ID F7F0V7_CALJA Unreviewed; 1811 AA.
AC F7F0V7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 64.
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:ENSCJAP00000015502.5};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000015502.5, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000015502.5}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000015502.5}
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 STRING; 9483.ENSCJAP00000015502; -.
DR Ensembl; ENSCJAT00000016376.5; ENSCJAP00000015502.5; ENSCJAG00000008373.5.
DR eggNOG; KOG0803; Eukaryota.
DR GeneTree; ENSGT00390000016055; -.
DR HOGENOM; CLU_002412_0_0_1; -.
DR InParanoid; F7F0V7; -.
DR OMA; IYGSHWE; -.
DR TreeFam; TF314286; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008225; Chromosome 21.
DR Bgee; ENSCJAG00000008373; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:Ensembl.
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:0051865; P:protein autoubiquitination; IEA:Ensembl.
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 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:UP000008225};
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 1760..1807
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 568..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1811 AA; 205553 MW; 0AE4CE3FE4027923 CRC64;
MGGKNKQRTK GNLRRRGFAM LPRLVLNFRA QVIYPPWPLK SVGITGMSHP ALLPSNSGRA
AELLAKEQGT VPGFIGFGTS HNDLGYVPAI QGAEEIDSLV DSDFRMVLRK LSKKDVTTKL
KAMQEFGTMC TERDTETVKG VLPYWPRIFC KISLDHDRRV REATQQAFEK LILKVKKQLA
PYLKSLMGYW LMAQCDTYTP AAFAAKDAFE AAFPPSKQPE AIAFCKDEIT SVLQDHLLKE
TPDTLSDPQT VPEEEREAKF YRVVTCSLLA LKKLLCLLPD NELHSLEEKI KSLLSQNKFW
KYGKHSVPQI RSAYFELVSA LCQRIPQLMK EEASKVSPSV LLSIDDSDPI VCPALWEAVL
YTLTTIQDCW LHVNAKKSVF PKLSTVIREG GRGLATVIYP YLLPFISKLP QSITDPKLDF
FKNFLTSVVA GLSTEKTKTS SSESSAVISA FFECLRFIMQ QNLGEEEIEQ MLVNDQLIPF
IDAVLKDPRL QHGQLFNHLA ETLSSWEAKA DTEKDEKTAH NLENVLIHFW ERLSEICIAK
INEPEANAES VLGVSNLLQV LQKPESSLKS NKKKNGKVRF ADETPESNKG SEKCVSSEGE
NIEGWELSTE PSLTHNSEDS KSEDFLSPLR KKPLEVLVCK LAEMSINYVN EQKSEQHLRF
LSTLLDSFSS SQVFKMLLGD EKQSIGQAKP PEIAKLAQKN PAVQFLYQKL IGWLNEDQRK
DSGFLVDILY SALRCCDNDM ERKKVLDDLT KVDLKWNSLL KIIEKACSSS DKHALVTPWL
KGDILGEKLV DLADRLCNNK DLKSRVSSES HFSERWTLLS LVLSQHVKND YLIGDVYVER
IIVKLHETLF KTKKLSEAEN SDSSVSFICD VAYNYFSSAK GCLLMPSSED LLLTLFQLCA
QSKEKTHMPD FLICKLKNTW LSGVNLLVHQ TDSTYKESTF LHLSALWLKN QVQASSLDIN
SLQVLLSAVD DLLNTLLESE DSYLMGVYIG SVMPSNNEWE KMRQSLPMQW LHRPLLEGRL
SLNYECFKTD FKEQDIKTLP SHLCTSALLS KMVLIALRKK IVLENNELEK IIGELLYSLQ
WCEELDNPPV FLTGFCEMLQ KMNITYDNLR VLGNTSGLLQ LLFNRSREHG TLWSLIIAKL
ILSRSISSDE VKPHYKRKEG FFPLTEGNLH TIQSLCPFLS KEEKKEFSAQ CIPALFAWTK
KDLCSTNGGF GHLAIFNSCL QTRSIDDGEL LHGILKIIMS WKKEHEDIFL FSCNLSEASP
EVLGVNIEII RFLSLFLKYC TSPLAESEWD FIMCSMLAWL ETTSENQALY SVPLVQLFAC
VSCDLACDLS AFFDSTTLDT SGSLPINLIS EWKEFFSQGI HSLLLPILVT VTGENKDMSE
TSFQNAMLKP MCETLTYISK EQLLSHKLPA RLVADQKTNL PEYLQTLLNT LAPLLLFRAR
PVQIAVYRML YKLMPELPQY DQDNLKSYGD EEEEPALSPP AALMSLLSTQ EDLLENVLGC
IPVGQIVTIK PLSEDFCYVL GYLLTWKLIL TFFKAASSQL RALYSMYLRK TKSLNKLLYH
LFRLMPENPT YAETAIEVPN KDPKTFFTEE LQLSIRETAT LPYHIPHLAC SVYHMTLKDL
PAMVRLWWNS SEKRVFNIVD RFTSKYVSNV LSFQEISSVQ TSTQLFNGMT VKARATTREV
MATYTIEDIV IELIIQLPSN YPLGSITVES GKRVGVAVQQ WRNWMLQLST YLTHQNGSIM
EGLALWKNNV DKRFEGVEDC MICFSVIHGF NYSLPKKACR TCKKKFHSAC LYKWFTSSNK
STCPLCRETF F
//
