LTV1_DROME
ID LTV1_DROME Reviewed; 493 AA.
AC Q7KN79; A0A0B4LF59;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein LTV1 homolog {ECO:0000303|PubMed:25858587};
DE AltName: Full=Low temperature viability protein 1 {ECO:0000303|PubMed:25858587, ECO:0000312|FlyBase:FBgn0027525};
DE AltName: Full=Ribosome biogenesis factor LTV1 {ECO:0000312|FlyBase:FBgn0027525};
GN Name=LTV1 {ECO:0000303|PubMed:25858587, ECO:0000312|FlyBase:FBgn0027525};
GN ORFNames=CG7686 {ECO:0000312|FlyBase:FBgn0027525};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345; SER-369; SER-370;
RP SER-424 AND SER-427, 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).
RN [5]
RP FUNCTION, INTERACTION WITH RPS3, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=25858587; DOI=10.1074/jbc.m114.607036;
RA Kim W., Kim H.D., Jung Y., Kim J., Chung J.;
RT "Drosophila Low Temperature Viability Protein 1 (LTV1) Is Required for
RT Ribosome Biogenesis and Cell Growth Downstream of Drosophila Myc (dMyc).";
RL J. Biol. Chem. 290:13591-13604(2015).
CC -!- FUNCTION: Necessary for the biogenesis of 40S ribosome subunits by
CC regulating pre-rRNA processing. Non-ribosomal factor required for
CC efficient nuclear export of the ribosomal 40S subunit. Necessary for
CC endoreplication driven by Myc. {ECO:0000269|PubMed:25858587}.
CC -!- SUBUNIT: Interacts with RpS3; the interaction is RNA-independent.
CC Associates with free 40S ribosome subunits.
CC {ECO:0000269|PubMed:25858587}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25858587}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the larval body and salivary glands.
CC {ECO:0000269|PubMed:25858587}.
CC -!- DISRUPTION PHENOTYPE: Lethal at the second larval stage because of
CC defects in pre-rRNA processing. RNAi-mediated knockdown in fat body
CC cells results in accumulation of RpS2 and the pre-40S ribosome in the
CC nucleus and overall decreased cell and nucleus size. RNAi-mediated
CC knockdown in wing imaginal disk results in caspase-dependent cell-
CC death. {ECO:0000269|PubMed:25858587}.
CC -!- SIMILARITY: Belongs to the LTV1 family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58742.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56098.1; -; Genomic_DNA.
DR EMBL; AF132172; AAD34760.1; -; mRNA.
DR RefSeq; NP_001286300.1; NM_001299371.1.
DR RefSeq; NP_610620.1; NM_136776.4.
DR AlphaFoldDB; Q7KN79; -.
DR BioGRID; 61953; 3.
DR IntAct; Q7KN79; 1.
DR STRING; 7227.FBpp0087340; -.
DR iPTMnet; Q7KN79; -.
DR PaxDb; Q7KN79; -.
DR DNASU; 36146; -.
DR EnsemblMetazoa; FBtr0088245; FBpp0087340; FBgn0027525.
DR EnsemblMetazoa; FBtr0339475; FBpp0308558; FBgn0027525.
DR GeneID; 36146; -.
DR KEGG; dme:Dmel_CG7686; -.
DR UCSC; CG7686-RA; d. melanogaster.
DR CTD; 84946; -.
DR FlyBase; FBgn0027525; LTV1.
DR VEuPathDB; VectorBase:FBgn0027525; -.
DR eggNOG; KOG2637; Eukaryota.
DR GeneTree; ENSGT00390000002789; -.
DR HOGENOM; CLU_035718_0_0_1; -.
DR InParanoid; Q7KN79; -.
DR OMA; HPVVMQC; -.
DR OrthoDB; 917248at2759; -.
DR PhylomeDB; Q7KN79; -.
DR BioGRID-ORCS; 36146; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG7686; fly.
DR GenomeRNAi; 36146; -.
DR PRO; PR:Q7KN79; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0027525; Expressed in second segment of antenna (Drosophila) and 24 other tissues.
DR Genevisible; Q7KN79; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IDA:FlyBase.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:FlyBase.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:FlyBase.
DR GO; GO:0006364; P:rRNA processing; IMP:FlyBase.
DR InterPro; IPR007307; Ltv1.
DR PANTHER; PTHR21531; PTHR21531; 1.
DR Pfam; PF04180; LTV; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..493
FT /note="Protein LTV1 homolog"
FT /id="PRO_0000302820"
FT REGION 42..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 437..468
FT /evidence="ECO:0000255"
FT COMPBIAS 44..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 493 AA; 57223 MW; B59F442FA30BC58C CRC64;
MVKGKKPYID RKKAVTFHLV HRSQHDPLVT DENAPQRVLL EAAARQQKPK DPEPPTDPAQ
RQEELKKFGI HFDDDYDYMQ HLKKRENDVV WEFMENPNQA RKQKVQDSEK PGPAPKLMLP
SSVFASEFEE SEGMLNKAAP QTLRLDWDPD VVAALDSDCE NEELEDDFVI QAMAEGDSDD
EEWDDEDGEE QSDMDFDSDD LNEDENEDEL MDRLAPLMRE RRFDDEEVKS RFTEYSMSSS
VIRRNEQLSL LDDRFEKFYA TYDDPELGDL ALEDIEGNWH QKHPVVMQCF QEFKKKDKGI
EYNKEWDRER IEKYRNVVEG EEDPTEELVE YEVDDPKQKK WDCESILSTY SNIYNHPKVI
DEPRRSRRSS ASTNPAPIQI DPKTGLPTNV LRGGVDGQLT AKALANLADE SPAATGPKSL
CAKSVLSTLS VLSIRPKDET HEEKKERKRL LKDYRNERRI EKKANTEAFK EEKKRQTHVK
INQRTNQQGA SIV
