LTN1_ARATH
ID LTN1_ARATH Reviewed; 1873 AA.
AC Q9FGI1;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=E3 ubiquitin-protein ligase listerin;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q04781};
DE AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000305};
GN OrderedLocusNames=At5g58410; ORFNames=MCK7.28;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Component of the ribosome
CC quality control complex (RQC), a ribosome-associated complex that
CC mediates ubiquitination and extraction of incompletely synthesized
CC nascent chains for proteasomal degradation. Ubiquitination leads to
CC CDC48 recruitment for extraction and degradation of the incomplete
CC translation product. {ECO:0000250|UniProtKB:O94822,
CC ECO:0000250|UniProtKB:Q04781}.
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 LTN1 and NEMF. The complex
CC probably also contains TCF25 as well as CDC48 and its ubiquitin-binding
CC cofactors. RQC forms a stable complex with 60S ribosomal subunits.
CC {ECO:0000250|UniProtKB:O94822, 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; AB025632; BAB10256.1; -; Genomic_DNA.
DR EMBL; AB019228; BAB10256.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED97049.1; -; Genomic_DNA.
DR RefSeq; NP_200649.1; NM_125227.2.
DR AlphaFoldDB; Q9FGI1; -.
DR STRING; 3702.AT5G58410.1; -.
DR PaxDb; Q9FGI1; -.
DR PRIDE; Q9FGI1; -.
DR EnsemblPlants; AT5G58410.1; AT5G58410.1; AT5G58410.
DR GeneID; 835954; -.
DR Gramene; AT5G58410.1; AT5G58410.1; AT5G58410.
DR KEGG; ath:AT5G58410; -.
DR Araport; AT5G58410; -.
DR TAIR; locus:2161238; AT5G58410.
DR eggNOG; KOG0803; Eukaryota.
DR HOGENOM; CLU_002223_0_0_1; -.
DR InParanoid; Q9FGI1; -.
DR OrthoDB; 19753at2759; -.
DR PhylomeDB; Q9FGI1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FGI1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGI1; baseline and differential.
DR Genevisible; Q9FGI1; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12389; PTHR12389; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1873
FT /note="E3 ubiquitin-protein ligase listerin"
FT /id="PRO_0000404574"
FT REPEAT 57..94
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 96..136
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 240..280
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 281..317
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 322..359
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 365..402
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 532..569
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 614..652
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 788..826
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 853..892
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1059..1099
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1120..1157
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1163..1203
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1310..1347
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1370..1408
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1440..1477
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REPEAT 1507..1544
FT /note="HEAT 17"
FT /evidence="ECO:0000255"
FT REPEAT 1612..1649
FT /note="HEAT 18"
FT /evidence="ECO:0000255"
FT REPEAT 1676..1714
FT /note="HEAT 19"
FT /evidence="ECO:0000255"
FT ZN_FING 1823..1870
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1873 AA; 208744 MW; 777F4E6E620854EA CRC64;
MGKPKGDAAR SKARPSSSSL AASLLPSGSA AAVGFGGYVG SSRFQTSLSN EDSASFLDLD
SEVAQHLQRL SRKDPTTKIK ALASLSELVK QKQGKELLPI IPQWTFEYKK LILDYSRDVR
RATHDVMTNV VTGAGRDIAP HLKSIMGPWW FSQFDLASEV SQAAKSSFQV GSSFGNSVFL
VEAAFPAQEK RLHALNLCSA EIFAYLEENL KLTPQNLSDK SLASDELEEM YQQMISSSLV
GLATLLDILL REPDNTGSAN INSESKLASK ARAVATSSAE KMFSSHKCFL NFLKSESPSI
RSATYSLLSS FIKNVPEVFG EGDVRSLAPA LLGVFRENNP TCHSSMWEAV LLFSKKFPQS
WVYLNVHKSV LNHLWQFLRN GCYGSPQVSY PALILFLEVM PAQSVESDKF FVNFFKNLLA
GRSMCESSST DQLSLLRATT ECFLWGLRNA SRYCDVPNSI HDLQVDLIDK VLVKILWADF
TELSKGSIPP NQRKSAENLG MGNSVSYLQE LGRCILEILS GINLLEQNLL SFFCKAVQES
FLNMLQQGDL EIVAGSMRKM IDFLLLLERY SVLEGESWPL HQFMGPLLSK AFPWIRSSEL
LDGVKLLSVS VSVFGPRKVV PVLIDDIETS TLLSVEKEKN MSPEKLIKVF QEIFIPWCMD
GYDSSTAARQ DLLFSLLDDE CFTQQWSDVI SYVFNQQHQG FNNLAAMKML LEKARDEITK
RSSGQELNQR IGSRPEHWHH TLIESTAISL VHSSSATTTS AVQFLCSVLG GSTQDSSISF
VSRSSLVLIY RGILEKLLSF IKQSPLCSVN DTCSSLIVEA IAFDSSSSVD VIVVAKFAAE
VIDGSFFSLK SLSQDATLLT TVLSSIFIID LENRMTSLVD NTLSESKEKR KDRNFVCDYV
HAVCSKMDNQ FWKSINYDVR KSSASTLAQF LRSVVLLEDD LQPFELTLLC ASRMTEVLEY
LSLDQSDEEN ICGLLLLESD AWPIWVSPSS SASIDTHGMP VQLCELRKSK SQRYVSFIDS
LIMKLGIHRF IVGHKDHGFA SQAWLSVEIL CTWEWPGGKV QTSFLPNLVS FCKDEPSSGG
LLNSIFDILL NGALVHVKDE EEGLGNMWVD FNNNIVDVVE PFLRALVSFL HILFKEDLWG
EEEAMAAFKM ITDKLFIGEE TSKNCLRIIP YIMSIIISPL RTKVKSGGSG KDTLLPLEVL
LRNWLERSLS FPPLVLWQSG EDIQDWFQLV ISCYPVSDKA EEAKELQRHL STEERTLLLD
LFRKQKQDPG ASTVVTQLPA VQILLARLIM IAVSYCGNDF NEDDWDFVFS NLKRLIQSAV
VVMEETSENV NDFISGVSSM EKEKENDTLE GLGHIVFISD PSINSAQNAL SAFSLLNALV
NHKSVEGEDN LKSLADETWD PVKDRILEGV LRLFFCTGLT EAIAASYSPE AASIVASFRV
DHLQFWELVA HLVVDSSPRA RDRAVRAVEF WGLSRGSISS LYAIMFSSNP IPSLQLAAYT
VLSTEPISRL AIVADLNAPL NDESLNDQDS SNAGLPSEDK LLLRDEVSCM VEKLDHELLD
TDLTAPERVQ TFLAWSLLLS NVNSLPSLTQ GRERLVQYIE KTANPLILDS LFQHIPLELY
MGQSLKKKDG DIPSELSVVA SAATRAIITG SSLSTVESLW PIETGKMASL AGAIYGLMLR
VLPAYVREWF SEMRDRSASS LIEAFTRTWC SPSLIKNELS QIKKADFNDE SFSVSISKAA
NEVVATYTKD ETGMDLVIRL PVSYPLKPVD VNCAKSIGIS EAKQRKWLMS MQMFVRHQNG
ALAEAIRIWK RNSDKEFEGV EDCPICYSVI HIGNHSLPRR ACVTCKYKFH KACLDKWFYT
SNKKLCPLCQ SPC
