KCD11_BOVIN
ID KCD11_BOVIN Reviewed; 232 AA.
AC Q58DF7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=BTB/POZ domain-containing protein KCTD11;
DE AltName: Full=KCASH1 protein {ECO:0000305};
DE AltName: Full=Potassium channel tetramerization domain-containing protein 11;
DE AltName: Full=RING-type E3 ubiquitin transferase subunit KCTD11 {ECO:0000305};
GN Name=KCTD11;
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).
CC -!- FUNCTION: Plays a role as a marker and a regulator of neuronal
CC differentiation; Up-regulated by a variety of neurogenic signals, such
CC as retinoic acid, epidermal growth factor/EGF and NGFB/nerve growth
CC factor. Induces apoptosis, growth arrest and the expression of cyclin-
CC dependent kinase inhibitor CDKN1B. Plays a role as a tumor repressor
CC and inhibits cell growth and tumorigenicity of medulloblastoma (MDB).
CC Acts as probable substrate-specific adapter for a BCR (BTB-CUL3-RBX1)
CC E3 ubiquitin-protein ligase complex towards HDAC1. Functions as
CC antagonist of the Hedgehog pathway on cell proliferation and
CC differentiation by affecting the nuclear transfer of transcription
CC factor GLI1, thus maintaining cerebellar granule cells in
CC undifferentiated state, this effect probably occurs via HDAC1 down-
CC regulation, keeping GLI1 acetylated and inactive (By similarity).
CC {ECO:0000250|UniProtKB:Q693B1}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homopentamer. Interacts with KCTD6 and KCTD21; KCTD11 and
CC KCTD6 or KCTD21 may associate in pentameric assemblies. Component of
CC the BCR(KCTD11) E3 ubiquitin ligase complex, at least composed of CUL3
CC and KCTD11 and RBX1. Interacts (via BTB domain) with CUL3; initially a
CC 4:4 stoichiometry has been reported, however, electron microscopy
CC revealed pentameric states of the BTB domain.
CC {ECO:0000250|UniProtKB:Q693B1}.
CC -!- DOMAIN: When BTB domain is deleted, growth-suppressing properties are
CC lost. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46487.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; BT021640; AAX46487.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001030498.2; NM_001035421.2.
DR AlphaFoldDB; Q58DF7; -.
DR SMR; Q58DF7; -.
DR STRING; 9913.ENSBTAP00000013923; -.
DR PaxDb; Q58DF7; -.
DR PRIDE; Q58DF7; -.
DR GeneID; 539167; -.
DR KEGG; bta:539167; -.
DR CTD; 147040; -.
DR eggNOG; KOG2723; Eukaryota.
DR InParanoid; Q58DF7; -.
DR OrthoDB; 1051383at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR045763; KCTD11/21_C.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF19329; KCTD11_21_C; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Developmental protein; Growth regulation; Reference proteome;
KW Transferase; Tumor suppressor; Ubl conjugation pathway.
FT CHAIN 1..232
FT /note="BTB/POZ domain-containing protein KCTD11"
FT /id="PRO_0000248590"
FT DOMAIN 1..49
FT /note="BTB"
SQ SEQUENCE 232 AA; 26015 MW; AE08A6BBBC752407 CRC64;
MLGAMFRAGT PMTPNLNPEG GGHYFIDRDG KAFRHILNFL RLGRLDLPLG YGETALLRAE
ADFYQIRPLL DALRELEASR GTPAPTAALL HADVDSSPRL VHFSARRGPH HYELSSVQVD
TFRANLFCTD PECLGALRAR FGVTNEDRAE GGPHFRLEWA PRPAELPEVE YRRLGLQPLW
TGAPGEPRDV VGTPSFLEEV LRVALEHGFR LDSVFPDPED LLNSRSLRFV RH