LSD2_DROME
ID LSD2_DROME Reviewed; 352 AA.
AC Q9VXY7;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Lipid storage droplets surface-binding protein 2;
DE Short=Lsd2;
GN Name=Lsd-2 {ECO:0000312|EMBL:AAF48419.1}; ORFNames=CG9057;
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:AAF48419.1}
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:0000305, ECO:0000312|EMBL:AAF48419.1}
RP GENOME REANNOTATION.
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 [3] {ECO:0000312|EMBL:AAL25281.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL25281.1};
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).
RN [4] {ECO:0000305}
RP 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 [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12676093; DOI=10.1016/s0960-9822(03)00175-1;
RA Groenke S., Beller M., Fellert S., Ramakrishnan H., Jaeckle H.,
RA Kuehnlein R.P.;
RT "Control of fat storage by a Drosophila PAT domain protein.";
RL Curr. Biol. 13:603-606(2003).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=14550535; DOI=10.1016/s0925-4773(03)00158-8;
RA Teixeira L., Rabouille C., Roerth P., Ephrussi A., Vanzo N.F.;
RT "Drosophila Perilipin/ADRP homologue Lsd2 regulates lipid metabolism.";
RL Mech. Dev. 120:1071-1081(2003).
CC -!- FUNCTION: Essential for embryogenesis. Required for normal deposition
CC of neutral lipids in the oocyte. {ECO:0000269|PubMed:12676093,
CC ECO:0000269|PubMed:14550535}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12077142,
CC ECO:0000269|PubMed:12676093, ECO:0000269|PubMed:14550535}. Lipid
CC droplet {ECO:0000269|PubMed:12077142, ECO:0000269|PubMed:12676093,
CC ECO:0000269|PubMed:14550535}. Note=Cytoplasm and on surface of neutral
CC lipid storage droplets in oocytes. Colocalizes with Lsd-1 to the
CC droplet surface in cells of fat bodies. {ECO:0000269|PubMed:14550535}.
CC -!- TISSUE SPECIFICITY: Ubiquitous expression in early embryos. At stage 5
CC expression is restricted to the pole cells. At stage 11 expression is
CC seen in the amnioserosa, refined to the fat body and midgut by stage
CC 14. Also seen in the hindgut by the end of embryogenesis. Expression is
CC seen in larval fat body (at protein level).
CC {ECO:0000269|PubMed:12676093, ECO:0000269|PubMed:14550535}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed throughout development with highest zygotic expression in
CC third instar larva and pupae. {ECO:0000269|PubMed:12676093,
CC ECO:0000269|PubMed:14550535}.
CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48419.1; -; Genomic_DNA.
DR EMBL; AY060242; AAL25281.1; -; mRNA.
DR RefSeq; NP_572996.1; NM_132768.3.
DR AlphaFoldDB; Q9VXY7; -.
DR SMR; Q9VXY7; -.
DR BioGRID; 58792; 12.
DR IntAct; Q9VXY7; 187.
DR PRIDE; Q9VXY7; -.
DR DNASU; 32437; -.
DR EnsemblMetazoa; FBtr0073967; FBpp0073784; FBgn0030608.
DR GeneID; 32437; -.
DR KEGG; dme:Dmel_CG9057; -.
DR CTD; 32437; -.
DR FlyBase; FBgn0030608; Lsd-2.
DR VEuPathDB; VectorBase:FBgn0030608; -.
DR GeneTree; ENSGT00950000182920; -.
DR HOGENOM; CLU_064803_1_0_1; -.
DR InParanoid; Q9VXY7; -.
DR OMA; ENDMPVP; -.
DR Reactome; R-DME-9706019; RHOBTB3 ATPase cycle.
DR BioGRID-ORCS; 32437; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Lsd-2; fly.
DR GenomeRNAi; 32437; -.
DR PRO; PR:Q9VXY7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030608; Expressed in cleaving embryo and 36 other tissues.
DR ExpressionAtlas; Q9VXY7; baseline and differential.
DR Genevisible; Q9VXY7; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; IGI:FlyBase.
DR GO; GO:0034389; P:lipid droplet organization; IMP:UniProtKB.
DR GO; GO:0031887; P:lipid droplet transport along microtubule; IMP:FlyBase.
DR GO; GO:0019915; P:lipid storage; IMP:FlyBase.
DR GO; GO:0006869; P:lipid transport; IEP:UniProtKB.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IMP:FlyBase.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IGI:FlyBase.
DR GO; GO:0051049; P:regulation of transport; IMP:FlyBase.
DR GO; GO:0030730; P:sequestering of triglyceride; IMP:FlyBase.
DR InterPro; IPR004279; Perilipin.
DR Pfam; PF03036; Perilipin; 1.
DR PIRSF; PIRSF036881; PAT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Lipid droplet; Lipid transport;
KW Reference proteome; Transport.
FT CHAIN 1..352
FT /note="Lipid storage droplets surface-binding protein 2"
FT /id="PRO_0000099895"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 352 AA; 38229 MW; 422B7811B07F8952 CRC64;
MASAEQKHAT GNGTTGNGTA MNDVDQPKDA KDLLPHLESL ERIIKLPVVN AAWDKSQDVY
GKVKGKNRVF EWALTAAEDC VTRAVTTAAP FVTKLDRPIA YVDQTLVKGI DKLEVKAPII
KDTPQEIYNQ AKSKVIDVVQ PHLERVVKFK AAGQQKAASL KDLAWQKANE VLATQYGSLA
VNGVDTTTAL AERLLEYYFP KCESDVEEDN DDKQNAVVQN GKSSENDMPV PASEDPVLHT
VQTVGRLSNK ISRRVYRNVS RQIKQVQKGN INDYLSSLIA ALKLHQYINF INSSMGTNVE
QSGGSSSDAC SPFGTTTSTT TTTTTSSTSN NKPVVALPHV AKSKRAPAVS SQ
