LTN1_CAEBR
ID LTN1_CAEBR Reviewed; 1503 AA.
AC B6IFN4;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 55.
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=CBG25264;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE600926; CAR98714.1; -; Genomic_DNA.
DR AlphaFoldDB; B6IFN4; -.
DR SMR; B6IFN4; -.
DR STRING; 6238.CBG25264; -.
DR WormBase; CBG25264; CBP40098; WBGene00086678; -.
DR eggNOG; KOG0803; Eukaryota.
DR HOGENOM; CLU_004730_0_0_1; -.
DR InParanoid; B6IFN4; -.
DR OMA; WHEKRNG; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008549; Chromosome I.
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; 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 SMART; SM00184; RING; 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..1503
FT /note="E3 ubiquitin-protein ligase listerin"
FT /id="PRO_0000404570"
FT REPEAT 52..89
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 93..129
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 133..170
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 280..318
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 323..345
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 346..384
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 552..589
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 640..663
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 664..700
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 845..882
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1022..1065
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1078..1117
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1141..1183
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1302..1340
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT ZN_FING 1446..1499
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 1503 AA; 171887 MW; 7E46AE8F0BB3549D CRC64;
MSKQQRRKGN AKNASSASAH GYLAQGGENF VGLTPEMNIF EMASSNRLSN FSGIDDETRI
VMRKLTKKDC QTREKGLREL TNIIAETSSI ENCYEHFCGL VPQLSTDGSP TVRLLTMKTI
TLFLVKLEKS ACKGLKKIIP MVLFARCDVT NGVAAAAGAV IRDGFEADKK QKVIQLFAPL
VFEMAAKIVQ GKHDLSVPVE YDASEDREAR KSRLETQSLN VFLSYIKEFG ADSTIWEEEA
RKLFENIAFL KMVFGGTNAA LKVQVLNLAY RFKNNVEVIL NTPSIVTYIQ NHLDSQTFTP
ECSTAWEGMI ILLPSAQFHT KVSLQNGIYP RFLNVIRKKG NHWRVLQHFL LPAVVLLLKE
MGSLENNMKV LGTIMESFTD NLPWPTDASI NAVLSWFNAF SDFVRWILTN DRINLVVWEK
LHPLIVTVTE QAMTFPTKEI AECVTDLLQW IIELKTINEA DVSTLLLNIE SKIVGAGTEN
SRLIKHLLTE PGKNIVLSNL HANLLSSPEL VDFQIIKNLS CSENDYFNAT SQKISNFSFI
EKTENFDITQ AGDIVRLIKL LLENQEIKSL NISVKNDHVG RRLLLTGGST IWNKLLKNVP
VSTFQNMINY WHEKRNGTAI ADAVSFLKEM GVEMDTKQAA ENVEFLITLL RKMKSTDVSN
EAEKNVLILK LFTAIFESDE DAKSEHYNCL SEHLTSDFNS GQFFEKLFAS SEEYDIERIL
ETACRVDKLI DLCEEQTRQN IVNNVLLSGK QCGTIIEQFQ FLELEVMSCS TKPTVISTTH
QHCYSHLDEH KAKEIVTESA RIALFNISSK CECFFLISHE QFFFSDYNSA HQVFGWQVIS
IISALEKRYS LVALTEELQR SRREIEERLI RSDEVRFKLD DSSPCIFLAD AYDMSFEQKK
KYIQCQAEPS KVPEHALEVL YRENQTPLDF LMNVFEGGYQ MFDFDRSKNY HWMINLMFVK
KCIQYGGSIF VAEESGLRDY ALCGIVTVLD IHKRSTLQQS TDILGNTPNA FDEDPRLEAL
TTLFIELYLV LNDSIKNDNH PTQTIEEWKE FYVPTINSLF IRMFRMIRKE QQPTPFVRTL
LKAMFTLVEF PTNVPNDSVV TREFVPELSV FKYSLLEESF IAQAFILLSS NVEHVQLIGY
AAAKLLVPIM FKTENPQVLD DDQDETEIMV ANRSKLNLPV MISKSYPVDH IHKHVGPLLL
SLAILPLETT KEFVLNQEQR VAYCDAIDSF FKNALNALML DQPFDFSQVP IVCKIRKQMY
FFQFRYSSHF FTAKSQEREY YLQSDLTASP LFFEKFASRL LFKSITLLPA AVRLFHKNIP
NNFKPIFQEV VTKHASKLLI ENELNKVQNA EFGEVLKVRT VPVTGQIISE YTVEDTKMKL
TIELPRDYPL SVPAMNLDKA IVKGDRAKKW LLQLNAYLFH QNGAILEGIE MWKRNVDKGI
EGAEDCTICM MTVHQQTNQL PKVKCKQCKN RFHSNCLVSS FHTYKWFESS NQSTCPLCRN
NFT
