LTN1_MOUSE
ID LTN1_MOUSE Reviewed; 1767 AA.
AC Q6A009; E9QN94; Q6PIW6; Q8BZ44;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 137.
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 AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000305};
DE AltName: Full=Zinc finger protein 294;
DE Short=Zfp-294;
GN Name=Ltn1; Synonyms=Kiaa0714, Lister, Rnf160, Zfp294, Znf294;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1108.
RC STRAIN=C57BL/6J; TISSUE=Bone;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1314-1767.
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AUTOUBIQUITINATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19196968; DOI=10.1073/pnas.0812819106;
RA Chu J., Hong N.A., Masuda C.A., Jenkins B.V., Nelms K.A., Goodnow C.C.,
RA Glynne R.J., Wu H., Masliah E., Joazeiro C.A., Kay S.A.;
RT "A mouse forward genetics screen identifies LISTERIN as an E3 ubiquitin
RT ligase involved in neurodegeneration.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2097-2103(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase (PubMed:19196968). Component of
CC the ribosome quality control complex (RQC), a ribosome-associated
CC complex that mediates ubiquitination and extraction of incompletely
CC synthesized nascent chains for proteasomal degradation (By similarity).
CC Ubiquitination leads to Vcp/p97 recruitment for extraction and
CC degradation of the incomplete translation product (By similarity).
CC {ECO:0000250|UniProtKB:O94822, ECO:0000250|UniProtKB:Q04781,
CC ECO:0000269|PubMed:19196968}.
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 -!- TISSUE SPECIFICITY: Widely expressed, including in the brain and spinal
CC cord. {ECO:0000269|PubMed:19196968}.
CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:19196968}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality. Mice with a milder mutant
CC caused by an internal in-frame deletion of exon 11, producing a 14-
CC amino acid deletion prior to the RING-type zinc finger, display
CC profound early-onset and progressive neurological and motor
CC dysfunction. {ECO:0000269|PubMed:19196968}.
CC -!- MISCELLANEOUS: Was named listerin because of the 'tilting' or 'listing'
CC phenotype observed in mutant mice. {ECO:0000305|PubMed:19196968}.
CC -!- SIMILARITY: Belongs to the LTN1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27795.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD32287.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173009; BAD32287.1; ALT_INIT; mRNA.
DR EMBL; AC140319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK036725; BAC29552.1; -; mRNA.
DR EMBL; BC027795; AAH27795.1; ALT_INIT; mRNA.
DR CCDS; CCDS37382.1; -.
DR RefSeq; NP_001074537.1; NM_001081068.1.
DR AlphaFoldDB; Q6A009; -.
DR SMR; Q6A009; -.
DR BioGRID; 219701; 1.
DR DIP; DIP-48713N; -.
DR IntAct; Q6A009; 2.
DR MINT; Q6A009; -.
DR STRING; 10090.ENSMUSP00000038775; -.
DR iPTMnet; Q6A009; -.
DR PhosphoSitePlus; Q6A009; -.
DR EPD; Q6A009; -.
DR MaxQB; Q6A009; -.
DR PaxDb; Q6A009; -.
DR PeptideAtlas; Q6A009; -.
DR PRIDE; Q6A009; -.
DR ProteomicsDB; 293411; -.
DR Antibodypedia; 41917; 131 antibodies from 21 providers.
DR Ensembl; ENSMUST00000039449; ENSMUSP00000038775; ENSMUSG00000052299.
DR GeneID; 78913; -.
DR KEGG; mmu:78913; -.
DR UCSC; uc033gzo.1; mouse.
DR CTD; 26046; -.
DR MGI; MGI:1926163; Ltn1.
DR VEuPathDB; HostDB:ENSMUSG00000052299; -.
DR eggNOG; KOG0803; Eukaryota.
DR GeneTree; ENSGT00390000016055; -.
DR HOGENOM; CLU_002412_0_0_1; -.
DR InParanoid; Q6A009; -.
DR OMA; CRNNFVY; -.
DR OrthoDB; 19753at2759; -.
DR PhylomeDB; Q6A009; -.
DR TreeFam; TF314286; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 78913; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Ltn1; mouse.
DR PRO; PR:Q6A009; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6A009; protein.
DR Bgee; ENSMUSG00000052299; Expressed in cumulus cell and 255 other tissues.
DR ExpressionAtlas; Q6A009; baseline and differential.
DR Genevisible; Q6A009; MM.
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; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
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 SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Neurodegeneration; Reference proteome; Repeat;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1767
FT /note="E3 ubiquitin-protein ligase listerin"
FT /id="PRO_0000056305"
FT REPEAT 59..96
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 100..138
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 273..314
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 335..372
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 380..418
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 433..473
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 509..547
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 621..658
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 676..714
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1067..1104
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1183..1226
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1315..1353
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1378..1415
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1476..1513
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT ZN_FING 1716..1763
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 550..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1009..1011
FT /note="VAQ -> IAP (in Ref. 1; BAD32287)"
FT /evidence="ECO:0000305"
FT CONFLICT 1042
FT /note="A -> P (in Ref. 1; BAD32287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1767 AA; 198921 MW; EFEC1BAAD32776C6 CRC64;
MGGKNKQRTK GNLRPSNSGR AAELLAKEQG TVPGFIGFGT SHSDLGYVPA VQGAEDIDSL
VDSDFRMVLR KLSKKDVTTK LKAMQEFGIM CTERDTEAVK GVLPYWPRIF CKISLDHDRR
VREATQQAFE KLILKVKKHL APYLKSVMGY WLMAQCDTYP PAALAAKDAF EAAFPPSKQP
EAIAFCKEEI TTVLQDHLLK ETPDTLSDPQ TVPEEEREAK FHRVVTCSLL ALKRLLCFLP
NNELDSLEEK FKSLLSQNKF WKYGKHSVPQ VRSAYFELVS ALCQHVPQVM KEEAAKVSPS
VLLSIDDSDP VVCPALWEAV LYTLTTIEDC WFHVNAKKSV FPKLMAMIRE GGRGLAAVMY
PYLLPFISKL PQSITEPKLD FFKNFLTSLV TGLSTERTKS SSSECSAVIS AFFECLRFIM
QQNLGEEEMV QMLINEQLIP FIDTVLKDSG LHHGPMFDHL ADTLSSWEAK ADAERDPGAV
YNLENVLLSF WGRLSEICTE KIRQPEADVK SVLCVSSLVG VLQRPRSSLK LHRKKTAQVR
FAINIPEAHK GDEKSMSSEG ENSEGSDGGA QSPLSNTSSD LVSPLRKKPL EDLVCKLAEV
SISFVNERKS EQHLQFLSTL LDSFSSVQVF NILLSDKQKN VVKAKPLEIT KLAEKNPAVK
FLYHKLIGWL NDSQKEDGGF LVDILYSALR CCDSGVERKE VLDDLTKEDL KWSSLLQVIE
KACSSSDKHA LVTPWLKGSI LGEKLVALAD CLCDKDLEAT TSESHSSEQW SLLRLALSQH
VKNDYLIGEV YVGRIIVKLH ETLSKTKDLS EAANSDSSVS FVCDVVHSFF SSAGGGLLMP
PSEDLLLTLF QLCAQSKERT HLPDFLICKL KNTLLSGVNL LVHQTASTYE QSTFLRLSVL
WLKDQVQSSA LDNTSLQVLL SAAGDLLGTL VESEDTSLLG VYIGSVMPSD SEWEKMRQAL
PVQWLHRPLL EGRLSLNYEC FKTDFKEQDT KTLPNHLCTS SLLSKMILVA QKKKLVLEDN
VLEKIIAELL YSLQWCEELD NAPSFLSGFC GILQKMNITY SNLSVLSETS SLLQLLFDRS
RKNGTLWSLI IAKLILSRSI SSDEVKPYYK RKESFFPLTE GSLHTIQSLC PFLSKEEKKE
FSAQCIPAFL GWTKEDLCSI NGAFGHLAIF NSCLQTRSID DKQLLHGILK IITSWRKQHE
DIFLFSCNLS EASPEVLGLN IEIMRFLSLF LKHCAYPLPL ADSEWDFIMC SMLAWLETTS
ENQALYSVPL VQLFACVSFD LACDLCAFFD SITPDIVDNL PVNLISEWKE FFSKGIHSLL
LPLLVNAIGE NKDLSETSFQ NAMLKPMCET LTYISKDQLL SHKLPARLVA SQKTNLPEHL
QTLLNTLTPL LLFRARPVQI AAYHMLCKLM PELPQHDQDN LRSYGDEEEE PALSPPAALM
SLLSSQEELL ENVLGCVPVG QIVTVKPLSE DFCYVLGYLL TWKLILTFFK AASSQLRALY
SMYLRKTKSL NKLLYHLFRL MPENPTYGET AIEVSSKDPK TFFTEEVQLS IRETATLPYH
IPHLACSVYH MTLKDLPAMV RLWWNSSEKR VFNIVDRFTS KYVSNVLSFQ EISSVQTSTQ
LFNGMTVKAR ATTREVMATY TIEDIVIELI IQLPSNYPLG SITVESGKRI GVAVQQWRNW
MLQLSTYLTH QNGSIMEGLA LWKNNVDKRF EGVEDCMICF SVIHGFNYSL PKKACRTCKK
KFHSACLYKW FTSSNKSTCP LCRETFF
