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Database: UniProt
Entry: F6ZU08_HORSE
LinkDB: F6ZU08_HORSE
Original site: F6ZU08_HORSE 
ID   F6ZU08_HORSE            Unreviewed;      1828 AA.
AC   F6ZU08;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 3.
DT   27-MAR-2024, entry version 65.
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};
GN   Name=LTN1 {ECO:0000313|VGNC:VGNC:19836};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000009027.3, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000009027.3, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000009027.3,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000009027.3}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000009027.3};
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}.
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DR   STRING; 9796.ENSECAP00000009027; -.
DR   PaxDb; 9796-ENSECAP00000009027; -.
DR   Ensembl; ENSECAT00000011535.4; ENSECAP00000009027.3; ENSECAG00000010824.4.
DR   CTD; 26046; -.
DR   VGNC; VGNC:19836; LTN1.
DR   GeneTree; ENSGT00390000016055; -.
DR   HOGENOM; CLU_002412_0_0_1; -.
DR   InParanoid; F6ZU08; -.
DR   OMA; IYGSHWE; -.
DR   OrthoDB; 179130at2759; -.
DR   TreeFam; TF314286; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002281; Chromosome 26.
DR   Bgee; ENSECAG00000010824; Expressed in brainstem and 23 other cell types or tissues.
DR   ExpressionAtlas; F6ZU08; baseline.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0022626; C:cytosolic ribosome; IEA:Ensembl.
DR   GO; GO:1990112; C:RQC complex; IBA:GO_Central.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
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; 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   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:UP000002281};
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          1777..1824
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1828 AA;  206768 MW;  49D4673B150221D9 CRC64;
     MVRDAAGGGS GSGAAGGQGV WRKGWAGRSR PSGPSSGARG RKLWPGRVNR DQRAESAAET
     PTMGGKNKQR TKGNLRPSNS GRAAELLAKE QGTVPGFIGF GTSQSDLGYV PAIQGAEEID
     SLVDSDFRMV LRKLSKKDVT TKLKAMQEFG IMCTERDTEI VKGVLPYWPR IFCKISLDHD
     RRVREATQQA FEKLILKVKK HLAPYLKSLM GYWLMAQCDT YTPAASAAKD AFEAAFPPSK
     QPEAIAFCKD EITIVLQDHL IKETPDTLSD PQTVPEEERE AKFYRVVTCS LLALKKLLCL
     LPDNELDSLE EKFKSLLSQN KFWKYGKHSI PQIRSAYFEL VSALCLRIPQ LMKDEASKVS
     PSVLLSIDDS DPIVCPALWE AVLYTLTTIE DCWLHVNAKK SVFPKLSAVV REGGRGLATV
     IYPYLLPFIS KLPQSITDPK LDFFKNFLTS LIVGLSTERI KTSFSECSAV ISAFFECLRF
     IMQQNLGEKE IEEMLVNDQL IPFIDAVLKD PKLQDGQLFN HLAETLNSWE AKADMEKDDK
     TVHNLEKVLL NFWERLSEIC VEKINEPEAD LKSVLGVSNL LQVLQKPKSS LKSNKKKVSK
     VRFADEMPES NKENEKCVSS EGENSEGSEL VAELSLTHNC SDVISPLRKK PLEDLVCKLA
     EMSINYVNEQ KSEQHLRFLS TLLNSFSSTQ VFKMLLGDEK QSVVKAKPPE ITKLAQKNPA
     VQFLYQKLIG WLNEDPKKDA GFLVDILYSA LRCCDNNMER KDVLDDLTKV DLNWNSVLQV
     IEKACSSSDK HALVTPWLKG DILGEELVTL AEHLCNKHLE SKGSSESYFS ERWTLLSLVL
     SQHVKDDYLI GEVYVERIIV KLHETLSKTE TLTEAENNDS SVSFICDVAY NYFSSAKGCL
     LMPSSEDLLL TLFQLCAQSK EKTHLPDFLI CKLKNTWLSG VNLLVHQTGS IYKQSTFLRL
     SALWLKNQVQ SSSLDIKSLQ VLLSTVDDLL NALVESEDTY LLGVYIGSVM PNNSEWEKMR
     QSLPIQWLHR PLLEGRLSLN YECFKTDFKE QDTKKLPSHL CTSALLSKMI LVALKKEIVL
     ENNELEKIIA ELLYSLQWCE ELDNPPIFLT GFCEMLQKMN ITYDNLCGLG NTSGLLQLLF
     NRSRENGTLW SLIIAKLILS RSVSSDEVKR HYRRKECFFP LTEGNMHTIQ SLCPFLSKED
     KKEFIAQCIP ALLAWTKEDL CSTNGGFGHL AIFNSCLQTR SIDDEELLHG ILKILISWKK
     DHEDIFLFSC NLSEVSPEIL GVNIEIIRFL SLFLKYCSSP LAESEWDFIM CSMLAWLETT
     SENQALYSVP LVQLFACVSC DLACKLSAFF DSTTLDTTGN LPVNLISEWK EFFSQGIHSL
     LLPLLVNVTG ESKDTSETSF HNAMLKPMCE TLTYIPKDQL LSHKLPARLV AGQKTNLPEY
     LQTLLNTLVP LLLFRARPVQ IAVYHMLYKL MPELPQYDQD NLKSYGDEEE EPALSPPAAL
     MSLLSTQEDL LENVLGCIPV GQIVTIKPLS EDFCYVLGYL LTWKLILTFF KAASSQLRAL
     YSMYLRKTKS LNKLLYHLFR LMPENPTYAE TAIELSNKDP KTFFTEELQL SIRETATLPY
     HIPHLACSVY HMTLKDLPAM VRLWWNSSEK RVFNIVDRFT SKYVSNVLSF QEISSVQTST
     QLFNGMTVKA RATTREVMAT YTIEDIVIEL IIQLPSNYPL GSITVESGKR VGVAVQQWRN
     WMLQLSTYLT HQNGSIMEGL ALWKNNVDKR FEGVEDCMIC FSVIHGFNYS LPKKACRTCK
     KKFHSACLYK WFTSSNKSTC PLCRETFF
//
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