LTN1_CAEEL
ID LTN1_CAEEL Reviewed; 1446 AA.
AC Q65XX2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 ORFNames=Y54E10A.11;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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: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 vcp/p97 and its ubiquitin-
CC binding cofactors. RQC forms a stable complex with 60S ribosomal
CC subunits. {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; FO081614; CCD72830.1; -; Genomic_DNA.
DR RefSeq; NP_491118.2; NM_058717.5.
DR AlphaFoldDB; Q65XX2; -.
DR SMR; Q65XX2; -.
DR BioGRID; 37370; 4.
DR STRING; 6239.Y54E10A.11; -.
DR EPD; Q65XX2; -.
DR PaxDb; Q65XX2; -.
DR PeptideAtlas; Q65XX2; -.
DR PRIDE; Q65XX2; -.
DR EnsemblMetazoa; Y54E10A.11.1; Y54E10A.11.1; WBGene00021831.
DR EnsemblMetazoa; Y54E10A.11.2; Y54E10A.11.2; WBGene00021831.
DR GeneID; 171893; -.
DR KEGG; cel:CELE_Y54E10A.11; -.
DR UCSC; Y54E10A.11; c. elegans.
DR CTD; 171893; -.
DR WormBase; Y54E10A.11; CE37436; WBGene00021831; -.
DR eggNOG; KOG0803; Eukaryota.
DR GeneTree; ENSGT00390000016055; -.
DR HOGENOM; CLU_004730_0_0_1; -.
DR InParanoid; Q65XX2; -.
DR OMA; WHEKRNG; -.
DR OrthoDB; 19753at2759; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q65XX2; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021831; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:1990112; C:RQC complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12389; PTHR12389; 2.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 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..1446
FT /note="E3 ubiquitin-protein ligase listerin"
FT /id="PRO_0000404571"
FT REPEAT 71..108
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 115..153
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 324..361
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 363..399
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 413..450
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 630..669
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 684..721
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 1046..1083
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 1107..1144
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1165..1202
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1251..1289
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT ZN_FING 1395..1442
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 1446 AA; 165403 MW; 46AFE23502C29B7C CRC64;
MSKQQRRKGN AKNASSAAAH EYLAQGGATF VGLTPEMNIF EVASSNRLHQ VVEIDDETRI
VMKKLTKKDC QTREKGLKEL MELINTENSS IESSYEHFCG LVAQLTTDGS PTVRMLTMKV
ISQFLTKLKK SASKGLKKII PFVLFAKSDV TNGVAAAASA VIRDGFDADK KRQVVELFVP
NTFDLAAKIA EGKHELSLPA EYDASEDLET RKMRLETQSL NTFLSYIKEY GNESKLWEEP
ARKLFSNSEF IKKTFAGKKE ALKVQLLNIS YKFSDNIEVI LSNPVISTYI QASLDAQTFS
TECATAWEGI LILLPDERFH AKCSLQKGIY PRLLNLIRKK GNHWRVLKHY LLPAVSVLLQ
KLENPALITS IITSFTDNLP WQAEASMNAI HCWFCTFSDF VKWILGNDRI NLEILKDLSP
LIVEMSNQSM HFNTAEATEC ISGLIHWIIE KKVLENPAEF FDLLKTSIYE VAPPEKSRLF
ADSLTLPAKH LELAHLHGNL LSNPDVDFHI IRNLARASNS EYFEETCRNI NNFEFIENSD
RFDMLQAVEI VKLIEMKPSL SLQIKNNHVG RQLLLSENSE IWEKSLKNVP AGVFQEMVNF
WHEKRNGKAI AQAVNFLKKM GIQLDTNAAA ENVDFLISLL QSLDSKEDPE ERKNLVLKLL
SALFDAEDEP KLEHFESLKS HLNGDFEQFF EKLFANMEEE DAERVLEIAA RFDKLVGFCD
ADSRGEIAGK MILGRREFDE MSEKLHFLEL DVLTVSQHTT IITDALSRPI EHLEEKEATK
MVKELGRLAL FSVASNYNSS IHQLFAWQMI RVISALGNRY CLKFLDEELQ QLRIELEKRV
IKSEEIQKLI NDGCCCAPNF ITDTYGIPEK RQKFEEYSED MDTKIETIYL KTDTPLEYVE
KVFEASQSEN SFPLFQFDQS KKYEWLANLT FVKRFIQCGG EIFRAENLEF RDFTLCGIIT
VLDTSTDILI DSPHSFSENP LLEALTTLYL ELFVVLTDAT KRGAYSEQSV EEWNEFYTPT
IHTYCIRLFR TIRRDQQPTP FVRALLRALF VISEFPTSFS NDDDVANQEF IPELSVFKYP
AFQESCIAQA FSLFASNNEH IQLIAYSVAR LLMPIMFKLE NAAALKSNED SELPVSTNRR
KLSLPVMISK SYPKDHHNPH VGPLLLDLTL LPLENTKDSG FSQEHRVAYC DVIDPFFKNA
LNALMLDQPF EFRQVPIGCR IPKSQERAYY LESDLSASPI FFDKFASRLL FKSMTLLPAA
IRLFYKGMPN CFMPMFQETV TKYASRLLIE QELGKVREAK FEGEMKVRTV PVTGEIIAEY
VVEETKMKLT IGLPPDYPLS VPSLTLDKAI VKTDRAKKWL LQLNAYLFHQ NGAILEGIEM
WKRNVDKGVE GVEDCTICMM TVHQQTHQLP KIKCKQCKNK FHSNCLYKWF ESSNQSTCPL
CRNNFT
