WDR12_BOVIN
ID WDR12_BOVIN Reviewed; 423 AA.
AC Q0VC24; A5PJI2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ribosome biogenesis protein WDR12 {ECO:0000255|HAMAP-Rule:MF_03029};
DE AltName: Full=WD repeat-containing protein 12 {ECO:0000255|HAMAP-Rule:MF_03029};
GN Name=WDR12 {ECO:0000255|HAMAP-Rule:MF_03029};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon, and Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PeBoW complex, which is required for
CC maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_03029}.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and
CC WDR12. The complex is held together by BOP1, which interacts with PES1
CC via its N-terminal domain and with WDR12 via a high-affinity
CC interaction between the seven-bladed beta-propeller domains of the 2
CC proteins. The PeBoW complex associates with the 66S pre-ribosome.
CC Interacts (via UBL domain) with MDN1 (via VWFA/MIDAS domain).
CC {ECO:0000255|HAMAP-Rule:MF_03029}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03029}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03029}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03029}.
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DR EMBL; BT029892; ABM06142.1; -; mRNA.
DR EMBL; BC120386; AAI20387.1; -; mRNA.
DR EMBL; BC142121; AAI42122.1; -; mRNA.
DR RefSeq; NP_001069375.1; NM_001075907.1.
DR AlphaFoldDB; Q0VC24; -.
DR SMR; Q0VC24; -.
DR STRING; 9913.ENSBTAP00000020499; -.
DR PaxDb; Q0VC24; -.
DR PRIDE; Q0VC24; -.
DR Ensembl; ENSBTAT00000020499; ENSBTAP00000020499; ENSBTAG00000015424.
DR GeneID; 528209; -.
DR KEGG; bta:528209; -.
DR CTD; 55759; -.
DR VEuPathDB; HostDB:ENSBTAG00000015424; -.
DR VGNC; VGNC:36882; WDR12.
DR eggNOG; KOG0313; Eukaryota.
DR GeneTree; ENSGT00930000150950; -.
DR HOGENOM; CLU_000288_57_0_1; -.
DR InParanoid; Q0VC24; -.
DR OMA; VDCTRTK; -.
DR OrthoDB; 1540178at2759; -.
DR TreeFam; TF313023; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000015424; Expressed in conceptus and 108 other tissues.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0070545; C:PeBoW complex; ISS:UniProtKB.
DR GO; GO:0030687; C:preribosome, large subunit precursor; ISS:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03029; WDR12; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR012972; NLE.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR028599; WDR12/Ytm1.
DR Pfam; PF08154; NLE; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribosome biogenesis; rRNA processing; Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9GZL7"
FT CHAIN 2..423
FT /note="Ribosome biogenesis protein WDR12"
FT /id="PRO_0000283706"
FT REPEAT 99..137
FT /note="WD 1"
FT REPEAT 138..180
FT /note="WD 2"
FT REPEAT 187..226
FT /note="WD 3"
FT REPEAT 255..293
FT /note="WD 4"
FT REPEAT 295..334
FT /note="WD 5"
FT REPEAT 340..380
FT /note="WD 6"
FT REPEAT 384..422
FT /note="WD 7"
FT REGION 4..87
FT /note="Ubiquitin-like (UBL) domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT REGION 98..423
FT /note="Sufficient for nucleolar localization"
FT /evidence="ECO:0000250"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZL7"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZL7"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9GZL7"
SQ SEQUENCE 423 AA; 47709 MW; F321563DB8F91E00 CRC64;
MAQLQTRFFT DNKKYAVDDV PFSIPAASEI ADLSNLINKL LEAKNEFHKH VEFDFLIKGQ
FLRMPLFKHM ELENISSEEV VELEYVEKYT APQPEQCMFH DDWISAIEGT EEWILTGSYD
KTSRIWSLEG KSIMTIVGHT DVVKDVAWVK KDSLSCLLLS ASMDQTILLW EWNVERNKVK
ALHCCRGHAG SVDSIAVDST GTKFCSGSWD KMLKIWSTVP TDEEDEMEES TNRPRKKQKT
EQLGLTRTPI VTLSGHKEAI SSVLWSDAEE ICSASWDHTI KVWDVESGSL KSTLTGNKVF
NCISYSPLCK RLASGSTDRH IRLWDPRTKD GSLVSLSLTS HTGWVTSVKW SPTHEQQLIS
GSLDNMVKLW DTRSCKAPLY DLAAHEDKVL SVDWTDSGLL LSGGADNKLY SYRYSPTTSH
VGA