LSD1_DROME
ID LSD1_DROME Reviewed; 431 AA.
AC Q9VCI3; Q7KS41; Q9BIJ6; Q9VCI1; Q9VCI2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Lipid storage droplets surface-binding protein 1;
GN Name=Lsd-1 {ECO:0000312|EMBL:AAF56183.2}; ORFNames=CG10374;
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:0000305, ECO:0000312|EMBL:AAK27222.1}
RP NUCLEOTIDE SEQUENCE (ISOFORM C), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12077142; DOI=10.1074/jbc.m204410200;
RA Miura S., Gan J.-W., Brzostowski J., Parisi M.J., Schultz C.J., Londos C.,
RA Oliver B., Kimmel A.R.;
RT "Functional conservation for lipid storage droplet association among
RT Perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila,
RT and Dictyostelium.";
RL J. Biol. Chem. 277:32253-32257(2002).
RN [2] {ECO:0000312|EMBL:AAF56183.2}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF56183.2}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAK92860.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK92860.1};
RC TISSUE=Head {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).
CC -!- FUNCTION: Required for normal deposition of neutral lipids in the
CC oocyte. {ECO:0000303|PubMed:12077142}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12077142}. Lipid
CC droplet {ECO:0000269|PubMed:12077142}. Note=Cytoplasmic and in lipid
CC storage droplets of adipocytes of first instar larvae. Colocalizes with
CC Lsd-2 on the surface of neutral lipid storage droplets in cells of fat
CC bodies.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VCI3-1; Sequence=Displayed;
CC Name=B {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VCI3-2; Sequence=VSP_051638, VSP_051639;
CC Name=C {ECO:0000269|PubMed:12077142};
CC IsoId=Q9VCI3-3; Sequence=VSP_051639;
CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
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DR EMBL; AF357214; AAK27222.1; -; mRNA.
DR EMBL; AE014297; AAF56182.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF56183.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF56184.2; -; Genomic_DNA.
DR EMBL; AY051436; AAK92860.1; -; mRNA.
DR RefSeq; NP_001262883.1; NM_001275954.1. [Q9VCI3-3]
DR RefSeq; NP_651183.3; NM_142926.4. [Q9VCI3-3]
DR RefSeq; NP_732904.2; NM_170092.3. [Q9VCI3-1]
DR RefSeq; NP_732905.2; NM_170093.3. [Q9VCI3-2]
DR AlphaFoldDB; Q9VCI3; -.
DR BioGRID; 67748; 10.
DR IntAct; Q9VCI3; 1.
DR STRING; 7227.FBpp0083846; -.
DR iPTMnet; Q9VCI3; -.
DR PaxDb; Q9VCI3; -.
DR PRIDE; Q9VCI3; -.
DR DNASU; 42810; -.
DR EnsemblMetazoa; FBtr0084455; FBpp0083846; FBgn0039114. [Q9VCI3-1]
DR EnsemblMetazoa; FBtr0084456; FBpp0083847; FBgn0039114. [Q9VCI3-3]
DR EnsemblMetazoa; FBtr0084457; FBpp0083848; FBgn0039114. [Q9VCI3-2]
DR EnsemblMetazoa; FBtr0335002; FBpp0307010; FBgn0039114. [Q9VCI3-3]
DR GeneID; 42810; -.
DR KEGG; dme:Dmel_CG10374; -.
DR CTD; 42810; -.
DR FlyBase; FBgn0039114; Lsd-1.
DR VEuPathDB; VectorBase:FBgn0039114; -.
DR eggNOG; ENOG502QRYF; Eukaryota.
DR InParanoid; Q9VCI3; -.
DR OMA; ISTDQDQ; -.
DR PhylomeDB; Q9VCI3; -.
DR Reactome; R-DME-9706019; RHOBTB3 ATPase cycle.
DR BioGRID-ORCS; 42810; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42810; -.
DR PRO; PR:Q9VCI3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039114; Expressed in capitellum (Drosophila) and 27 other tissues.
DR ExpressionAtlas; Q9VCI3; baseline and differential.
DR Genevisible; Q9VCI3; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0032994; C:protein-lipid complex; IDA:FlyBase.
DR GO; GO:0034389; P:lipid droplet organization; IMP:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IEP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEP:UniProtKB.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IBA:GO_Central.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:FlyBase.
DR GO; GO:1990044; P:protein localization to lipid droplet; IMP:FlyBase.
DR GO; GO:0010883; P:regulation of lipid storage; IMP:FlyBase.
DR GO; GO:0006642; P:triglyceride mobilization; IMP:FlyBase.
DR InterPro; IPR004279; Perilipin.
DR Pfam; PF03036; Perilipin; 1.
DR PIRSF; PIRSF036881; PAT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Lipid droplet; Lipid transport;
KW Reference proteome; Transport.
FT CHAIN 1..431
FT /note="Lipid storage droplets surface-binding protein 1"
FT /id="PRO_0000099894"
FT REGION 397..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_051638"
FT VAR_SEQ 172..198
FT /note="VKKLVSALNDNFSPIRQQLNRMFGHKS -> G (in isoform C and
FT isoform B)"
FT /evidence="ECO:0000303|PubMed:12077142,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_051639"
SQ SEQUENCE 431 AA; 48833 MW; F0F90B246F51692C CRC64;
MATATSGSGL HLEAIDRIGS IPLVESSVKR VETIYDKVKN NNRLFSWYFE TAEATISAAY
ETIQPAVKLF EPSIQRLDNV MCKSLDILEQ RIPLVYLPPE MMYWNTKEYM SDHLVRPVLK
RADSVKQIGN AVLESPLTTY AAERIDGAFT VGDKFVDKYL VPIQTDQDQT DVKKLVSALN
DNFSPIRQQL NRMFGHKSPQ EDDNEAVPDE RGAIKAIHHG QRFSRKLKRR LTQRTIAEAR
ALKKQSKEAI HVLFYAAELI ATDPKQAVQK AKELWVYLSA DEPENQARPA TLEQLIVLLT
RESARRVVHL VNFSAHVAAN IPRNLAHTTT EVAHHIIYIN HRIITISRLD KVKTISKEEA
ESLFKRMLAF YGSLQGLTNA YLERVASFLS GRMEAEKVTG SDGGNSNHRS SRRRQDPNHY
SATHNNINGV Y
