LTN1_SCHPO
ID LTN1_SCHPO Reviewed; 1610 AA.
AC O74349;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 Name=rkr1 {ECO:0000312|PomBase:SPBC21D10.09c}; ORFNames=SPBC21D10.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: E3 ubiquitin-protein ligase component of the ribosome quality
CC control complex (RQC), a ribosome-associated complex that mediates
CC ubiquitination and extraction of incompletely synthesized nascent
CC chains for proteasomal degradation. Ubiquitination leads to cdc48
CC recruitment for extraction and degradation of the incomplete
CC translation product. {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 the E3 ubiquitin ligase rkr1/ltn1, rqc1 and mtr1/rqc2, as
CC well as cdc48 and its ubiquitin-binding cofactors. RQC forms a stable
CC complex with 60S ribosomal subunits. {ECO:0000250|UniProtKB:Q04781}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04781}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the LTN1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA20765.1; -; Genomic_DNA.
DR PIR; T11681; T11681.
DR RefSeq; NP_596004.1; NM_001021912.2.
DR AlphaFoldDB; O74349; -.
DR SMR; O74349; -.
DR BioGRID; 277155; 26.
DR STRING; 4896.SPBC21D10.09c.1; -.
DR iPTMnet; O74349; -.
DR MaxQB; O74349; -.
DR PaxDb; O74349; -.
DR PRIDE; O74349; -.
DR EnsemblFungi; SPBC21D10.09c.1; SPBC21D10.09c.1:pep; SPBC21D10.09c.
DR GeneID; 2540629; -.
DR KEGG; spo:SPBC21D10.09c; -.
DR PomBase; SPBC21D10.09c; rkr1.
DR VEuPathDB; FungiDB:SPBC21D10.09c; -.
DR eggNOG; KOG0803; Eukaryota.
DR HOGENOM; CLU_000471_0_0_1; -.
DR InParanoid; O74349; -.
DR PhylomeDB; O74349; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:O74349; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990112; C:RQC complex; ISO:PomBase.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISO:PomBase.
DR CDD; cd16491; RING-CH-C4HC3_LTN1; 1.
DR Gene3D; 3.30.40.10; -; 1.
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; PTHR12389; 2.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1610
FT /note="E3 ubiquitin-protein ligase listerin"
FT /id="PRO_0000310490"
FT REPEAT 110..148
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 314..351
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 372..408
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 409..443
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 590..626
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 627..664
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 736..773
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 965..1003
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 1119..1156
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1322..1354
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1355..1393
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1435..1473
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT ZN_FING 1558..1604
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1610 AA; 184373 MW; 08F202AFA7F7473E CRC64;
MKKKSTDLYG RKNPGMQSMS GSFSSLQIAL DESSSNFSTI YEPPDLSGLD AEMIVIVKNL
QKRDIVTKCR ALQDLIQWND PSQFDNEQFL NALAVLFPRL SIEVERHVRL KIFVFMSVLS
SALQKKLAPW LKFYITPWVM GFFDSDRAVS VSAKDSFKNL LSEEKWPHVW LKFGSTIAPI
VTDVFLHEDK ESLTDLRFFS NEEAESKVTR VKSSCLLTLS FLFKQTADLE NLETDKKIDK
QTFKSSLYEN LSTLFKSDEF WSLVSSPQDG VTVSLSDLLL IILKYDKPFV TQYKEKYFKR
VSRMISRLTS LTCVPMLRLL SNMISNFPNE VHQFANDSKR PLSKLFSNLI TKRISLPNSG
FYTSLLNLFK SIGAMQLVPS IESVDELCDA FLETANQEQR FLSTEVYDCL LNFLSFVYTD
SSDPQIKDHV RDRLRTIFTR YFKGEFVLRC STSDFDHCLQ SVFDKNSDFA SLWNEVLFGF
FNDESMDIET IPFDSLSRNL SLTVQTVLYL KNRNFQTGNE VMSILGPCLS FLMKLSTHKN
ERIACLSASQ LITVCHIFSD TTLIKPVKEL FQKYLVNDLP SSILKLGPQS PAFTLLRDIL
LLLKDYADLS EPWENVANQF TVSFDELENI RVLNSLPSLF ADGKLRGKIS LVKTLVEYYD
TAVFAIMQNP GNDWDMIRAC IGSKEILVPE ETIKNILFTT LEYFLTNDWV DNHLIILCAS
LHSLKAHLPT IFDENKSLYS LLPVILFSKP EDDGHVAAHF ESIFSLLKEK ALEDSGFSLK
LCSEVQEWSL NKVLNGSINE KLAADKCVLV FNSFGKLPSN FFTFPASFWD AKISSCIPFF
SNKLFIDQDF ILGFLDLVAS EPINVDMTDV GTQFVHIFHA SLYTLYYVET TGCDGDALFN
LTFAYLLIRI YLQNGIQSII DVPIRDAGIF VESFECYFKG EVVKFMRDKD ALTVLNELLI
DDIDGKMPVL FKRFKNLSSA ENTTSFSIFA AQGLTDFLIV VSNLLEMDEK HVDVVLGKLG
LSSSKSPIFV SSILEGLKPL EVDSEIIQRI RFKAVNDLTG KLHSANEVSK SLLILNAATT
QQITEKPLLP ITRCRLFLEN ITNWCSESGI KSLELLPVCC FLRFMYYFLP TVFSLSGSYW
NSIFDYIKYA MKMSVVDAPI VKSFELFALR LYNALSKNYE MNSDIKDCIV ESNESMNYLL
LKRFLFTHES TLRNSVTARM CNQYLVKLLE NCPGKVVRSF QYQEFFPSLC NSNDLQMESV
CMKFLREKLS HELKELTVYY MVESDYEPDV SLCPELLSLA IDFPGDPFVM VSKMEKYEHA
LRVYLLVWDL IFYHFEETTY NIKLSIINQL HAMDLLRPLL NTLVEILNLS YDRPINVDKY
PKIDYNLMDY SSATDRIRCL AIHIYYQCLR HLSSSVRSYW SEVKNRAFTS TVESFTGYNV
SPLLISASLD DVERSIESED FQSVGDVNVK VNRNTREISF IYNVDEHKLE MAIKIPSVYP
LQNVQVEGIE RVGVNERQWR SWILASQSIL SSQNGSITDA LLVLKKNISM HFEGVEECAI
CYSVLSVERT LPNKRCGTCR HKFHASCLYK WFKSSNSSRC PLCRSSFTFV
