ITT1_YEAST
ID ITT1_YEAST Reviewed; 464 AA.
AC Q04638; D6VZA5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Translation termination inhibitor protein ITT1;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
GN Name=ITT1; OrderedLocusNames=YML068W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND INTERACTION WITH SUP35 AND SUP45.
RX PubMed=11570975; DOI=10.1186/1471-2199-2-9;
RA Urakov V.N., Valouev I.A., Lewitin E.I., Paushkin S.V., Kosorukov V.S.,
RA Kushnirov V.V., Smirnov V.N., Ter-Avanesyan M.D.;
RT "Itt1p, a novel protein inhibiting translation termination in Saccharomyces
RT cerevisiae.";
RL BMC Mol. Biol. 2:9-9(2001).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Modulates the efficiency of translation termination,
CC resulting in the readthrough of all three types of nonsense codons UAA,
CC UAG and UGA. {ECO:0000269|PubMed:11570975}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:O60260};
CC -!- SUBUNIT: Interacts with translation release factors eRF1 (SUP45) and
CC eRF3 (SUP35) in vitro. {ECO:0000269|PubMed:11570975}.
CC -!- INTERACTION:
CC Q04638; P05453: SUP35; NbExp=3; IntAct=EBI-27858, EBI-6540;
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC type E3 enzymes: they bind E2s via the first RING domain, but require
CC an obligate trans-thiolation step during the ubiquitin transfer,
CC requiring a conserved cysteine residue in the second RING domain.
CC {ECO:0000250|UniProtKB:O60260}.
CC -!- MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000305}.
CC -!- CAUTION: Lacks the His residue in the RING-type domain 2 that is one of
CC the conserved features of the family. {ECO:0000305}.
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DR EMBL; Z38114; CAA86252.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09829.1; -; Genomic_DNA.
DR PIR; S48329; S48329.
DR RefSeq; NP_013643.1; NM_001182427.1.
DR AlphaFoldDB; Q04638; -.
DR BioGRID; 35098; 84.
DR DIP; DIP-1952N; -.
DR IntAct; Q04638; 7.
DR MINT; Q04638; -.
DR STRING; 4932.YML068W; -.
DR iPTMnet; Q04638; -.
DR MaxQB; Q04638; -.
DR PaxDb; Q04638; -.
DR PRIDE; Q04638; -.
DR EnsemblFungi; YML068W_mRNA; YML068W; YML068W.
DR GeneID; 854934; -.
DR KEGG; sce:YML068W; -.
DR SGD; S000004533; ITT1.
DR VEuPathDB; FungiDB:YML068W; -.
DR eggNOG; KOG1814; Eukaryota.
DR HOGENOM; CLU_021364_2_2_1; -.
DR InParanoid; Q04638; -.
DR OMA; SNLQRCP; -.
DR BioCyc; YEAST:G3O-32663-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q04638; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04638; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006449; P:regulation of translational termination; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Repeat; Transferase;
KW Translation regulation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..464
FT /note="Translation termination inhibitor protein ITT1"
FT /id="PRO_0000056340"
FT ZN_FING 180..236
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 267..338
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 402..431
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 176..455
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ACT_SITE 415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ SEQUENCE 464 AA; 54096 MW; F481372B742AF63D CRC64;
MALTQFENDL EILRDMYPEL EMKSVKVEEE GEFPQRINGK LLFKISLLAD VNIEFGEQHM
LLSNLSNECV EFTIYSCHYP DIRRCVVMDI KSLWISTDEK KMLIDKALRL VEETVDMSIE
FADSFTSILI LIFGFLIDDT AILLFPNGIR KCLTQDQYDL FKQISEEATL QKVSRSNYHC
CICMEMEKGV RMIKLPCENA NVEHYLCRGC AKSYFTAMIQ ENRISSVRCP QCEYKELKLE
DFKSYKKMLK ALFTPLIPVS FLKEVIDTEL CERYEKMFYN QAATRLSKYC PYACVTCRRC
DSWCTKEDLD DAMIQCQKCH FVFCFDCLHA WHGYNNKCGK KVSLSTDIIE EYLDDTVTSY
ERKRKLEAKY GRRVLELEVN DYLAEKMLDL AIKKEGSNLQ RCPKCKVVVE RSEGCNKMKC
EVCGTLFCFI CGVLLYPEDP YEHFREAYSG CYGRLFEGMP GTET
