ID W5MRH1_LEPOC Unreviewed; 1771 AA.
AC W5MRH1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=E3 ubiquitin-protein ligase listerin {ECO:0000256|ARBA:ARBA00017157, ECO:0000256|RuleBase:RU367090};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU367090};
DE AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000256|ARBA:ARBA00032366, ECO:0000256|RuleBase:RU367090};
GN Name=LTN1 {ECO:0000313|Ensembl:ENSLOCP00000010980.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000010980.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000010980.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|RuleBase:RU367090}.
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:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU367090};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367090}.
CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC).
CC {ECO:0000256|RuleBase:RU367090}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the LTN1 family. {ECO:0000256|ARBA:ARBA00007997,
CC ECO:0000256|RuleBase:RU367090}.
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DR EMBL; AHAT01013894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000010996.1; ENSLOCP00000010980.1; ENSLOCG00000008998.1.
DR GeneTree; ENSGT00390000016055; -.
DR HOGENOM; CLU_002412_0_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000008998; Expressed in bone element and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:1990112; C:RQC complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProtKB-UniRule.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd16491; RING-CH-C4HC3_LTN1; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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:SF0; E3 UBIQUITIN-PROTEIN LIGASE LISTERIN; 1.
DR PANTHER; PTHR12389; ZINC FINGER PROTEIN 294; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367090};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367090};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU367090};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367090};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1720..1767
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1771 AA; 199199 MW; 7348D4882E76CCE9 CRC64;
MGGKNKQRTK GNVRPSSSGR AAELLARERG SVPGFVGFST SSADLGYVPA VHGVEEIDSL
VDADFRMVLR KLSKRDTVTK LKAVQEFGAM CKERDSEIVK GVLPYWPRIY CKISVDHDRR
VREATQQAFE QLILKVKRNL APYLKSIMGH WLIAQCDTYS PAASAANLAF QAAFPIGKQS
EALAFCKEEV LNILQDNLLK ETPDTLSDPQ SVPEEEREAK YARLVTSSLL AVKKLLVTLP
KQEIDCLTER LTQLISQSKF WKYSKHKTSQ IRGAFFEAVT ALCERTPELI QNEGSRACPA
VLLSIDDTDP VVVPSLWEAV LHIITNIPDC WNYVNSKKGF LPKLWLLLKE GGKGLATVLH
PNLLPFISKL PSEVIDPKLE FYNTFFTSII LGLSSERAVV SPSESAAIVF ATMECLRFSL
LQNCSEEEES RKIQQMLIAD QLLPLVDCAL RNPRLQGGPL FYHVTDMLVS WEKRADSASD
SVSGDSFQRL LTDFWEGLMR LCVQQVDRTD AEEGALSGIS TLLQAMQNPG GTRKQSKKKA
VRICFSGLEG SDGKEGDVKD QPVEEEEQLP LKSGHLEELV CQLAELNMVY VNEQNSEKHL
KFLSLLVGSF SSRRLFEVLL DTHNRMEGRV LGQGGEPENC GELQSAVAQN PAVQFLLQKV
IMWLKQDHRK DTDFLVNMVF SVLHCCSTKE EKRLLLDHIT KMDLKWGILL QIIQKACADS
ATFEATSGWL KGGVLGEKLV VLAEALCDTG LKEISAMKPS HSDSWALISM ALSQHVQNES
LIGEAYVEKI IDKLHSTLTK AKNLSDAGNI EPLVSFICDV ASNFFGSVKD CLLLSSAEEL
LLTLFQLCAQ GQEITHLSDS LLQKLSHTCF TGVHSLVSCL DTDFNEGTFL HSAALWVKKQ
ILNSSFGVKS LQVLVSAVQS LAETLIKANK SSHKILEKFL SCLTPTDLEW KMMRLALPPQ
WLKYPLLSGR LRVNCEYPCL EVWKFRASLK VPSHLCASAL LGRIIFTSSS LESFHEKDSL
HLPDVKRTVS EILYALQWCE EMEYSPTVVS EYHGILQEMN ITQDRISRES GAWCDVLETL
YSRSLEEGSL WALTLAKYIE RRGPRNYDIQ NLYGTVESFF PLTEQNISTI QGLCSFLSRD
EQESLVALSI AELLRWQETS LSSIQSGRGC LAVLHCCLRS EITVDQEVLL AFLTTMMEWR
NRKEESFLFN VDLKEASPEL LALNVEMIRF LCWLSSHSPS FLKDSQWDFI LCSMLAWLET
ASENTSLYWN PWVQLFVCQT CDLIVALSEF FTAPPAAMVE LLPVNLMSEW EEFFAEGVHS
LLLPLLVKIT EEFTEPDDPL FPLPVLKALG DALSYIPVQQ LIQNKLPPRF IAGQRTNLPD
KLQTLLNTLA PLLLFKARPV QITVFQMLNK VMPQLPEFDS ESDSARSEDD EGEEPSLSPP
AALMSVFAAT EELLDNILGG VQVGEFAVVQ SLSDEYCCIL GYLLTWKLVL TFFKASSSHL
RVQYSLYLRK SKSLNKLLFH LFRLMPENPV YLSQAVEPGN KDSRTFFTES LLLSVRESDG
LKWEIPHLAC SVYYSTLKDL PAMVRLWWNG QEKRIFNTVD KFTSKYVSSV LSSQEITSVH
TSTQTFESMT VKARSATREV IATYSVDDIF IELVIQLPPN YPLGSISVES GRRVGVAVQQ
WRNWMLQLST YLTHQNGSIM EGLALWKNNV DKRFEGVEDC MICFSVIHGS NYSLPKKACR
TCKKKFHSAC LYKWFTSSNK STCPLCRETF F
//
