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Database: UniProt
Entry: TBL3_RAT
LinkDB: TBL3_RAT
Original site: TBL3_RAT 
ID   TBL3_RAT                Reviewed;         800 AA.
AC   Q5U2W5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Transducin beta-like protein 3;
GN   Name=Tbl3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Part of the small subunit (SSU) processome, first precursor
CC       of the small eukaryotic ribosomal subunit. During the assembly of the
CC       SSU processome in the nucleolus, many ribosome biogenesis factors, an
CC       RNA chaperone and ribosomal proteins associate with the nascent pre-
CC       rRNA and work in concert to generate RNA folding, modifications,
CC       rearrangements and cleavage as well as targeted degradation of pre-
CC       ribosomal RNA by the RNA exosome. {ECO:0000250|UniProtKB:Q12788}.
CC   -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more
CC       than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3.
CC       {ECO:0000250|UniProtKB:Q12788}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q12788}.
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DR   EMBL; BC085837; AAH85837.1; -; mRNA.
DR   RefSeq; NP_001008278.1; NM_001008277.1.
DR   AlphaFoldDB; Q5U2W5; -.
DR   SMR; Q5U2W5; -.
DR   STRING; 10116.ENSRNOP00000018405; -.
DR   iPTMnet; Q5U2W5; -.
DR   PhosphoSitePlus; Q5U2W5; -.
DR   PaxDb; 10116-ENSRNOP00000018405; -.
DR   Ensembl; ENSRNOT00000018405.6; ENSRNOP00000018405.4; ENSRNOG00000013429.6.
DR   Ensembl; ENSRNOT00055048737; ENSRNOP00055040051; ENSRNOG00055028159.
DR   Ensembl; ENSRNOT00060018033; ENSRNOP00060014038; ENSRNOG00060010647.
DR   Ensembl; ENSRNOT00065014825; ENSRNOP00065011083; ENSRNOG00065009275.
DR   GeneID; 287120; -.
DR   KEGG; rno:287120; -.
DR   UCSC; RGD:1305142; rat.
DR   AGR; RGD:1305142; -.
DR   CTD; 10607; -.
DR   RGD; 1305142; Tbl3.
DR   eggNOG; KOG0319; Eukaryota.
DR   GeneTree; ENSGT00940000157651; -.
DR   HOGENOM; CLU_009276_1_0_1; -.
DR   InParanoid; Q5U2W5; -.
DR   OMA; PYVQRHF; -.
DR   OrthoDB; 35744at2759; -.
DR   PhylomeDB; Q5U2W5; -.
DR   TreeFam; TF314872; -.
DR   Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q5U2W5; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000013429; Expressed in pancreas and 20 other cell types or tissues.
DR   Genevisible; Q5U2W5; RN.
DR   GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR   GO; GO:0034511; F:U3 snoRNA binding; IBA:GO_Central.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB.
DR   CDD; cd00200; WD40; 2.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR013934; Utp13_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19854; TRANSDUCIN BETA-LIKE 3; 1.
DR   PANTHER; PTHR19854:SF15; TRANSDUCIN BETA-LIKE PROTEIN 3; 1.
DR   Pfam; PF08625; Utp13; 1.
DR   Pfam; PF00400; WD40; 9.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 13.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 9.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW   Ubl conjugation; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q12788"
FT   CHAIN           2..800
FT                   /note="Transducin beta-like protein 3"
FT                   /id="PRO_0000362981"
FT   REPEAT          64..105
FT                   /note="WD 1"
FT   REPEAT          107..146
FT                   /note="WD 2"
FT   REPEAT          149..190
FT                   /note="WD 3"
FT   REPEAT          193..232
FT                   /note="WD 4"
FT   REPEAT          245..284
FT                   /note="WD 5"
FT   REPEAT          290..329
FT                   /note="WD 6"
FT   REPEAT          332..372
FT                   /note="WD 7"
FT   REPEAT          374..413
FT                   /note="WD 8"
FT   REPEAT          419..459
FT                   /note="WD 9"
FT   REPEAT          477..516
FT                   /note="WD 10"
FT   REPEAT          519..560
FT                   /note="WD 11"
FT   REPEAT          562..602
FT                   /note="WD 12"
FT   REPEAT          604..642
FT                   /note="WD 13"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12788"
FT   CROSSLNK        407
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q12788"
SQ   SEQUENCE   800 AA;  88372 MW;  3F1B4D1B3925D8C7 CRC64;
     MAETAAGLCR FKANYAVERK IEPFYKGGKA QLDQTGRHLF CVCGTKVNIL DVASGDLIRS
     LEQEDQEDIT AFDLSPDDEV LVTASRALLL AQWAWREGTV ARLWKAIHTA PVASMAFDAT
     STLLATGGCD GAVRVWDIVQ HYGTHHFRGS PGVVHLVAFH PDPTRLLLFS SAVDTSIRVW
     SLQDRSCLAV LTAHYSAVTS LSFSEDGHTM LSSGRDKICI VWDLRSYETS RTVPVFESVE
     ASVLLPEEPA LALGVKNSGL HFLTAGDQGI LRVWEAASGQ CVYTQPQMSG LRQELTHCTL
     ARAAGLLLTV TADHNLLLYE ARSLQLQKQF AGYSEEVLDV RFLGPNDSHI IVASNSPCLK
     VFELQTLACQ ILHGHTDIVL ALDVFRKGWL FASCAKDQSI RIWRMNKAGQ VACVAQGSGH
     THSVGTICCS RLKESFLVTG SQDCTVKLWP LPEALPSKNT ASDGDLIPLQ AQSTQRCHDK
     DINSLAVSPN DKLLATGSQD RTAKLWALPQ CQLLGVFSGH RRGLWNVQFS PTDQVLATAS
     ADGTIKLWAL QDFSCLKTFE GHDASVLKVA FVSRGAQLLS SGSDGLLKLW TIKSNECVRT
     LDAHEDKVWG LHCSRLDDHA ITGGSDSRII LWKDVTEAEQ AEEQAKREEQ VIKQQELDNL
     LHEKRYLRAL GLAISLDRPH TVLTVIQAIR RDPEACEKLE ATVLRLRRDQ KEALLRFCIT
     WNTNSRHCHE AQAVLGVLLR HEAPEELLAY DGVRGALEAL LPYTERHFQR LSRTLQAATF
     LDFLWHNMKL SPLPAAPPAL
//
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