ID A0A3B6N3G1_WHEAT Unreviewed; 1760 AA.
AC A0A3B6N3G1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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|RuleBase:RU367090};
GN ORFNames=CFC21_081167 {ECO:0000313|EMBL:KAF7076532.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5D02G553700.1};
RN [1] {ECO:0000313|EMBL:KAF7076532.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7076532.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5D02G553700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5D02G553700.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS5D02G553700.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7076532.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7076532.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM022225; KAF7076532.1; -; Genomic_DNA.
DR PaxDb; 4565-Traes_5DL_3CD4039DA-2; -.
DR EnsemblPlants; TraesCS5D02G553700.1; TraesCS5D02G553700.1; TraesCS5D02G553700.
DR Gramene; TraesCS5D02G553700.1; TraesCS5D02G553700.1; TraesCS5D02G553700.
DR Gramene; TraesCS5D03G1218400.1; TraesCS5D03G1218400.1.CDS; TraesCS5D03G1218400.
DR Gramene; TraesROB_scaffold_069175_01G000100.1; TraesROB_scaffold_069175_01G000100.1; TraesROB_scaffold_069175_01G000100.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019116; Chromosome 5D.
DR Proteomes; UP000815260; Chromosome 5D.
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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; SM00184; RING; 1.
DR SMART; SM00744; RINGv; 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:UP000019116};
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 1710..1757
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1760 AA; 197698 MW; DEA6FB3B7F3A6C27 CRC64;
MSSLVTAVKK GLAPHLKSLM GPWWFSQFDP AAEVAQAGRR SFEAAFPQSD RRLDALMLCV
KETFVYLNEN LKLTTQALSD KVTPTDELED MHHRVISSSL LAMATLIDIL LGVKLKSNGG
ESANTESKSH LKVRSATLSS AEAALSMHKY FIDFLKSKSA AIRSATYTLL TSYIKYVPHV
FNEEAMKILS STILGAFNEK DPLCHSAMWD TILVFSRKFP EAWSYCNIHK VVLNRFWHFL
QNGCYGSKQA SYPLIVQFLD VIPSEVATEK FAIEFLQNLW AGRNQRQLSA ADSLAFFTAF
KLSFLWLLKK VPRNSVGDSS DNIHNRLITN VLVKIVWHDY LQLSLSKNLD TIPGLLSEEA
TTDDHQLSHK SLLVQNVRLP IYYYQDLGKC IVEILDEISV AESHLLEVAC ESLLRDYLDI
VHQGEKLSKF QDHVDQLASF FCSLDLLVVQ NGRTWPLENL ARPLVIHSLP AIKSMDSPSL
VKLLLNLVEI FGPVHLFLKY SEKNDDKSYV EPYLNVFNSD FVPWCLDGKH ITCSSKIDLL
LSLIQEECFF DQWCLIIKYI IAKQKRSVDD KISHTNDQFE LLTLILQKVR ERIAGGKLRN
LQRSGSLPEH WRHDLLDSVA VSVFCDLPAT DSHVHFLCAA LGGSSQDDQV CFLSAEAVCK
IRESILKSLA SVLTTSTFEW TRSAHFLLLP AEHEHLKLLG EQSLLANFEM AQFAFQVFER
SLFALRIHEE DSVFSHILAA LFIIEWECSM ALTLEEENDL EGHKEEIDAE TLLCNSSDDR
LGATVHLKAN LAEHIHAFRQ SLIPSFWNDL RSDTLNRLAN ILAQSVRYSV FDTRDLGIDR
TAALCSEWVV DMLRLVCLDH IKLQSFYDIL LSEREDWPLW VKPSLQNGHA SVKFQCEPLA
TEETELKHQR FVAFVDKIVL NLSFGEVILG IPRNQHCTTS SSIDVTSPVS SFSRAWVAAE
MICTWKWKGG SAFSTFLPSL VQYMKTESCP EVSIMPFLLD TLLEGALMHE SSNWALFNVW
HLSDSEIDKI QDRFLRALVA LLFTTYTKER IWRESDALAL FEKLLEKMKS GEASSCTDLM
GESILSWLNE AISCLSLSPR EVTQQDIEDW MQVVLSCFPL EITGGTAKLV VKFDREISDA
ETSLLLTLFS RYRAFYASAD PSLSSSGTSL SKTAELLGVK LTAVMVGYCC TKLGEDDWCF
VFRILRKWIE SSVLLVEEMT DGVNDAVINR TSAEDILEKL KLIACTPEEL TFTFAESALV
TLCCINHVDS LHESQTLQLI RSGEYAESND KMMENVLRLF LASGVSEAIA GSCSEEASSI
IASSRVVYLH FWELVASFII DASPQIRGCA LESMKLWGLS KDSVSGLYSI LFSSEPISHL
QFAAYSLLMS EPICEVSLVN GENPQESDMD QQSIESTPDS EKALCLRDEL SALIEMPTSG
LAKTDLIARD RVNVFVAWAL LLSHLQRLPL SSTSRALLLS YVQDKISPCI LDCIFQHIPL
RSGSGGGASA SGKKKDAELV PEAKAAAEAS KNAIVTCSLL PYVESLWPVG VLEMASLAGS
LYGMMIRLLP SYVRTWFTGL RDRSLSSSIE SLTRVWCSPP LLLDEFCQVK ESVYADETFS
VSVNRSAYEI IATYKKEETG IDLVIRLPSC YPLRHVEVEC TRSLGISEVK CRKWLLSLTS
FVRNQNGAVA EAIQTWKKNF DKEFEGVEEC PICYSILHTS NHGLPRLACK TCKHKFHGAC
LYKWFSTSNK STCPLCQTPF
//
