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Lamin-B receptor (dLBR)

 LBR_DROME               Reviewed;         741 AA.
Q8MLV1; Q0E8Z1; Q709R7; Q9W2D2;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-OCT-2017, entry version 111.
RecName: Full=Lamin-B receptor;
AltName: Full=dLBR;
Name=LBR {ECO:0000312|FlyBase:FBgn0034657}; ORFNames=CG17952;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:CAE54809.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, SUBCELLULAR
LOCATION, AND INTERACTION WITH LAM.
PubMed=15054108; DOI=10.1242/jcs.01052;
Wagner N., Weber D., Seitz S., Krohne G.;
"The lamin B receptor of Drosophila melanogaster.";
J. Cell Sci. 117:2015-2028(2004).
[2] {ECO:0000312|EMBL:AAM71015.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000305, ECO:0000312|EMBL:AAM71015.1}
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000305, ECO:0000312|EMBL:AAL48033.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5] {ECO:0000305, ECO:0000312|EMBL:AAZ86740.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; THR-135; SER-144;
SER-223; SER-225; THR-234; THR-237; SER-243; SER-246; SER-248;
SER-250; SER-263; THR-266; SER-284; THR-288; SER-291; THR-293;
SER-298; SER-640 AND SER-642, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Anchors the lamina and the heterochromatin to the inner
nuclear membrane. {ECO:0000269|PubMed:15054108}.
-!- SUBUNIT: Interacts directly with LAM.
{ECO:0000269|PubMed:15054108}.
-!- SUBCELLULAR LOCATION: Nucleus inner membrane
{ECO:0000269|PubMed:15054108}; Multi-pass membrane protein
{ECO:0000269|PubMed:15054108}; Nucleoplasmic side
{ECO:0000269|PubMed:15054108}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=C {ECO:0000269|PubMed:15054108};
IsoId=Q8MLV1-1; Sequence=Displayed;
Name=A {ECO:0000303|PubMed:12537572}; Synonyms=B
{ECO:0000303|PubMed:12537572};
IsoId=Q8MLV1-2; Sequence=VSP_051851;
Note=No experimental confirmation available. {ECO:0000305};
-!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000255}.
-!- CAUTION: Unlike other members of this family, it does not possess
sterol C14 reductase activity. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ606680; CAE54809.1; -; mRNA.
EMBL; AE013599; AAM71015.1; -; Genomic_DNA.
EMBL; AE013599; AAF46760.2; -; Genomic_DNA.
EMBL; AY070562; AAL48033.1; -; mRNA.
EMBL; BT023819; AAZ86740.1; -; mRNA.
RefSeq; NP_611608.1; NM_137764.3. [Q8MLV1-2]
RefSeq; NP_726114.1; NM_166484.2. [Q8MLV1-1]
RefSeq; NP_726115.1; NM_166485.2. [Q8MLV1-2]
UniGene; Dm.6462; -.
ProteinModelPortal; Q8MLV1; -.
BioGrid; 63107; 4.
IntAct; Q8MLV1; 4.
MINT; MINT-1740287; -.
STRING; 7227.FBpp0071630; -.
iPTMnet; Q8MLV1; -.
PaxDb; Q8MLV1; -.
PRIDE; Q8MLV1; -.
EnsemblMetazoa; FBtr0071711; FBpp0071628; FBgn0034657. [Q8MLV1-2]
EnsemblMetazoa; FBtr0071712; FBpp0071629; FBgn0034657. [Q8MLV1-2]
EnsemblMetazoa; FBtr0071713; FBpp0071630; FBgn0034657. [Q8MLV1-1]
GeneID; 37482; -.
KEGG; dme:Dmel_CG17952; -.
CTD; 3930; -.
FlyBase; FBgn0034657; LBR.
eggNOG; KOG1435; Eukaryota.
eggNOG; ENOG410XP67; LUCA.
GeneTree; ENSGT00390000000417; -.
InParanoid; Q8MLV1; -.
KO; K19532; -.
OMA; MPSRKFA; -.
OrthoDB; EOG091G0F22; -.
PhylomeDB; Q8MLV1; -.
Reactome; R-DME-191273; Cholesterol biosynthesis.
ChiTaRS; LBR; fly.
GenomeRNAi; 37482; -.
PRO; PR:Q8MLV1; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0034657; -.
Genevisible; Q8MLV1; DM.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0005639; C:integral component of nuclear inner membrane; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
GO; GO:0005637; C:nuclear inner membrane; IDA:FlyBase.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0005521; F:lamin binding; IPI:UniProtKB.
GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
GO; GO:0006997; P:nucleus organization; IC:UniProtKB.
GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
InterPro; IPR001171; Ergosterol_biosynth_ERG4_ERG24.
Pfam; PF01222; ERG4_ERG24; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; DNA-binding; Membrane;
Nucleus; Phosphoprotein; Receptor; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 741 Lamin-B receptor.
/FTId=PRO_0000207512.
TRANSMEM 308 328 Helical. {ECO:0000255}.
TRANSMEM 363 383 Helical. {ECO:0000255}.
TRANSMEM 402 422 Helical. {ECO:0000255}.
TRANSMEM 429 449 Helical. {ECO:0000255}.
TRANSMEM 497 517 Helical. {ECO:0000255}.
TRANSMEM 543 563 Helical. {ECO:0000255}.
TRANSMEM 577 599 Helical. {ECO:0000255}.
TRANSMEM 604 624 Helical. {ECO:0000255}.
TRANSMEM 687 707 Helical. {ECO:0000255}.
MOD_RES 111 111 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 135 135 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 234 234 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 237 237 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 250 250 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 263 263 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 266 266 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 288 288 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 293 293 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 642 642 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 1 25 Missing (in isoform A).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:12537572}.
/FTId=VSP_051851.
CONFLICT 52 52 S -> T (in Ref. 1 and 5). {ECO:0000305}.
CONFLICT 67 67 G -> A (in Ref. 1 and 5). {ECO:0000305}.
CONFLICT 317 317 F -> L (in Ref. 1 and 5). {ECO:0000305}.
CONFLICT 408 408 S -> G (in Ref. 1 and 5). {ECO:0000305}.
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


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