BSCL2_MOUSE
ID BSCL2_MOUSE Reviewed; 383 AA.
AC Q9Z2E9; Q3TY41; Q3U1S5; Q810B0; Q9JJC2; Q9JMF1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Seipin;
DE AltName: Full=Bernardinelli-Seip congenital lipodystrophy type 2 protein homolog;
GN Name=Bscl2 {ECO:0000312|MGI:MGI:1298392};
GN Synonyms=Gng3lg {ECO:0000312|EMBL:AAC77923.2}; ORFNames=MNCb-2630;
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] {ECO:0000305, ECO:0000312|EMBL:AAC77923.2}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAC77923.2};
RC TISSUE=Brain {ECO:0000312|EMBL:AAC77923.2};
RX PubMed=9790771; DOI=10.1006/geno.1998.5508;
RA Downes G.B., Copeland N.G., Jenkins N.A., Gautam N.;
RT "Structure and mapping of the G protein gamma3 subunit gene and a
RT divergently transcribed novel gene, Gng3lg.";
RL Genomics 53:220-230(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA95071.1}
RP SEQUENCE REVISION TO N-TERMINUS.
RA Downes G.B., Gautam N.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:BAA92759.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAA92759.1};
RX PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA Inoue S., Sano H., Ohta M.;
RT "Growth suppression of Escherichia coli by induction of expression of
RT mammalian genes with transmembrane or ATPase domains.";
RL Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAA95071.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAA95071.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAA95071.1};
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow macrophage, Dendritic cell, and Visual cortex;
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 [6] {ECO:0000312|EMBL:AAH61689.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Brain, and Olfactory epithelium {ECO:0000312|EMBL:AAH61689.1};
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18458148; DOI=10.2337/db08-0184;
RA Payne V.A., Grimsey N., Tuthill A., Virtue S., Gray S.L., Dalla Nora E.,
RA Semple R.K., O'Rahilly S., Rochford J.J.;
RT "The human lipodystrophy gene BSCL2/seipin may be essential for normal
RT adipocyte differentiation.";
RL Diabetes 57:2055-2060(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19574402; DOI=10.1210/en.2009-0236;
RA Chen W., Yechoor V.K., Chang B.H., Li M.V., March K.L., Chan L.;
RT "The human lipodystrophy gene product Berardinelli-Seip congenital
RT lipodystrophy 2/seipin plays a key role in adipocyte differentiation.";
RL Endocrinology 150:4552-4561(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, Pancreas, Spleen, and 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 [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21551454; DOI=10.1093/hmg/ddr205;
RA Cui X., Wang Y., Tang Y., Liu Y., Zhao L., Deng J., Xu G., Peng X., Ju S.,
RA Liu G., Yang H.;
RT "Seipin ablation in mice results in severe generalized lipodystrophy.";
RL Hum. Mol. Genet. 20:3022-3030(2011).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22269949; DOI=10.1128/mcb.06465-11;
RA Chen W., Chang B., Saha P., Hartig S.M., Li L., Reddy V.T., Yang Y.,
RA Yechoor V., Mancini M.A., Chan L.;
RT "Berardinelli-seip congenital lipodystrophy 2/seipin is a cell-autonomous
RT regulator of lipolysis essential for adipocyte differentiation.";
RL Mol. Cell. Biol. 32:1099-1111(2012).
RN [12]
RP POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23049863; DOI=10.1371/journal.pone.0045790;
RA Garfield A.S., Chan W.S., Dennis R.J., Ito D., Heisler L.K., Rochford J.J.;
RT "Neuroanatomical characterisation of the expression of the lipodystrophy
RT and motor-neuropathy gene Bscl2 in adult mouse brain.";
RL PLoS ONE 7:E45790-E45790(2012).
RN [13]
RP INDUCTION.
RX PubMed=30901948; DOI=10.3390/cells8030268;
RA Castro I.G., Eisenberg-Bord M., Persiani E., Rochford J.J., Schuldiner M.,
RA Bohnert M.;
RT "Promethin Is a Conserved Seipin Partner Protein.";
RL Cells 8:0-0(2019).
CC -!- FUNCTION: Plays a crucial role in the formation of lipid droplets (LDs)
CC which are storage organelles at the center of lipid and energy
CC homeostasis (By similarity).In association with LDAF1, defines the
CC sites of LD formation in the ER (By similarity). Also required for
CC growth and maturation of small nascent LDs into larger mature LDs (By
CC similarity). Mediates the formation and/or stabilization of endoplasmic
CC reticulum-lipid droplets (ER-LD) contacts, facilitating protein and
CC lipid delivery from the ER into growing LDs (By similarity). Regulates
CC the maturation of ZFYVE1-positive nascent LDs and the function of the
CC RAB18-ZFYVE1 complex in mediating the formation of ER-LD contacts (By
CC similarity). Binds anionic phospholipids including phosphatidic acid
CC (By similarity). Plays an important role in the differentiation and
CC development of adipocytes (PubMed:18458148, PubMed:19574402,
CC PubMed:21551454, PubMed:22269949). {ECO:0000250|UniProtKB:Q96G97,
CC ECO:0000269|PubMed:18458148, ECO:0000269|PubMed:19574402,
CC ECO:0000269|PubMed:21551454, ECO:0000269|PubMed:22269949}.
CC -!- SUBUNIT: Undecamer (an oligomer having eleven subunits) (By
CC similarity). Oligomerization is important for its function in lipid
CC droplet formation (By similarity). Interacts with LDAF1 to form an
CC oligomeric complex (By similarity). Interacts with RAB18 (By
CC similarity). Interacts with ZFYVE1 in a RAB18-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q96G97}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19574402}; Multi-pass membrane protein
CC {ECO:0000255}. Lipid droplet {ECO:0000250|UniProtKB:Q96G97}.
CC Note=Localizes at endoplasmic reticulum-lipid droplets (ER-LD) contact
CC sites. {ECO:0000250|UniProtKB:Q96G97}.
CC -!- TISSUE SPECIFICITY: Expressed in the paraventricular nucleus of the
CC hypothalamus (PVN) and brainstem dorsal vagal complex (DVC) in oxytocin
CC and catecholaminergic neurons (at protein level). Highest expression
CC detected in subcutaneous and epididymal white adipose tissue, brown
CC adipose tissue and testis. Also expressed in brain, skeletal muscle and
CC adrenal gland, with lower levels detected in liver, heart, kidney,
CC spleen, lung and small intestine. In brain, detected in piriform
CC cortex, olfactory tubercle, islands of Calleja, lateral septal nucleus,
CC medial septal nucleus, nucleus of the vertical limb of the diagonal
CC band, nucleus of the horizontal limb of the diagonal band, preoptic
CC area, paraventricular thalamic nucleus, lateral globus pallidus,
CC supraoptic nucleus, suprachiasmatic nucleus, subfornical organ,
CC paraventricular nucleus of the hypothalamus, zona incerta, dorsomedial
CC nucleus of the hypothalamus, ventromedial nucleus of the hypothalamus,
CC arcuate nucleus of the hypothalamus, basomedial amygdaloid nucleus,
CC medial amygdaloid nucleus, medial habenular, pyramidal cell layer of
CC the hippocampus, granular layer of the dentate gyrus, posterior
CC hypothalamus, supramammilliary nucleus, premammillary nucleus, nucleus
CC of Darkschewitsch, Edinger-Westphal nucleus, ventral tegmental area,
CC dorsal raphe nucleus, periaqueductal gray, median raphe nucleus,
CC lateral parabrachial nucleus, dorsal tegmental nucleus, laterodorsal
CC tegmental nucleus, locus coeruleus, Barrington's nucleus, medial
CC vestibular nucleus, ambiguous nucleus, dorsal vagal complex and
CC hypoglossal nucleus. {ECO:0000269|PubMed:18458148,
CC ECO:0000269|PubMed:19574402, ECO:0000269|PubMed:23049863,
CC ECO:0000269|PubMed:9790771}.
CC -!- INDUCTION: Up-regulated during in vitro adipocyte differentiation.
CC {ECO:0000269|PubMed:18458148, ECO:0000269|PubMed:19574402,
CC ECO:0000269|PubMed:30901948}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice display increased early postnatal
CC mortality rate, reduction of total body fat mass, nearly total absence
CC of gonadal fat and great reduction in subcutaneous fat. Mice have
CC enlarged visceral organs, markedly steatotic liver, decreased adipocyte
CC size and number, and display decreased levels of plasma adiponectin and
CC leptin, glucose intolerance and insulin resistance but not
CC hypertriglyceridemia. {ECO:0000269|PubMed:21551454,
CC ECO:0000269|PubMed:22269949}.
CC -!- SIMILARITY: Belongs to the seipin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61689.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA95071.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE34722.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF069954; AAC77923.2; -; mRNA.
DR EMBL; AB030196; BAA92759.1; -; mRNA.
DR EMBL; AB041588; BAA95071.1; ALT_INIT; mRNA.
DR EMBL; AK151606; BAE30545.1; -; mRNA.
DR EMBL; AK155753; BAE33418.1; -; mRNA.
DR EMBL; AK158901; BAE34722.1; ALT_INIT; mRNA.
DR EMBL; AK170183; BAE41621.1; -; mRNA.
DR EMBL; BC043023; AAH43023.2; -; mRNA.
DR EMBL; BC061689; AAH61689.1; ALT_INIT; mRNA.
DR CCDS; CCDS70931.1; -.
DR RefSeq; NP_001129536.1; NM_001136064.3.
DR RefSeq; NP_001277752.1; NM_001290823.1.
DR RefSeq; NP_032170.3; NM_008144.5.
DR RefSeq; XP_006526754.1; XM_006526691.1.
DR AlphaFoldDB; Q9Z2E9; -.
DR SMR; Q9Z2E9; -.
DR BioGRID; 199989; 1.
DR STRING; 10090.ENSMUSP00000127685; -.
DR GlyConnect; 2691; 3 N-Linked glycans (1 site).
DR GlyGen; Q9Z2E9; 2 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q9Z2E9; -.
DR PhosphoSitePlus; Q9Z2E9; -.
DR EPD; Q9Z2E9; -.
DR jPOST; Q9Z2E9; -.
DR MaxQB; Q9Z2E9; -.
DR PaxDb; Q9Z2E9; -.
DR PeptideAtlas; Q9Z2E9; -.
DR PRIDE; Q9Z2E9; -.
DR ProteomicsDB; 265382; -.
DR Antibodypedia; 28672; 172 antibodies from 26 providers.
DR DNASU; 14705; -.
DR Ensembl; ENSMUST00000086058; ENSMUSP00000083224; ENSMUSG00000071657.
DR Ensembl; ENSMUST00000159634; ENSMUSP00000125422; ENSMUSG00000071657.
DR Ensembl; ENSMUST00000160556; ENSMUSP00000123976; ENSMUSG00000071657.
DR GeneID; 14705; -.
DR KEGG; mmu:14705; -.
DR UCSC; uc008gni.2; mouse.
DR CTD; 26580; -.
DR MGI; MGI:1298392; Bscl2.
DR VEuPathDB; HostDB:ENSMUSG00000071657; -.
DR eggNOG; KOG4200; Eukaryota.
DR GeneTree; ENSGT00390000011639; -.
DR HOGENOM; CLU_049458_1_1_1; -.
DR InParanoid; Q9Z2E9; -.
DR OMA; WAFEVIF; -.
DR OrthoDB; 1390748at2759; -.
DR TreeFam; TF314000; -.
DR BioGRID-ORCS; 14705; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Bscl2; mouse.
DR PRO; PR:Q9Z2E9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9Z2E9; protein.
DR Bgee; ENSMUSG00000071657; Expressed in aorta tunica adventitia and 248 other tissues.
DR ExpressionAtlas; Q9Z2E9; baseline and differential.
DR Genevisible; Q9Z2E9; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0061725; P:cytosolic lipolysis; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; IDA:MGI.
DR GO; GO:0034389; P:lipid droplet organization; IMP:MGI.
DR GO; GO:0019915; P:lipid storage; IMP:MGI.
DR GO; GO:0051651; P:maintenance of location in cell; IMP:MGI.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IMP:MGI.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IMP:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:1905693; P:regulation of phosphatidic acid biosynthetic process; IMP:MGI.
DR GO; GO:0048515; P:spermatid differentiation; IMP:MGI.
DR InterPro; IPR009617; Seipin.
DR PANTHER; PTHR21212; PTHR21212; 1.
DR Pfam; PF06775; Seipin; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..383
FT /note="Seipin"
FT /id="PRO_0000191680"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..242
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 279..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96G97"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVJ6"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVJ6"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q96G97"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 341
FT /note="A -> V (in Ref. 3; BAA92759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 43105 MW; AB185C29BC67634E CRC64;
MVNDPPVPAL LWAQEVGHVL AGRARRLMLQ FGVLFCTILL LLWVSVFLYG SFYYSYMPTV
SHLSPVHFHY RTDCDSSTAS LCSFPVANVS LAKSGRDRVL MYGQPYRVTL ELELPESPVN
QDLGMFLVTV SCYTRGGRII STSSRSVMLH YRSQLLQVLD TLLFSSLLLF GFAEQKQLLE
VELYSDYREN SYVPTTGAII EIHSKRIQMY GAYLRIHAHF TGLRYLLYNF PMTCAFVGVA
SNFTFLSVIV LFSYMQWVWG AVWPRHRFSL QVNIRQRDNS HHGAPRRISR HQPGQESTQQ
SDVTEDGESP EDPSGTEGQL SEEEKPEKRP LNGEEEQEPE ASDGSWEDAA LLTEANPPTS
ASASALAPET LGSLRQRPTC SSS
