LTN1_CHICK
ID LTN1_CHICK Reviewed; 1766 AA.
AC E1C231;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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; AC147443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1C231; -.
DR SMR; E1C231; -.
DR STRING; 9031.ENSGALP00000025437; -.
DR PaxDb; E1C231; -.
DR PRIDE; E1C231; -.
DR VEuPathDB; HostDB:geneid_418482; -.
DR eggNOG; KOG0803; Eukaryota.
DR HOGENOM; CLU_002412_0_0_1; -.
DR InParanoid; E1C231; -.
DR OrthoDB; 19753at2759; -.
DR PhylomeDB; E1C231; -.
DR TreeFam; TF314286; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000539; 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; 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; 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 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1766
FT /note="E3 ubiquitin-protein ligase listerin"
FT /id="PRO_0000404568"
FT REPEAT 100..138
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 193..231
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 292..329
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 335..372
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 512..549
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 606..644
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 672..710
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 916..953
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 1184..1227
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1314..1355
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1406..1447
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT ZN_FING 1715..1762
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1766 AA; 199446 MW; EDD92365A975B23E CRC64;
MGGKNKQRTK GNVRPSSSGR AAELLAKERG TVPGFIGFGT SQSDLGYVPA VQGAEEIDSL
VDADFRMVLR KLSKRDIITK LKAMQEFGTM CKEREAEVVK GVLPYWPRIY CKISLDHDRR
VREATQQSFE QLILKVKKHL APYLKSIMGY WLIAQCDTYS PAASAAKEAF EKAFPSSKQP
EALAFCKDEI LNVLQDHLLK ETPDTLSDPQ TVPEEEREAK FFRILTCSLL ALKKLLSMLP
KKEMHSLEEK LMSLLSQNKF WKYGKHSTPQ VRSAFFELAS AFCQFLPELV KAEAPRVCPA
VLLSIDDSDA VVCPALWEAV LHAIATIEDC WSHVNARKGV LPKLWTVLRE GGRGLATVIY
PNILPFISKV PPGITEPKLE YFRTFFSSII QGLSNERALA SPSESSAIIT TFMECLRFAI
LQKIDEDEQR QIHQMLIYDQ LIPLTDAVLQ EPRLQNGPLF YQIAETLSSW EAKAEVSSDD
NTNEVFQKLL SNFWDRLLKM CILHVDKLEA DEKTLFAISD MLEVLQNPKT ATKPNNRKSL
KVKFSDEDES ERNTENGKIT EVRSNSDSEI QADLQHSSIL RKEPLENLVC NLAELSIVYV
NEQKSEQHLK FLSALLNFFS SNRVFQVLLE QGSNAGCPPA ESQEDMKVHN ENPSVQFLYM
NLITWLKEDW RKDMHFLVDI LYSVLNCCNS DDERKVILDD LTKMDLKWIV FLQIIQKACS
STTKLSLISE WLKGDMLGER LVMLADDLCH LGLKPIATSP ESSSSEKWTV LSLVLSQHIK
NESLIGETYV ERIIDKLQAA LSKAKDLSEA GNTEPSVSFI CDVASSFFSS VKGCLLMPSS
EDLLLTIFQL CAQRQDATHL TVDLLVCKLK HTWISGVNSL VRHLRSMQNQ STFLHKSALW
IKNQIQSSSL DVKSLQVLIS AVSDLLSTLL EADRQSGCLV GAYVEHVMPN RTEWETLRES
LSAEWMHKPL LEGRLSMNCE HLGSCVKLCG TTKLPGHLCT SALLSKMVLL VLENDMVKGN
EDAEILVAEL LYSLQWIEEL ENPPYLLLEY LHMLEEMHIT YEKFSALSNT TNLQQTIFDR
SEEHGRLWSL TMAKVIRGEN AVSREMTKLF KTSEGFLPLT EGRLHTLQCL SPFLIEEEKR
ELVFHCVAKL MTCTQTELSS TDGAFGCLAI LNSSLNDKSF GCDHLLPGVL KIIISWKNDN
EDSFLFSCNL KETSAQLLGF NIEMIRYLPL LLKYSTAPLA DNEWDFIMCS MLAWLETTSE
NYSLYHVPLV QIFACVSCDL ASALSAYFEP AAPKTTENLP VNLVSEWKEF FSEGIHNLLL
PLFVKVTGET KTAAEGSFQN SVLTSLGEAL TYISKDQLLN HKLPAKFVAG QKTNLPDNLQ
TLLNTLSPLL LFWARSVQVS VYHMLSKLMP ELPKFDDEDL KSYGDEEEEL ALSPPAALMS
VLATQELLLE NILECIPVGE FAVIQPLSDE FCLVLGYLLT WKLTLTFFKA ASSQLRVLYS
QYLRRTKSLN KLLYHLFRLM PENPVFSGLT SEVPNKDTKT FFTEELHLDV KGTGALSSQI
PHLACSVYHI TLKDLPAMVR LWWNSCEKRV FNVVDKFTSK YVSSVLSSQE ISSVQTSTQL
FNGMTVKARS AAREVIATYS VDDIFIELII QLPSNYPLGS ITVESGKRVG VAVQQWRNWM
LQLSTYLTHQ NGSIMEGLSL WKNNVDKRFE GIEDCMICFS VIHGSNYSLP KKACRTCKKK
FHSACLYKWF TSSNKSTCPL CRETFF
