LTN1_DROME
ID LTN1_DROME Reviewed; 1747 AA.
AC Q9VW09; Q8T3L4;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase listerin;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q04781};
DE AltName: Full=Listerin E3 ubiquitin protein ligase 1 {ECO:0000303|PubMed:25128630, ECO:0000312|FlyBase:FBgn0262517};
DE AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000305};
GN Name=Ltn1 {ECO:0000303|PubMed:25128630, ECO:0000312|FlyBase:FBgn0262517};
GN Synonyms=l(3)76BDr {ECO:0000312|FlyBase:FBgn0262517};
GN ORFNames=CG32210 {ECO:0000312|FlyBase:FBgn0262517};
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=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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, AND IDENTIFICATION BY
RP 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.
RX PubMed=25128630; DOI=10.1016/j.biochi.2014.08.001;
RA Kashima I., Takahashi M., Hashimoto Y., Sakota E., Nakamura Y., Inada T.;
RT "A functional involvement of ABCE1, eukaryotic ribosome recycling factor,
RT in nonstop mRNA decay in Drosophila melanogaster cells.";
RL Biochimie 106:10-16(2014).
CC -!- FUNCTION: E3 ubiquitin-protein ligase component of the ribosome quality
CC control complex (RQC), a ribosome-associated complex that mediates
CC ubiquitination and extraction of incompletely synthesized nascent
CC chains for proteasomal degradation (PubMed:25128630). Ubiquitination
CC leads to TER94/VCP recruitment for extraction and degradation of the
CC incomplete translation product (By similarity).
CC {ECO:0000250|UniProtKB:O94822, ECO:0000250|UniProtKB:Q04781,
CC ECO:0000269|PubMed:25128630}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q04781};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC),
CC composed of at least the E3 ubiquitin ligase l(3)76BDr/LTN1 and
CC Clbn/NEMF. The complex probably also contains TCF25 as well as
CC TER94/VCP and its ubiquitin-binding cofactors. RQC forms a stable
CC complex with 60S ribosomal subunits. {ECO:0000250|UniProtKB:O94822,
CC ECO:0000250|UniProtKB:Q04781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O94822}.
CC -!- SIMILARITY: Belongs to the LTN1 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49146.2; -; Genomic_DNA.
DR EMBL; AY094955; AAM11308.1; -; mRNA.
DR RefSeq; NP_730427.1; NM_168802.2.
DR AlphaFoldDB; Q9VW09; -.
DR SMR; Q9VW09; -.
DR STRING; 7227.FBpp0074742; -.
DR iPTMnet; Q9VW09; -.
DR PaxDb; Q9VW09; -.
DR PRIDE; Q9VW09; -.
DR EnsemblMetazoa; FBtr0074974; FBpp0074742; FBgn0262517.
DR GeneID; 40127; -.
DR KEGG; dme:Dmel_CG32210; -.
DR UCSC; CG32210-RA; d. melanogaster.
DR CTD; 26046; -.
DR FlyBase; FBgn0262517; Ltn1.
DR VEuPathDB; VectorBase:FBgn0262517; -.
DR eggNOG; KOG0803; Eukaryota.
DR GeneTree; ENSGT00390000016055; -.
DR HOGENOM; CLU_002412_0_0_1; -.
DR InParanoid; Q9VW09; -.
DR OMA; CRNNFVY; -.
DR OrthoDB; 19753at2759; -.
DR PhylomeDB; Q9VW09; -.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 40127; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40127; -.
DR PRO; PR:Q9VW09; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0262517; Expressed in brain and 14 other tissues.
DR Genevisible; Q9VW09; DM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:1990112; C:RQC complex; IBA:GO_Central.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR CDD; cd16491; RING-CH-C4HC3_LTN1; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039795; LTN1/Rkr1.
DR InterPro; IPR039804; RING-CH-C4HC3_LTN1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12389; PTHR12389; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1747
FT /note="E3 ubiquitin-protein ligase listerin"
FT /id="PRO_0000404572"
FT REPEAT 65..102
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 106..144
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 346..383
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 424..461
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 508..547
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 612..653
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 664..711
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 789..825
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 952..989
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1005..1042
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1053..1090
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1129..1166
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1216..1258
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1269..1307
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1330..1363
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1364..1400
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REPEAT 1500..1539
FT /note="HEAT 17"
FT /evidence="ECO:0000255"
FT ZN_FING 1697..1744
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 70
FT /note="Q -> L (in Ref. 3; AAM11308)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="E -> D (in Ref. 3; AAM11308)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="P -> T (in Ref. 3; AAM11308)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="M -> L (in Ref. 3; AAM11308)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="E -> D (in Ref. 3; AAM11308)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="N -> H (in Ref. 3; AAM11308)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="R -> K (in Ref. 3; AAM11308)"
FT /evidence="ECO:0000305"
FT CONFLICT 1324
FT /note="V -> I (in Ref. 3; AAM11308)"
FT /evidence="ECO:0000305"
FT CONFLICT 1344
FT /note="V -> A (in Ref. 3; AAM11308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1747 AA; 198640 MW; 2A83E5E4F18DB5B4 CRC64;
MGGKTKQAPR TKNNAKPSSS SRTAELLGSS TPIFVGFSAQ TDGGGLVPFA PGFASAEQMP
DSFDAAISPQ TQIILRKLSK KDPMTKKKAL QELHELIEQS DVEVLKNILP LWPKYYLNLA
SDPEHTVREQ TQTVLQLLMA KCKKAMAPYL KLLVPVWLGS RFDTYAPAAS IASQSFRDTF
AGNANRSREV CMHCQVEILE YATRNLTFHT AATLSIGKSL TPEDAEQKYQ RVIISSLKLL
SFFMGQTAQT EELSQVKEGF GTLVAHQKFW SFAKHKVPAI KAAWFECIYH ILQSVALLDV
ITPQKTQLTN LCFQFIDDAD PVVAPHIWGC VLLLQSNYVD WFVPLNIRKT LLPKLSSLLQ
NGFNRNAQAI CPNLLPFLSK VTQASLQDLD IYDFYQRFFD DMKLAVTKKF DPPLSKSDCI
VIHNAYFECL RFLMQQINNN KQREQKEEEF SFSLLDNNVL EPIAWLLKSD STHVKIFFQH
SSALVAFWDR QINNRLDNGD LYAKLLNKFW IRIFELVTQD LSAEEVNEQL LGHVLLLVQD
LHMANPSLES PSVKFVEGPN EKIEKSEPTT PVKKAQEAAA FIQKELKQLV IKLVRICLDK
ANKGSGSGTS SSRYIEQIRT LTKMFNDAAF YKSLTDDGDL ASALNKFVSL LGQLSCQACE
SVVEIVFEIL PLLETGKRFE YIENTLMKLP QHGVQNLLLH RLLSYPLCAE AAVRQMLSGP
ETCEMIARIA EEVVVDNDRE KLNLLHKCFF QTDTGDILIN AKTVDKILLS MCGPLEQPVV
DDAVEVCGSF IAQIMPVICS NNNSSLHVRQ HIFLKLFKFS LEHRPEDYLS EDTLWEITTC
WQDGLSSKDI EIDDDMLKCC AGIVEELANS AELKADTLDG MAEAMAKFVI CSTENIEDEY
KRLERIDETL TALLETPLKT TDKVQQFENH CVLLEALHGS VTAGVPFENA CLSRNEILPL
LQRSTLNFST IYKLVYQFPP PQDTNDPEDE LTEDYCDPNA DVLKKWNEPL IAELLQCIRV
AGTAECWLEM SVLQSSTEEL VLILSEKVQS FMGNSSDLVA IVKERLQQAA VQQSSVIDCR
LLSYLRFCPQ YAAFEESASI LLHEDLSENL VTQGALKTYV IALQFLLPKL SQKAITLSSA
IMGTEPPEIW VKAAVFHALL LNNFEGDVNE QTDRNIIVSA VQFMTSIGER QASQKDLLHY
NVEIQRQPYE SVINTVEFIK LLTEVLKRFP YELSIKNWDA IRIGLSSWVL SVSKSIAQYQ
DPKTSLFIVA VYELFAALID FIRSEKQKSS TELLKNMIDE WDSLFAKEVN LVLFKSYYLL
THEVSVDPGF QACYEALLEQ ITPVIERLDY SFVYSFCKSN SNITLDHLCN FLFKQLYSVQ
HSVRLSAVHS LRQLTPHFVA DDIELNEKQS ESLDASTTIC KWHFLNRFED YLTRYDALIT
KYLEEFTFKL SELDDLEPID RHNALSYLFL WDCIINACAK SPVALRAVYT NWLNDNKYEE
NFLHFLFRAM PVDILKNHGA KVHSNGVYKE LTWSQQKDRH LPLERYACHL YTEVLRKLPA
VVRRWWNATQ SRQKNFIDNL TTNYVSSLIC SEELKAIANR KEKHENMQVT VHSSTREVLA
VYAIDEARME LVITLAPNYP LGAVKVECGK QIGGRASSRN VGMQLTIFLT HQNGTIYDGL
TMWKNNLDKK FEGVEECYVC YTVIHQETCQ LPKLTCKTCK KKFHGPCLYK WFTTSSKSTC
PICRNVF
