LTN1_XENTR
ID LTN1_XENTR Reviewed; 1696 AA.
AC A0JM49;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=E3 ubiquitin-protein ligase listerin;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O94822};
DE AltName: Full=RING finger protein 160;
DE Short=Zfp-294;
DE AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000305};
GN Name=ltn1; Synonyms=rnf160;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 vcp/p97 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:O94822};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:O94822}.
CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC),
CC composed of at least the E3 ubiquitin ligase LTN1 and NEMF associated
CC with the 60S ribosomal subunit. The complex probably also contains
CC TCF25 as well as VCP/p97 and its ubiquitin-binding cofactors.
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; BC125737; AAI25738.1; -; mRNA.
DR RefSeq; NP_001072745.1; NM_001079277.1.
DR AlphaFoldDB; A0JM49; -.
DR SMR; A0JM49; -.
DR STRING; 8364.ENSXETP00000060508; -.
DR PaxDb; A0JM49; -.
DR GeneID; 780202; -.
DR KEGG; xtr:780202; -.
DR CTD; 26046; -.
DR Xenbase; XB-GENE-1217544; ltn1.
DR eggNOG; KOG0803; Eukaryota.
DR InParanoid; A0JM49; -.
DR OrthoDB; 19753at2759; -.
DR Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:1990112; C:RQC complex; ISS:UniProtKB.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR CDD; cd16491; RING-CH-C4HC3_LTN1; 1.
DR Gene3D; 3.30.40.10; -; 1.
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 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1696
FT /note="E3 ubiquitin-protein ligase listerin"
FT /id="PRO_0000404569"
FT REPEAT 17..55
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 102..140
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 144..181
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 209..250
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 252..289
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 354..394
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 431..468
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 542..580
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 596..634
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 921..958
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 992..1029
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1108..1148
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1150..1188
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1245..1282
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1307..1344
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1371..1405
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REPEAT 1406..1442
FT /note="HEAT 17"
FT /evidence="ECO:0000255"
FT ZN_FING 1645..1692
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 1696 AA; 191061 MW; C2880DB8074F279E CRC64;
MQEFGFMCKE REMETVRGVL PYWPRIYCKI SLDLDRRVRE ATQQAFEQLI LKVKKYLAPH
LKSLMGFWLI AQCDTYSPAA SSARVAFEAA FPAHKQPEAL AFCKEEIMNV LLDHLLKETP
DTLSDTQAVP IEDRESKYFR VVTCSLLALK RLLCMLPRSE NSSLQERLAH LLSQSKFWKY
SKHSTSSIRS AFFELMSALC QCSPDVLRAE ASRLCPAVLL SIDDSDAVVC PALWEAVLYT
ITTIEDCWEH VNAQKGVLPK LWSVLREGGR GLATVIFPNL LPFISRVPTN IIKTPTDFYS
NFFNSLGQGL SSERAVASPA ECSAIISAYM ECLRFAMQEN AGEEEENKKV QQILISDQLM
PLIDSSLKDP KLQNSPLFSQ VEETLYSWEK KAESQGLDDK LSRIHATLLR EFWENLAHIC
VSHVDVIEAG EKNLAGVSGL LQVLQNPNCL LKVNKKKKAK IRFKGEGDDE SDAVSHVSES
QPMSKFIMET CSSSGRDPGI AQLRQERLED LVCKLAELSM VYISEQRSQQ HLMFLAALLS
TFPSIRVFQV LLQQSSEEDP KNLNSPDHDV TPRHKNPAVQ FLYAKLIFWF NDKSLEESDF
LVDILYSVLF CCTDSSERKH LLDDMTKMNF KWSVFLYIIQ KACTDPEKYS LASDWLKGEV
LGERLICLAN DLCTSGLMDK ATPSEAYCSK KWALLSLVLS EHVHNEYLIA DAYVEKIINK
LHSALMKARN LSKAGHLEQS VSFICDVGSN FFSSIKGCLQ MPSAEDLLLT IFQLCAQASD
TSHMSESLLL KLKNTWLAGL HSLVCQYKNM PQGSNFLKQS AQWVKDQIQT SHLNVKSLQS
LICTVDDLYS TILDSSLSGF SLLAEHTASM MPSAETWQKM RHALSSQWLS KPLLEGRLSM
NTETSGTDLK SFPKTWLPSH LCTASLLSKM ALRLLEKEKS LKEEEIGVKI NITVAEMLYS
LQWCEELEKP PTLIGECCEM LCSLGVSHEK VMDLSVHLPG LLELLYNRSK EDGSLWSLTA
NRFIHKRGAG PSELLPLTED TEKYFPVTLG SLHTIQSLSA FLCPELKEEL VIQCTARLMT
CSASAVSCTD GGFGYLAIIN SCLGSDSDLC QEILPGVLKV MLSWKDDQED IFLFSSNVQD
SSQSLIGLNV EMIRFLSILL KYLASSVSSL VDVDWDFIMC SMLAWLESAC ESSAAYHIPL
VRLFACASCD LATEISHYFE SVATSTTMSL PANLMSEWKE FFSEGIYSLM LPMLVRIAEE
YKASETSHMS HVLKSLGRTL GYISKEQLLN HKLPAKFVAG QKTNLTDSLQ SLLNTLAPLL
LYRERSVQIT VYHLLDKIMA DLPGFDDEDL KSYGDEDEEP ALSPPAALMS VLAIQEDLVE
SILKEIPVGE FAVIEPLKEE FCFVLGYLLT WKLILTFFKA ASSQLRALYS QYLRKTKSLN
KLLYNLFKLM PHNPVLPGQA SDMPSKEPKT FFTEELQLAV KGTATVQQEV PHLACCVYHM
TLKDLPAMVR LWWNGCEKRI FNVVDRFTTK YVSSVLSSQE ISSVQLSTQV FDGMTVKARS
TTREVIATYS VDDICIELII QLPQNYPLGS ITVESGRRVG VAVQQWRNWM LQLNTYLTHQ
NGSIMEGLAL WKNNVDKRFE GVEDCMICFS VIHGSNYSLP KKACRTCKKK FHSECLYKWF
TSSNKSTCPL CRETFF
