WDR12_PONAB
ID WDR12_PONAB Reviewed; 423 AA.
AC Q5REE6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR857583; CAH89861.1; -; mRNA.
DR RefSeq; NP_001124867.1; NM_001131395.1.
DR RefSeq; XP_009236273.1; XM_009237998.1.
DR AlphaFoldDB; Q5REE6; -.
DR SMR; Q5REE6; -.
DR STRING; 9601.ENSPPYP00000014627; -.
DR Ensembl; ENSPPYT00000051442; ENSPPYP00000042103; ENSPPYG00000040830.
DR GeneID; 100171729; -.
DR KEGG; pon:100171729; -.
DR CTD; 55759; -.
DR eggNOG; KOG0313; Eukaryota.
DR GeneTree; ENSGT00930000150950; -.
DR HOGENOM; CLU_000288_57_0_1; -.
DR InParanoid; Q5REE6; -.
DR OMA; VDCTRTK; -.
DR OrthoDB; 1540178at2759; -.
DR TreeFam; TF313023; -.
DR Proteomes; UP000001595; Chromosome 2B.
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: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; 5.
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_0000354080"
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 220..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; 47708 MW; 9E412EEA46A998D0 CRC64;
MAQLQTRFYT DNKKYAIDDV PFSIPAASEI ADLSNIINKL LKDKNEFHKH VEFDFLIKGQ
FLRMPLDKHM EMENISSEEV VEIEYVEKYT APQPEQCMFH DDWISSIKGA EEWILTGSYD
KTSRIWSLEG KSIMTIVGHT DVVKDVAWVK KDSLSCLLLS ASMDQTILLW EWNVERNKVK
ALHCCRGHAG SVDSIAVDGS GTKFCSGSWD KMLKIWSTVP TDEEDEMEES TNRPRKKQKT
EQLGLTRTPV VTLSGHMEAV SSVLWSDAEE ICSASWDHTI RVWDVESGSL KSTLTGNKVF
NCISYSPLCK RLASGSTDRH IRLWDPRTKD GSLVSLSLTS HTGWVTSVKW SPTHEQQLIS
GSLDNIVKLW DTRSCKAPLY DLAAHEDKVL SVDWTDTGLL LSGGADNKLY SYRYSPTTSH
VGA
