ID LTN1_DICDI Reviewed; 1864 AA.
AC Q555H8;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 113.
DE RecName: Full=E3 ubiquitin-protein ligase listerin;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q04781};
DE AltName: Full=RING finger protein 160;
DE AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000305};
GN Name=rnf160; ORFNames=DDB_G0274875;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 cdcD/CDC48 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 rnf160/LTN1 and nemf. The
CC complex probably also contains tcf25 as well as cdcD/CDC48 and its
CC ubiquitin-binding cofactors. RQC forms a stable complex with 60S
CC ribosomal subunits. {ECO:0000250|UniProtKB:O94822,
CC 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; AAFI02000012; EAL70330.1; -; Genomic_DNA.
DR RefSeq; XP_644091.1; XM_638999.1.
DR AlphaFoldDB; Q555H8; -.
DR SMR; Q555H8; -.
DR STRING; 44689.Q555H8; -.
DR PaxDb; 44689-DDB0304711; -.
DR EnsemblProtists; EAL70330; EAL70330; DDB_G0274875.
DR GeneID; 8619520; -.
DR KEGG; ddi:DDB_G0274875; -.
DR dictyBase; DDB_G0274875; rnf160.
DR eggNOG; KOG0803; Eukaryota.
DR HOGENOM; CLU_002223_0_0_1; -.
DR InParanoid; Q555H8; -.
DR OMA; IYGSHWE; -.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q555H8; -.
DR Proteomes; UP000002195; Chromosome 2.
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: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; 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; SM01197; FANCL_C; 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; Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1864
FT /note="E3 ubiquitin-protein ligase listerin"
FT /id="PRO_0000404573"
FT REPEAT 100..138
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 265..303
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 349..377
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 378..418
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 598..635
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 642..668
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 669..694
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 695..733
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 800..847
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 900..937
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1021..1060
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1080..1117
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1137..1176
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1185..1223
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1271..1308
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1312..1349
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REPEAT 1599..1636
FT /note="HEAT 17"
FT /evidence="ECO:0000255"
FT REPEAT 1662..1699
FT /note="HEAT 18"
FT /evidence="ECO:0000255"
FT ZN_FING 1815..1860
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1864 AA; 213101 MW; B6106856BD4E593E CRC64;
MGKDRDKGFR GAKYNPSSSG EANTLMGSQS SGFIGFSAFS SNLTNATDPD YYQVEPEYKV
LLKKLQKKDS ISRIKGLEEL NSKFQKINIE DAEFNISSIS PLMNAWEFMY KRLVNDDDRN
VRDLASQCLG SIGSRIGKHL GPHVKQLLGP WIVAICDQND QSINNALLSF QNIFPEKKRK
DVFKFGHDEA LTYLCENLQE TPQTIGDSKS ISQEILQERY ERCISNSLLA IEYLINNTTA
TATDSSSSSS TTTTTTTTNN TGNTEIYEKI FESQFFSFFQ SKSSNIRKTA YRVLTTVIKK
LAGYVEKNFK DFSSKVLGLF SEKDSSTHLY MWDAIISFLQ QYGDKAWSNV DVRKHVLPRL
WAFLRSGCYG SFELSYPSIL PLLTFIPNSI VIGSPSPSPS PSPNTNIDIG FFKELFTNLE
KGLEVVDNPR QYGNPNSVDR PSNLLLSCYL ECLIYSSKKW GQQYQQINDY LIDTLLFNFY
NNHFNLEHSC FSEKLFIEKL LESTIKLANL SNSNLLKIQN LFNSNSFINF NNKENLLNNN
EPITTDNNNN NNNNSSPIIK KQEKIIQPIS KETLISRLNT FIIVCSNNNN SNNSNNNNVI
QVIIKRLFNL ACDNLNSNQE LSIKILDFIL GNYKIDQIIS NGLDDIKKII TQLALALNES
LLSTGGLNLG VGGDLVSVIV GLLALVPDED EIKLIWSQIL QIFLDSINNN NNNSKKKNNR
SNLITNTTNS LVHLINSASN KINRNLLLST TLFKSIKIQD KKQLQLIKSI LFNNNNNNNN
EFSPIIPNES VELLIKWVYN KLVDIINTMV QLNLVFNDND KGGDNNNDDD SDDNDVSIDY
LVELSKLLFS SRFKSKSLES LLIEWCKFNI EINNRPSLSG FKSKCNSIDE YLFSTTSNIE
NDKFILSLLI ESIDRNSSTI ITNDNLNLNF LSNCAIKLIK SGSYRHDENG DDDDDDDQLY
SYFIKEFTSN QLVINSKDQI KISWFRYNRI TPFYLLDNYG SNKDNNDSTT FSTDKLLKVL
IFNFKVIESF GLEKFIKYSN KENNNSIELL LLNLLFVNGD NQLPPTPTTT TTTTTTITTA
VVVSTNEQIL EFIENNSTNL LNQFIESLFK FYGDEIFNCN WFNCLVSNVG GDGNNGGIYS
VLLALFIDYI TSDACLPTSS MKLKSALLNS IKIDNDDNGN SIDSIRQLNL VQILLPILQK
ESIESYKQWS INQLSQLSSS IPTNFKSISI QLSILSSIVI QRQQQQHQQS QKEQQQITQD
DNEILKEKEW LTLLNLIQTI QQWNSKIKSA IIKQQEPELE FLFMKEVELS CLNFILIVIQ
YISNINSNKS KQPIYLSNNQ SQFVQSFLSI WLSNNFTLLS FNKFKSNYYY QQYRNLIEYQ
SLKIYNIIIS NDNIKFIIPG IGDQFQIDHS ILILNNWLNR VSNSRSNNNN GNTSDSSYIL
ELYSNTFMKM SNDIKYKISL TKLDNLIELL STFNYSTSIY NNKGIKKTSY NLLESYFGNE
NTQLVKSFLL ENENNNNNNN NDDGEEKVSF ILFSNIFEKI LLDFDSTFKP MKKSKDNQLI
NSISMGQLMC WNLLLLNYSK IDLNRRSILN GWLNDNNIQK VTLFLNQIFP FINKDESPLT
TTTTTTDNNG NNYSIEFPFS IIDNDQLITY RMIQKLCSNC FYSLVNYLPS MVRRWADDNS
TNSKMNQQIQ SYITRFISPI IIQNEIQRVN SYRCTDSDSS DAKFQIKGST SSKEVTASYE
KDEMTISLVL FISDNYPLRV LTVEFSKRVG VSESQWRQWL LSMTSLLLTQ DGTVLDACLL
WKNSLDKHFQ GVEVCPICYS MFHNGTIPKF QCKTCKNKFH AGCIYKWFQT SHKSNCPLCQ
TDLS
//
