BACD3_RAT
ID BACD3_RAT Reviewed; 315 AA.
AC Q7TPL3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3;
DE AltName: Full=BTB/POZ domain-containing protein KCTD10;
GN Name=Kctd10;
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 [MRNA], INTERACTION WITH PCNA AND POLD2, TISSUE
RP SPECIFICITY, MOTIF, INDUCTION, AND MUTAGENESIS OF 242-VAL--PHE-244.
RC STRAIN=Wistar;
RX PubMed=15982757; DOI=10.1016/j.bbaexp.2005.05.005;
RA Zhou J., Ren K., Liu X., Xiong X., Hu X., Zhang J.;
RT "A novel PDIP1-related protein, KCTD10, that interacts with proliferating
RT cell nuclear antigen and DNA polymerase delta.";
RL Biochim. Biophys. Acta 1729:200-203(2005).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex. The BCR(BACURD3) E3 ubiquitin ligase
CC complex mediates the ubiquitination of target proteins, leading to
CC their degradation by the proteasome (By similarity).
CC {ECO:0000250|UniProtKB:Q8WZ19}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9H3F6}.
CC -!- SUBUNIT: Homotetramer; forms a two-fold symmetric tetramer in solution.
CC Interacts with CUL3; interaction is direct and forms a 5:5
CC heterodecamer (By similarity). Component of the BCR(BACURD3) E3
CC ubiquitin ligase complex, at least composed of CUL3, KCTD10/BACURD3 and
CC RBX1 (By similarity). Interacts with DNA polymerase delta subunit
CC 2/POLD2 (PubMed:15982757). Interacts with PCNA (By similarity).
CC {ECO:0000250|UniProtKB:Q8WZ19, ECO:0000250|UniProtKB:Q9H3F6,
CC ECO:0000269|PubMed:15982757}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H3F6}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in lung. Also detected
CC in testis and heart. Very low expression, if any, in brain, liver,
CC spleen, kidney and skeletal muscle. {ECO:0000269|PubMed:15982757}.
CC -!- INDUCTION: By tumor necrosis factor/TNF in cells.
CC {ECO:0000269|PubMed:15982757}.
CC -!- SIMILARITY: Belongs to the BACURD family. {ECO:0000305}.
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DR EMBL; AY318756; AAP79438.1; -; mRNA.
DR RefSeq; NP_001009973.1; NM_001009973.1.
DR AlphaFoldDB; Q7TPL3; -.
DR SMR; Q7TPL3; -.
DR BioGRID; 268948; 2.
DR IntAct; Q7TPL3; 1.
DR STRING; 10116.ENSRNOP00000065635; -.
DR PhosphoSitePlus; Q7TPL3; -.
DR jPOST; Q7TPL3; -.
DR PaxDb; Q7TPL3; -.
DR PRIDE; Q7TPL3; -.
DR GeneID; 494521; -.
DR KEGG; rno:494521; -.
DR CTD; 83892; -.
DR RGD; 1591979; Kctd10.
DR VEuPathDB; HostDB:ENSRNOG00000047896; -.
DR eggNOG; KOG2716; Eukaryota.
DR HOGENOM; CLU_060008_0_0_1; -.
DR InParanoid; Q7TPL3; -.
DR OMA; IKYPSEY; -.
DR OrthoDB; 1306250at2759; -.
DR PhylomeDB; Q7TPL3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q7TPL3; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000047896; Expressed in lung and 20 other tissues.
DR Genevisible; Q7TPL3; RN.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0036038; C:MKS complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005112; F:Notch binding; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR045068; BACURD1-3.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR PANTHER; PTHR11145; PTHR11145; 1.
DR Pfam; PF02214; BTB_2; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..315
FT /note="BTB/POZ domain-containing adapter for CUL3-mediated
FT RhoA degradation protein 3"
FT /id="PRO_0000247423"
FT DOMAIN 32..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 269..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 239..245
FT /note="Interaction with PCNA"
FT COMPBIAS 280..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3F6"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3F6"
FT MUTAGEN 242..244
FT /note="VEF->AEA: Loss of PCNA binding."
FT /evidence="ECO:0000269|PubMed:15982757"
SQ SEQUENCE 315 AA; 35745 MW; 469FEA48EE6FA7A1 CRC64;
MEEMSGESVV TSAVPAAATR TTSFKGASPS SKYVKLNVGG ALYYTTMQTL TKQDTMLKAM
FSGRMEVLTD SEGWILIDRC GKHFGTILNY LRDGAVPLPE SRREIEELLA EAKYYLVQGL
LEECQAALQN KDTYEPFCKV PVITSSKEEQ RLIATSDKPA VKLLYNRSNN KYSYTSNSDD
NMLKNIELFD KLSLRFNGRV LFIKDVIGDE ICCWSFYGQG RKIAEVCCTS IVYATEKKQT
KVEFPEARIY EETLNILLYE AQDGRGPDNA LLEATGGAAG RSHHLDEDEE RERERIERVR
RIHIKRPDDR AHLHQ
