ID H2YUW6_CIOSA Unreviewed; 1716 AA.
AC H2YUW6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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};
OS Ciona savignyi (Pacific transparent sea squirt).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000009126.1, ECO:0000313|Proteomes:UP000007875};
RN [1] {ECO:0000313|Proteomes:UP000007875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000009126.1}
RP IDENTIFICATION.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 51511.ENSCSAVP00000009126; -.
DR Ensembl; ENSCSAVT00000009240.1; ENSCSAVP00000009126.1; ENSCSAVG00000005380.1.
DR eggNOG; KOG0803; Eukaryota.
DR GeneTree; ENSGT00390000016055; -.
DR InParanoid; H2YUW6; -.
DR OMA; IYGSHWE; -.
DR TreeFam; TF314286; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007875; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:1990112; C:RQC complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
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; SM01197; FANCL_C; 1.
DR SMART; SM00744; RINGv; 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 {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367090};
KW Reference proteome {ECO:0000313|Proteomes:UP000007875};
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 1664..1712
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1716 AA; 192533 MW; E662E5739A671B2D CRC64;
MGKQKGQSNR TKGNARPSSS IAAANAFDGT RGVVGFASFS GDLGYIPVLK SVEDDSEGSI
DPDFRVPLCK LSKRDVTTKL KALAELIELS QNNDSDKSVS MLPNWPRIYN RLSEDSDRRV
REGLQQTHHA IVTKVGKEIA PFLKGLFGAW WIATCDAYAP VASAAWNAFS AAFPTPAKQG
KVLVFCHQEI LHAVKSNVFM AAVQGQKEDE ENDMERILAS SLSALAAFIT TLESVNCMDK
LGTENFTDFL TKPRFWKLAR HKAPGVGSAF FSVITSFLSG SNALLGDYLS QVCKAVLSRL
NDSSSLACRA QWDATEKLMI SFPNWHEHID LRKVFLPSFW SVIKSGFNGN AKIICPHLLP
MVGCFPASLF AIPVYQELFN CLQIALDSNT VQSSASETRA VITATVECAQ LILQKSVEVC
DDPNWEAIDL ILKGQLLPIF EKSIQYPDSN KYLTAPLHQL VVGTLSTLSY KANDETKQQK
SYIRICCMIW KEITRIATEL LNQCKTRTNS LQCMINFLFA VKLASCGSKP FQIQASVKSK
PGVRFRDEAG INSKETDKAP SSKVTNVYLF QSLEICLRDV VGHILQSQFN PGQRLSFASL
VLEKFATSTL FDQVFHLLAD IVPSGSDHDL SYECLRQYFL PCVKDIVSSN PETQHHSATL
LYTCLKCCGS DAETIAQEIF SDPEIHGGVQ CCMLLAVHFL TNDDNPTWLR NWLSSETGNF
SKFLLDIVES DAHLKLEESW KLLNMSMTGD KAVLQSKSAL DILKKLYETV ETTEKSNFTV
TEKASLLTTA SIISYISDSG FVTAADVLLG LMFEKLFRSV LYNQHETSFD IFVQLLQMLD
SSRHLNDDLL QLSNNYFIRC ADTVCKEILE KKETAEDNLP ANIEKVLDFL SATISHHGPE
VINNFYSHLL PSESTWLQHR SDMSRKSWLP IEDVIEGRVI SSTFEKTKMD SNYVNLVRVF
SDLACRILQG SDDTADQEQL LQIASKHDSM KQLCFESLLV DSQQLSSNKY IELLDCYKES
AEWCKYMLSI LAQKSSQVGG GWICCFSKFL SKIDFSCNWK QITLLNDIDY ANQTMNEAFC
STLISVVNSC DMLSAKKLFD WIVPKTLSFS GTFDTILDGG YVYEFTALVN IFRRLLFLEN
YENVLADTSE QIIEQLLLCK SSFSSVFLFD VAFNNNSFQL LFNSSVARFI KLAVECKPSG
RSSEFWEFAQ CSLVSWLESA CMTFEGKEFI SEPQFHNQLA LLHSAASLLS ALDKYLTDPA
TIEDPTLPTS LTREWHEFFQ PAAHSTLVTI FLHLSKEVSL SSPAVYSLIQ NCLWNIHPDS
ITSCSSRLPV YLTPDSQLSD KMQTLLHHLC LALEPNGKTY TTQAITYTLL SKISGKVFLK
ENGDLLTAES IRQPIKLVRS LTSILNFHAE NPDSDLENPL LPEMYQSNTF AYLLMWKVLL
HLICNVPADA KSDFLSKLEE NGLSISESLL PKLLQLMPLN PHRKDDAQVI NMFQSEVDFR
TSSGENVAVV QHLACSLFKE VLTNLPVLIR SWYNGLGKVV RGQVDDYTTK HISGMISNEE
LKSVSVSKDE KDLHVSARTA SREILATYQI VDAEFEISIQ LPPNYPLSPA QVNTVRRVGV
GAAQWRYWIL QMTMLLQHQN GRILDALSLW KNKVDKRLDG LEECMICFSV VHGSNAQSLP
KLQCRTCRKK YHAECLYKWF DTSNQSTCPL CRAPMM
//
