ID   BACD1_BOVIN             Reviewed;         329 AA.
AC   Q2T9W0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1;
DE   AltName: Full=BTB/POZ domain-containing protein KCTD13;
GN   Name=KCTD13;
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].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC       ubiquitin-protein ligase complex required for synaptic transmission.
CC       The BCR(KCTD13) E3 ubiquitin ligase complex mediates the ubiquitination
CC       of RHOA, leading to its degradation by the proteasome, thereby
CC       regulating the actin cytoskeleton and promoting synaptic transmission.
CC       {ECO:0000250|UniProtKB:Q8BGV7}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q8WZ19}.
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. Component of the BCR(KCTD13) E3 ubiquitin ligase
CC       complex, at least composed of CUL3, KCTD13/BACURD1 and RBX1. Interacts
CC       with RHOA; with a preference for RhoA-GDP. Interacts with POLD2 and
CC       PCNA. Interacts with SPRTN. {ECO:0000250|UniProtKB:Q8WZ19}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WZ19}.
CC   -!- SIMILARITY: Belongs to the BACURD family. {ECO:0000305}.
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DR   EMBL; BC111242; AAI11243.1; -; mRNA.
DR   RefSeq; NP_001033146.1; NM_001038057.2.
DR   AlphaFoldDB; Q2T9W0; -.
DR   SMR; Q2T9W0; -.
DR   STRING; 9913.ENSBTAP00000021258; -.
DR   PaxDb; Q2T9W0; -.
DR   GeneID; 507911; -.
DR   KEGG; bta:507911; -.
DR   CTD; 253980; -.
DR   eggNOG; KOG2716; Eukaryota.
DR   InParanoid; Q2T9W0; -.
DR   OrthoDB; 1306250at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0050806; P:positive regulation of synaptic transmission; ISS:UniProtKB.
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:0043149; P:stress fiber assembly; ISS:UniProtKB.
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.
PE   2: Evidence at transcript level;
KW   Nucleus; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..329
FT                   /note="BTB/POZ domain-containing adapter for CUL3-mediated
FT                   RhoA degradation protein 1"
FT                   /id="PRO_0000283061"
FT   DOMAIN          41..109
FT                   /note="BTB"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   329 AA;  36425 MW;  9F0B80696AF830F0 CRC64;
     MSAEASGPAA AEAPSLEVAK PSELEPGSAA YGLKPLTTNS KYVKLNVGGS LHYTTLRTLT
     GQDTRLKAMF SGRAEVLTDA GGWVLIDRSG RHFGTILNYL RDGSVPLPES TRELGELLGE
     ARHYLVQGLI EDCQLALQQK RENVSPLCLI PTVTSPREEQ QLLASTSKPV VKLLHNRSNN
     KYSYTSTSDD NLLKNIELFD KLALRFHGRL LFLKDVLGDE ICCWSFYGQG RKIAEVCCTS
     IVYATEKKQT KVEFPEARIF EETLNILIYE TPRGPDPALL EATGGAAGGG GASRGEDEDN
     REHRVRRIHV RRHITHDERP HGQQIVFKD