscle and hypodermis
CC (PubMed:26025681). {ECO:0000269|PubMed:26025681,
CC ECO:0000269|PubMed:26357594}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryos to adults
CC (PubMed:26357594). First expressed at the 3-fold stage of embryonic
CC development (PubMed:26357594). Highly expressed in embryos
CC (PubMed:26025681). {ECO:0000269|PubMed:26025681,
CC ECO:0000269|PubMed:26357594}.
CC -!- DISRUPTION PHENOTYPE: Viable, and able to reproduce normally, but
CC embryos contain large lipid droplets (PubMed:26121959,
CC PubMed:26357594). Reduced body fat accumulation (PubMed:26121959).
CC Lipid droplets cluster in intestinal cells and contain a reduced amount
CC of triglycerides (PubMed:26025681). RNAi-mediated knockdown results in
CC a reduced brood size (PubMed:26357594). {ECO:0000269|PubMed:26025681,
CC ECO:0000269|PubMed:26357594}.
CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
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DR EMBL; BX284601; CAA95854.1; -; Genomic_DNA.
DR EMBL; BX284601; CAH19105.1; -; Genomic_DNA.
DR EMBL; BX284601; CAP16290.1; -; Genomic_DNA.
DR PIR; T26032; T26032.
DR RefSeq; NP_001021646.1; NM_001026475.3. [A8WHP8-2]
DR RefSeq; NP_001021647.1; NM_001026476.3. [A8WHP8-3]
DR RefSeq; NP_001122526.1; NM_001129054.2. [A8WHP8-1]
DR AlphaFoldDB; A8WHP8; -.
DR SMR; A8WHP8; -.
DR IntAct; A8WHP8; 1.
DR STRING; 6239.W01A8.1c.2; -.
DR EPD; A8WHP8; -.
DR PaxDb; A8WHP8; -.
DR PeptideAtlas; A8WHP8; -.
DR EnsemblMetazoa; W01A8.1a.1; W01A8.1a.1; WBGene00007024. [A8WHP8-2]
DR EnsemblMetazoa; W01A8.1b.1; W01A8.1b.1; WBGene00007024. [A8WHP8-3]
DR EnsemblMetazoa; W01A8.1b.2; W01A8.1b.2; WBGene00007024. [A8WHP8-3]
DR EnsemblMetazoa; W01A8.1c.1; W01A8.1c.1; WBGene00007024. [A8WHP8-1]
DR GeneID; 172437; -.
DR KEGG; cel:CELE_W01A8.1; -.
DR UCSC; W01A8.1c.1; c. elegans.
DR CTD; 172437; -.
DR WormBase; W01A8.1a; CE18303; WBGene00007024; plin-1. [A8WHP8-2]
DR WormBase; W01A8.1b; CE06531; WBGene00007024; plin-1. [A8WHP8-3]
DR WormBase; W01A8.1c; CE41705; WBGene00007024; plin-1. [A8WHP8-1]
DR eggNOG; ENOG502SAGX; Eukaryota.
DR InParanoid; A8WHP8; -.
DR OMA; PKNTAYE; -.
DR OrthoDB; 1441489at2759; -.
DR PRO; PR:A8WHP8; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00007024; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR InterPro; IPR004279; Perilipin.
DR Pfam; PF03036; Perilipin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipid droplet; Reference proteome.
FT CHAIN 1..418
FT /note="Perilipin-1 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000442203"
FT REGION 211..275
FT /note="Required for lipid droplet localization"
FT /evidence="ECO:0000269|PubMed:26025681"
FT VAR_SEQ 231..233
FT /note="Missing (in isoform a and isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059202"
FT VAR_SEQ 383..388
FT /note="IISAEW -> VRQQTE (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059203"
FT VAR_SEQ 389..418
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059204"
SQ SEQUENCE 418 AA; 46523 MW; C8A5FF798C37908E CRC64;
MTDVEQPVSV EDQQAQAQSY YDQVLGNAYV QTAINAYTKT KEFHPLLNST LNSAEEKVST
VGNYAAQKAY DGYNSYYVKP KNTAYEAVSY GTERAKTAVE SGKQAAIVGG TFGIGAAVVL
TQFSLALSAG GAALVLEQVD SAKKLGSSAI STIKEAELAV EHRIFSALHQ AQRIAMVPVE
KITENTNSLL DILDGAVQKG LNIEVPPSVN LTIGQRVKNL ASLIVQGVSN KLFKAHDHVI
DPINERARNY LEQLSQSFVL LDIVREKKTW VIEKSNELST SVFDFKKTLE EEAQKYKVAP
EEMLMKHIQS TSEQLSTQLQ SLREKGQNVF GDGTKIDSTI DYLENLKKNF TDAEDVYKVR
DEVLNEGRQR IAELSTWTTS LLIISAEWQF EPEDLLIEEL YFDAPPPVRT RNLYRNRA
