BSCL2_DROME
ID BSCL2_DROME Reviewed; 370 AA.
AC Q9V3X4;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Seipin {ECO:0000303|PubMed:21533227};
DE Flags: Precursor;
GN Name=Seipin {ECO:0000312|FlyBase:FBgn0040336}; ORFNames=CG9904;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF45798.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|EMBL:AAF45798.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:CAB65856.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [4] {ECO:0000312|EMBL:AAM51042.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21533227; DOI=10.1371/journal.pgen.1001364;
RA Tian Y., Bi J., Shui G., Liu Z., Xiang Y., Liu Y., Wenk M.R., Yang H.,
RA Huang X.;
RT "Tissue-autonomous function of Drosophila seipin in preventing ectopic
RT lipid droplet formation.";
RL PLoS Genet. 7:E1001364-E1001364(2011).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27564575; DOI=10.7554/elife.16582;
RA Wang H., Becuwe M., Housden B.E., Chitraju C., Porras A.J., Graham M.M.,
RA Liu X.N., Thiam A.R., Savage D.B., Agarwal A.K., Garg A., Olarte M.J.,
RA Lin Q., Froehlich F., Hannibal-Bach H.K., Upadhyayula S., Perrimon N.,
RA Kirchhausen T., Ejsing C.S., Walther T.C., Farese R.V.;
RT "Seipin is required for converting nascent to mature lipid droplets.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Acts as a tissue-autonomous lipid modulator, preventing
CC ectopic lipid accumulation in salivary gland (a non-adipose tissue) and
CC in promoting lipid storage in fat tissue (PubMed:21533227). Required
CC for the growth and maturation of small nascent lipid droplets (LDs)
CC into larger mature LDs (PubMed:27564575). {ECO:0000269|PubMed:21533227,
CC ECO:0000269|PubMed:27564575}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21533227, ECO:0000269|PubMed:27564575}; Multi-pass
CC membrane protein {ECO:0000255}. Lipid droplet
CC {ECO:0000269|PubMed:27564575}. Note=Localizes at endoplasmic reticulum-
CC lipid droplets (ER-LD) contact sites. {ECO:0000269|PubMed:27564575}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels detected in
CC fat body, moderate levels detected in salivary gland, midgut and
CC muscle, and weak expression detected in brain.
CC {ECO:0000269|PubMed:21533227}.
CC -!- DEVELOPMENTAL STAGE: At late embryonic stages, highly expressed in
CC hindgut. At larval stages, expression detected in fat body, anterior
CC midgut and salivary gland. {ECO:0000269|PubMed:21533227}.
CC -!- DISRUPTION PHENOTYPE: Flies are viable and fertile with no noticeable
CC behavior defects, but display reduced average weight. The size of the
CC lipid droplets in larval fat bodies and the fat cells of young adults
CC is significantly reduced, but exhibit ectopic lipid droplets in
CC salivary gland and gut. Flies also display greatly reduced total
CC glyceride levels and hypersensitivity to starvation.
CC {ECO:0000269|PubMed:21533227}.
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DR EMBL; AE014298; AAF45798.1; -; Genomic_DNA.
DR EMBL; AL121804; CAB65856.1; -; Genomic_DNA.
DR EMBL; AY119182; AAM51042.1; -; mRNA.
DR RefSeq; NP_570012.1; NM_130656.4.
DR PDB; 6MLU; EM; 4.00 A; A/B=2-370.
DR PDBsum; 6MLU; -.
DR AlphaFoldDB; Q9V3X4; -.
DR SMR; Q9V3X4; -.
DR BioGRID; 57776; 16.
DR IntAct; Q9V3X4; 1.
DR STRING; 7227.FBpp0070426; -.
DR PaxDb; Q9V3X4; -.
DR PRIDE; Q9V3X4; -.
DR DNASU; 31245; -.
DR EnsemblMetazoa; FBtr0070442; FBpp0070426; FBgn0040336.
DR GeneID; 31245; -.
DR KEGG; dme:Dmel_CG9904; -.
DR UCSC; CG9904-RA; d. melanogaster.
DR CTD; 31245; -.
DR FlyBase; FBgn0040336; Seipin.
DR VEuPathDB; VectorBase:FBgn0040336; -.
DR eggNOG; KOG4200; Eukaryota.
DR GeneTree; ENSGT00390000011639; -.
DR HOGENOM; CLU_049458_0_0_1; -.
DR InParanoid; Q9V3X4; -.
DR OMA; LGWNVYD; -.
DR OrthoDB; 1390748at2759; -.
DR PhylomeDB; Q9V3X4; -.
DR BioGRID-ORCS; 31245; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31245; -.
DR PRO; PR:Q9V3X4; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0040336; Expressed in adult midgut (Drosophila) and 25 other tissues.
DR Genevisible; Q9V3X4; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IMP:FlyBase.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IMP:FlyBase.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:FlyBase.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:FlyBase.
DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; IMP:FlyBase.
DR GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IGI:FlyBase.
DR GO; GO:0010884; P:positive regulation of lipid storage; IMP:FlyBase.
DR GO; GO:0046890; P:regulation of lipid biosynthetic process; IMP:FlyBase.
DR GO; GO:0010883; P:regulation of lipid storage; IMP:FlyBase.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; IMP:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR InterPro; IPR009617; Seipin.
DR PANTHER; PTHR21212; PTHR21212; 1.
DR Pfam; PF06775; Seipin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..370
FT /note="Seipin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420612"
FT TOPO_DOM 19..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..251
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 346..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 42562 MW; 4871D465BD582C59 CRC64;
MNILLRLIVF ALDPLGLGRR FLIRPAVNLG WNVYDRVRSK ADEKVGTVRE LVLRLGLIAF
AVVLIIWLAV FMYAAFYYVY MPAISHTRPV HMQFKTCLET STPCTFPHAH VSLTKKQQLL
MVGQAYKVIV NIDMPESPQN LELGMFMVCA EMRDYDSMLR GHSCRSAMMR YRSPLIRMIS
TWVLSPLYVL GWKEEFQQVP VEIFSRYLEE RQHPITDVYV EIQSQKIQFY TVTLHIVADF
TGLRYIMFNW PVLSAIVAIS TNLFFILVVF LLSWYHWSDA KWLHSVQIKY ARLTKSLEPG
VIHSKASSLR DDDDDLVAYS DKSDIADVGG DTLSDVDADD LVLVKKSRSG KRESPDALRK
RPTKKTTADH
