PLIN4_MOUSE
ID PLIN4_MOUSE Reviewed; 1403 AA.
AC O88492; E9QN72; Q69Z80; Q8BNV5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Perilipin-4;
DE AltName: Full=Adipocyte protein S3-12;
GN Name=Plin4; Synonyms=Kiaa1881;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Adipocyte;
RX PubMed=9624692; DOI=10.1038/nbt0698-581;
RA Scherer P.E., Bickel P.E., Kotler M., Lodish H.F.;
RT "Cloning of cell-specific secreted and surface proteins by subtractive
RT antibody screening.";
RL Nat. Biotechnol. 16:581-586(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1263-1403 (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12840023; DOI=10.1074/jbc.m304025200;
RA Wolins N.E., Skinner J.R., Schoenfish M.J., Tzekov A., Bensch K.G.,
RA Bickel P.E.;
RT "Adipocyte protein S3-12 coats nascent lipid droplets.";
RL J. Biol. Chem. 278:37713-37721(2003).
RN [6]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15111493; DOI=10.2337/diabetes.53.5.1243;
RA Dalen K.T., Schoonjans K., Ulven S.M., Weedon-Fekjaer M.S., Bentzen T.G.,
RA Koutnikova H., Auwerx J., Nebb H.I.;
RT "Adipose tissue expression of the lipid droplet-associating proteins S3-12
RT and perilipin is controlled by peroxisome proliferator-activated receptor-
RT gamma.";
RL Diabetes 53:1243-1252(2004).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15731108; DOI=10.1074/jbc.m500978200;
RA Wolins N.E., Quaynor B.K., Skinner J.R., Schoenfish M.J., Tzekov A.,
RA Bickel P.E.;
RT "S3-12, Adipophilin, and TIP47 package lipid in adipocytes.";
RL J. Biol. Chem. 280:19146-19155(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-31; SER-1281 AND
RP THR-1287, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, and Pancreas;
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).
CC -!- FUNCTION: May play a role in triacylglycerol packaging into adipocytes.
CC May function as a coat protein involved in the biogenesis of lipid
CC droplets. {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15731108}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9624692}.
CC Cytoplasm {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15731108}.
CC Lipid droplet {ECO:0000269|PubMed:12840023,
CC ECO:0000269|PubMed:15731108}. Note=Nascent lipid droplet surface-
CC associated; association with lipid droplets is triacylglycerol
CC synthesis-dependent. {ECO:0000269|PubMed:12840023,
CC ECO:0000269|PubMed:15731108}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88492-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88492-2; Sequence=VSP_027279, VSP_027280;
CC -!- TISSUE SPECIFICITY: Specifically expressed in white adipose tissue and
CC also weakly detected in heart and skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:12840023, ECO:0000269|PubMed:15111493,
CC ECO:0000269|PubMed:9624692}.
CC -!- INDUCTION: Up-regulated by PPARG and during adipocyte differentiation.
CC {ECO:0000269|PubMed:15111493}.
CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37834.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD32564.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF064748; AAC23666.1; -; mRNA.
DR EMBL; AK173286; BAD32564.1; ALT_INIT; Transcribed_RNA.
DR EMBL; CT009719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK080156; BAC37834.1; ALT_INIT; mRNA.
DR CCDS; CCDS79565.1; -. [O88492-1]
DR PIR; T17372; T17372.
DR RefSeq; NP_065593.2; NM_020568.3. [O88492-1]
DR AlphaFoldDB; O88492; -.
DR SMR; O88492; -.
DR BioGRID; 208292; 4.
DR IntAct; O88492; 6.
DR STRING; 10090.ENSMUSP00000139859; -.
DR iPTMnet; O88492; -.
DR PhosphoSitePlus; O88492; -.
DR SwissPalm; O88492; -.
DR jPOST; O88492; -.
DR MaxQB; O88492; -.
DR PaxDb; O88492; -.
DR PeptideAtlas; O88492; -.
DR PRIDE; O88492; -.
DR ProteomicsDB; 289618; -. [O88492-1]
DR ProteomicsDB; 289619; -. [O88492-2]
DR Antibodypedia; 23665; 120 antibodies from 30 providers.
DR DNASU; 57435; -.
DR Ensembl; ENSMUST00000002908; ENSMUSP00000002908; ENSMUSG00000002831. [O88492-1]
DR Ensembl; ENSMUST00000190703; ENSMUSP00000139859; ENSMUSG00000002831. [O88492-1]
DR GeneID; 57435; -.
DR KEGG; mmu:57435; -.
DR UCSC; uc008day.2; mouse. [O88492-1]
DR CTD; 729359; -.
DR MGI; MGI:1929709; Plin4.
DR VEuPathDB; HostDB:ENSMUSG00000002831; -.
DR eggNOG; KOG4744; Eukaryota.
DR GeneTree; ENSGT00950000182920; -.
DR HOGENOM; CLU_273270_0_0_1; -.
DR InParanoid; O88492; -.
DR OrthoDB; 71918at2759; -.
DR PhylomeDB; O88492; -.
DR TreeFam; TF328397; -.
DR BioGRID-ORCS; 57435; 2 hits in 65 CRISPR screens.
DR ChiTaRS; Plin4; mouse.
DR PRO; PR:O88492; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O88492; protein.
DR Bgee; ENSMUSG00000002831; Expressed in epididymal fat pad and 120 other tissues.
DR ExpressionAtlas; O88492; baseline and differential.
DR Genevisible; O88492; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR InterPro; IPR004279; Perilipin.
DR Pfam; PF03036; Perilipin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Lipid droplet; Membrane;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1403
FT /note="Perilipin-4"
FT /id="PRO_0000297560"
FT REPEAT 104..136
FT /note="1"
FT REPEAT 137..169
FT /note="2"
FT REPEAT 170..202
FT /note="3"
FT REPEAT 203..235
FT /note="4"
FT REPEAT 236..268
FT /note="5"
FT REPEAT 269..301
FT /note="6"
FT REPEAT 302..334
FT /note="7"
FT REPEAT 335..367
FT /note="8"
FT REPEAT 368..400
FT /note="9"
FT REPEAT 401..433
FT /note="10"
FT REPEAT 434..466
FT /note="11"
FT REPEAT 467..499
FT /note="12"
FT REPEAT 500..532
FT /note="13"
FT REPEAT 533..565
FT /note="14"
FT REPEAT 566..598
FT /note="15"
FT REPEAT 599..631
FT /note="16"
FT REPEAT 632..664
FT /note="17"
FT REPEAT 665..697
FT /note="18"
FT REPEAT 698..730
FT /note="19"
FT REPEAT 731..763
FT /note="20"
FT REPEAT 764..796
FT /note="21"
FT REPEAT 797..829
FT /note="22"
FT REPEAT 830..862
FT /note="23"
FT REPEAT 863..895
FT /note="24"
FT REPEAT 896..928
FT /note="25"
FT REPEAT 929..961
FT /note="26"
FT REPEAT 962..994
FT /note="27"
FT REPEAT 995..1027
FT /note="28"
FT REPEAT 1028..1060
FT /note="29"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..1060
FT /note="29 X 33 AA approximate tandem repeat"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1287
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 206..601
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_027279"
FT VAR_SEQ 1267..1271
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_027280"
FT CONFLICT 241
FT /note="V -> A (in Ref. 1; AAC23666)"
FT /evidence="ECO:0000305"
FT CONFLICT 1121
FT /note="Q -> H (in Ref. 1; AAC23666)"
FT /evidence="ECO:0000305"
FT CONFLICT 1258
FT /note="L -> V (in Ref. 1; AAC23666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1403 AA; 139415 MW; D1A3A8F9C787FE07 CRC64;
MSASGDGTRV PPKSKGKTLS SFFGSLPGFS SARNLVSHTH SSTSTKDLQT ATDPSGTPAP
SSKVSTNSQM AGDAAGLLQP SEQTAGDKDM GSFSVTSSED AFSGVFGIMD AAKGMVQGGL
GATQSALVGT KEAVSGGVMG AVGVAKGLVK GGLDTSKNVL TNTKDTVTTG VMGAANMAKG
TVQTGLDTTK SVVMGTKDTV ATGLAGAVNV AKGTIQGGLD TTKSVVMGTK DTVTTGLTGA
VNVAKGVVQG GLDTTKSVVM GTKDTVTTGL TGAMNVAKGT AQMGIDTSKT VLTGTKDTVC
AGATGAINVA KGAAQGGLDT TKSVLIGTKD TVTTGLTGAV NVAKGAVQGG LDTTKSVVMG
TKDTVTTGLT GAMNVAKGTA QMGLGTSKTV LTGTKDTVCA GLTGAINVAK GAAQGGLDTT
KSVLMGTKDT VTTGLTGAVN VAKGTIQGGL DTTKSVVMGT KDTVTTGLTG AVNVAKGTIQ
GGLDTTKSVV MGTKDTVTTG LTGAVNVAKG AAQGGLDTTK SVVMGTKDTV TTGLTGAMNV
AKGTAQMGLG TSKTVLTGTK DTVCAGLTGA INVAKGAAQG GLDTTKSVLM GTKDTVTTGL
TGAVNVAKGT IQGGLDTTKS VVMGTKDTVT TGLTGAVNVA KGAVQGGLDT TKSVVMGTKD
TVTTGLTGAL NVAKGTAQMG IDTSKTVLIG TKDTVCAGAT GAINMAKGAA QGGLDTTKSV
LMGTKDTVTT GLTGAINVAK GSAQGGLDTT KSVLIGTKDT VTTGLTGALN VAKGTVQTGL
DTSQRVLTGT KDNVYAGVTG AVNVAKGTIQ GGLDTTKSVV MGTKDTVTTG LTGAVNVAKG
AVQGGLDTTK SVVMGTKDTV TTGLTGAMNV AKGTAQMGID TSKTVLTGTK DTVCAGLTGA
INVAKGATQG GLDTTKSVLM GTKDTVTTGL TGAINVAKGA AQGGLDTTKS VLLGTKDTVT
TGLTGAANVA KETVQMGLDT SKNILMDTKD SICAGATGAI TVVKGAAQGG LDTSNAALTG
TMDTAKGTVQ TSLDTSKHML IGMKDTVCAG VTSAMNMAKG IHKNTDTTRD TQSSVLAHSG
NVATNAIHTG VHTVPSSLSG SHSIICHEPS IYRATNHGVG QAILTSTESL CCETSSFSDK
YGLGHVTEPR ADTKTLVSGM ASSACAATRS VEECGQLAAT GFAALPDELK GLGDIFQPMT
TEEQAQLAVS ESGPRVLSAD RGSYYIRLGD LAPSFRQRAF EHALSHIQHN QFQARAALAQ
LQEAFQMTDM TMEAACGKLC SDQSLNTMVE AVGSHEMRAS VAQDRLCTLA HQLHAAYSSL
VTSLQGLPEV QQQAGQARHS LCKLYGLVSS EAGSELQTEQ LAQSSAGVVE AWQGLEVLLE
KLQQNPPLSW LVGPFTSMPC GQL
