LBR_DROME
ID LBR_DROME Reviewed; 741 AA.
AC Q8MLV1; Q0E8Z1; Q709R7; Q9W2D2;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Lamin-B receptor;
DE AltName: Full=dLBR;
GN Name=LBR {ECO:0000312|FlyBase:FBgn0034657}; ORFNames=CG17952;
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:CAE54809.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH LAM.
RX PubMed=15054108; DOI=10.1242/jcs.01052;
RA Wagner N., Weber D., Seitz S., Krohne G.;
RT "The lamin B receptor of Drosophila melanogaster.";
RL J. Cell Sci. 117:2015-2028(2004).
RN [2] {ECO:0000312|EMBL:AAM71015.1}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAM71015.1}
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:AAL48033.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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, ECO:0000312|EMBL:AAZ86740.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; THR-135; SER-144;
RP SER-223; SER-225; THR-234; THR-237; SER-243; SER-246; SER-248; SER-250;
RP SER-263; THR-266; SER-284; THR-288; SER-291; THR-293; SER-298; SER-640 AND
RP SER-642, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Anchors the lamina and the heterochromatin to the inner
CC nuclear membrane. {ECO:0000269|PubMed:15054108}.
CC -!- SUBUNIT: Interacts directly with LAM. {ECO:0000269|PubMed:15054108}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:15054108}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15054108}; Nucleoplasmic side
CC {ECO:0000269|PubMed:15054108}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C {ECO:0000269|PubMed:15054108};
CC IsoId=Q8MLV1-1; Sequence=Displayed;
CC Name=A {ECO:0000303|PubMed:12537572}; Synonyms=B
CC {ECO:0000303|PubMed:12537572};
CC IsoId=Q8MLV1-2; Sequence=VSP_051851;
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000255}.
CC -!- CAUTION: Unlike other members of this family, it does not possess
CC sterol C14 reductase activity. {ECO:0000305}.
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DR EMBL; AJ606680; CAE54809.1; -; mRNA.
DR EMBL; AE013599; AAM71015.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF46760.2; -; Genomic_DNA.
DR EMBL; AY070562; AAL48033.1; -; mRNA.
DR EMBL; BT023819; AAZ86740.1; -; mRNA.
DR RefSeq; NP_611608.1; NM_137764.3. [Q8MLV1-2]
DR RefSeq; NP_726114.1; NM_166484.2. [Q8MLV1-1]
DR RefSeq; NP_726115.1; NM_166485.2. [Q8MLV1-2]
DR AlphaFoldDB; Q8MLV1; -.
DR SMR; Q8MLV1; -.
DR BioGRID; 63107; 5.
DR IntAct; Q8MLV1; 4.
DR MINT; Q8MLV1; -.
DR STRING; 7227.FBpp0071630; -.
DR TCDB; 9.B.115.4.1; the steroid 5alpha-reductase/lamin b receptor (lbr) family.
DR iPTMnet; Q8MLV1; -.
DR PaxDb; Q8MLV1; -.
DR PRIDE; Q8MLV1; -.
DR DNASU; 37482; -.
DR EnsemblMetazoa; FBtr0071711; FBpp0071628; FBgn0034657. [Q8MLV1-2]
DR EnsemblMetazoa; FBtr0071712; FBpp0071629; FBgn0034657. [Q8MLV1-2]
DR EnsemblMetazoa; FBtr0071713; FBpp0071630; FBgn0034657. [Q8MLV1-1]
DR GeneID; 37482; -.
DR KEGG; dme:Dmel_CG17952; -.
DR CTD; 3930; -.
DR FlyBase; FBgn0034657; LBR.
DR VEuPathDB; VectorBase:FBgn0034657; -.
DR eggNOG; KOG1435; Eukaryota.
DR GeneTree; ENSGT00390000000417; -.
DR HOGENOM; CLU_392461_0_0_1; -.
DR InParanoid; Q8MLV1; -.
DR PhylomeDB; Q8MLV1; -.
DR Reactome; R-DME-191273; Cholesterol biosynthesis.
DR BioGRID-ORCS; 37482; 0 hits in 3 CRISPR screens.
DR ChiTaRS; LBR; fly.
DR GenomeRNAi; 37482; -.
DR PRO; PR:Q8MLV1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034657; Expressed in cleaving embryo and 20 other tissues.
DR Genevisible; Q8MLV1; DM.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005521; F:lamin binding; IPI:UniProtKB.
DR GO; GO:0006997; P:nucleus organization; IC:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:InterPro.
DR InterPro; IPR001171; ERG24_DHCR-like.
DR Pfam; PF01222; ERG4_ERG24; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Membrane; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..741
FT /note="Lamin-B receptor"
FT /id="PRO_0000207512"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 29..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 288
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 293
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:12537572"
FT /id="VSP_051851"
FT CONFLICT 52
FT /note="S -> T (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="G -> A (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="F -> L (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="S -> G (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 83185 MW; 679CD09855F07963 CRC64;
MQHSPSTTTD HIHFAARFFD RNSYTMDRRL RRPRRTEDVS SGPLLAQSKQ PSLLPVTRRT
GSVTAAGATA TATATAGPAT RTRASPSRNK VVAPPSPDLG PRTRRSSRPR SSVGPLTGSG
SGSSLPIKAA IKARTPIPEV SEVSSPIRLS TSNLPMTLTT NTSSGAPNKA FNTSSVNSGN
SFSRTTTSST TTTTERIEIR AEGDGEVDTD SIRKRITERL RRSVSKTISN LAGTPVTNTE
EGSRYSRSVS RSVYDDEKSS KRSYSTGEED IDEEDELEED QFRSFNVTRK SATPAEISCR
QLKAPREFGG WLGAFLFLLL LPTAVYYLTW SCTARNACQF KHLNLGILLD VNYLTRQVFQ
PRVVGAFAAY QVVVFLLVAL LPGRRVHLTR ETYKFNCLAV SLTLLIASGV AEYLKYPVVT
FVLRHYLRFC IFGLVGAFVA AAWSYWLVDT AKYNVLRQTL TNDYGRTGSF VVDFALGRQL
NPKWLGRVDW KQFQYRLSLV TTLIYATCYI YQTLVWPQKP QLGEQEGYLY QAKYYWNNVN
YDPATLFSAS CLLFYVLDAI IFEHHLSSSF ELQHEGYGCL LLLRYAATPY LLTAVTKYFY
EQRVPISCWY APLAVAALLS LGLLVKRFSC AYKYKYRLNS QSPIFANIET IHTYQGSRLL
LSGMWGWVRQ PNYLGDIVAL LALAAPMALR PAWPPVLGLS LIILLLLHRA TRANARNQAR
YHSSWQRYST QVRSYILPRV Y
