ID H2LJI4_ORYLA Unreviewed; 1761 AA.
AC H2LJI4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 69.
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:ENSORLP00000006172.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000006172.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000006172.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000006172.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000006172.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000006172.2};
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 RefSeq; XP_011481659.1; XM_011483357.1.
DR STRING; 8090.ENSORLP00000006172; -.
DR Ensembl; ENSORLT00000006173.2; ENSORLP00000006172.2; ENSORLG00000004903.2.
DR GeneID; 101155290; -.
DR KEGG; ola:101155290; -.
DR CTD; 26046; -.
DR eggNOG; KOG0803; Eukaryota.
DR GeneTree; ENSGT00390000016055; -.
DR HOGENOM; CLU_002412_0_0_1; -.
DR InParanoid; H2LJI4; -.
DR OrthoDB; 179130at2759; -.
DR TreeFam; TF314286; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001038; Chromosome 14.
DR Bgee; ENSORLG00000004903; Expressed in liver and 14 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990112; C:RQC complex; IBA:GO_Central.
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: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; 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; 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; 2.
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:UP000001038};
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 1710..1757
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1761 AA; 194742 MW; A7C2350E87795934 CRC64;
MGGKNKQRTK GNVRPSSSGR AAEVLSREGG VIPGFVGFGS TATSELSYVP AVHGAEDIDS
LVDADFRMVL RKLSKKDVVT RLKAVQDFGS MCQERDAEEV KGVLPFWPRI YCKISMDHDR
RIREATQQAF EQLVLKVRRS LAPFLKSLMG HWILSQCDTY TPAASAACQA FQAAFSPSKQ
PEALGFCKDE ILNVLQDILL NETADSLSDP QNVTAEEKEA KYLRMLTSSL LGVRTLLSLL
LPSDRAALEG RLASLLSSGK FWKYGKHKSP QVRGAFFEMV CSLCEFTPGL VQAEAGRLCP
AVLLSIDDTD PVVLPPVWEA VLHVVSTIPD CWTHVNARKA FLPKLWSVLK EGGKGMAKAL
HPNLMPLLSK LPGEVTDPSV DFYNSFFAAL TQGLSSERAL TSQSESAAIV TSFVECLKFC
VLKVADGHDR MRTVLVSQQL LPLIERALSE ASLQNGPLFY LLTDMLLSWE RKAAVSGEGE
APAASENFQS LLEDFWEDLG LLCVRYVDDE QADPRRLEGL AFLLQVMRSP ETTRTKHTQK
KKSTRICFSK LGKAETTAED GVKKPAQGTP GITNENATGA LQDGHFEDIV CQLALICLTH
VSEKNSEKHL VFLSRLLSSF HTPRVFRTLA ESGEQKSEEE EMKNNPAVRF LLERVVVWLS
ESDRSDTEPL VEMTFSSFRC CSQQEITRIL SHITTMGLPC GVLLQLIQRA CKDSETLSAC
RDWLKGSVLG QQLLELTKEL CRVGSSSRPS ASTTGGHSWT LISLVLSRNH DDESVIGDVY
LEKILEKLHA TLSETKSLSD AGNAEPLVSF ICDVASSFFS SVRGCLSLLP AEELLLTVFQ
LAAQDQRQTR LTDSVVEKLE GVCVAGVRSL VQDCDLELDE GGFLHSAAVW VKTHLLTASL
DVKSLQVLAA AVQTLIETVG SVSSQALPIL SNFLNLLMPN QTEWTRLRQA LPPQWIASAV
LSSHYRGVLD KPTRDMWTFR EFHYLPSHLC VCALLGRVAQ TAAAVSADHK EAESSLPLQH
LTSAVSELLY ALQWCREFKF SPTLVSSFHT LLTEWGLSDG RHSGLPVQPL LERLYSKSLQ
DGGLWSLTLH NFLSTNGQEG SCVAALRRLY GSADSLFPVS QSTLSTLQVI VTAMTDEHRE
TLITLATAGL INWQENDDVH GCLAVLLCCL HADAAVEEDI VKAVLATVME WRSSREDWFL
LSCDLADTAC ESVNLTVETM RLLSWVLGHH PTVLGGSQWD FVLCSLLAWL ETCSESVGSL
WNPWVQLFVS ETAALVVQLS QFFACAPSDV LQSLPPDVSA EWADFFVEGI YSLLLPLAVK
ITEAFPEPDD PAFPTAALQS VGSALTYTPL QQLLKSSLPP RFIADQKTNL PESLQTLLNT
LCPLLLFKAR PLQVTVHHLL DKVMPQLPEC DGDGDATKSD DDDGDEPCLS PPASLMAVLS
TCEELCDNIL AGVQVGEFAV VQPLSVEYSC ILGYLLAWKL LLTFFKASPS HLRAHYAQYL
KRSGSLKKLL LHLFKLMPEN PVYPGQGSET KDAKTFFTES MTLQVDQREG FEWELPHLAC
GVYYSTVQDL PAMVRLWWNS QEKKVSTAVE RFTIKYVSPV LSAQEISSVQ SSTQIFDSMT
VKARQAAREV IATYSVDDIF IELVIQLPQN YPLGSIAVDS GRRVGVAVQQ WRNWMLQLST
YLTHQNGSIM EGLALWKNNV DKRFEGIEDC MICFSVIHGS NYSLPKKACR TCKKKFHSAC
LYKWFTSSNK STCPLCRETF F
//
