ID   KCTD5_RAT               Reviewed;         234 AA.
AC   B5DEL1;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=BTB/POZ domain-containing protein KCTD5;
GN   Name=Kctd5;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Its interaction with CUL3 suggests that it may act as a
CC       substrate adapter in some E3 ligase complex (By similarity). Does not
CC       affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2
CC       and Kv3.4/KCNC4 (By similarity). {ECO:0000250|UniProtKB:Q9NXV2}.
CC   -!- SUBUNIT: Homopentamer (By similarity). Interacts (via C-terminus) with
CC       GRASP55/GORASP2 (By similarity). Interacts with CUL3 and with
CC       ubiquitinated proteins (By similarity). Interacts with CRY1 (By
CC       similarity). {ECO:0000250|UniProtKB:Q8VC57,
CC       ECO:0000250|UniProtKB:Q9NXV2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9NXV2}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9NXV2}. Nucleus {ECO:0000250|UniProtKB:Q9NXV2}.
CC       Note=Predominantly cytoplasmic, translocated to the nucleus upon
CC       interaction with Rep proteins. {ECO:0000250|UniProtKB:Q9NXV2}.
CC   -!- DOMAIN: The BTB (POZ) domain is atypical and mediates the formation of
CC       a homopentamer instead of a homotetramer (By similarity).
CC       Homopentamerization is due to the presence of 4 residues in the BTB
CC       (POZ) domain: Leu-56, Gly-100, Val-112 and Ala-118 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NXV2}.
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DR   EMBL; CH473948; EDM03804.1; -; Genomic_DNA.
DR   EMBL; BC168712; AAI68712.1; -; mRNA.
DR   RefSeq; NP_001099238.1; NM_001105768.1.
DR   AlphaFoldDB; B5DEL1; -.
DR   SMR; B5DEL1; -.
DR   STRING; 10116.ENSRNOP00000007850; -.
DR   jPOST; B5DEL1; -.
DR   PaxDb; B5DEL1; -.
DR   PeptideAtlas; B5DEL1; -.
DR   PRIDE; B5DEL1; -.
DR   Ensembl; ENSRNOT00000084991; ENSRNOP00000073503; ENSRNOG00000057186.
DR   GeneID; 287109; -.
DR   KEGG; rno:287109; -.
DR   UCSC; RGD:1304990; rat.
DR   CTD; 54442; -.
DR   RGD; 1304990; Kctd5.
DR   eggNOG; KOG2715; Eukaryota.
DR   GeneTree; ENSGT00940000160374; -.
DR   HOGENOM; CLU_070830_1_0_1; -.
DR   InParanoid; B5DEL1; -.
DR   OMA; ISVGMQY; -.
DR   OrthoDB; 1333587at2759; -.
DR   PhylomeDB; B5DEL1; -.
DR   TreeFam; TF313754; -.
DR   PRO; PR:B5DEL1; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Proteomes; UP000234681; Chromosome 10.
DR   Bgee; ENSRNOG00000057186; Expressed in jejunum and 18 other tissues.
DR   Genevisible; B5DEL1; RN.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   Pfam; PF02214; BTB_2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Nucleus; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV2"
FT   CHAIN           2..234
FT                   /note="BTB/POZ domain-containing protein KCTD5"
FT                   /id="PRO_0000390463"
FT   DOMAIN          44..146
FT                   /note="BTB"
FT   REGION          213..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXV2"
SQ   SEQUENCE   234 AA;  26164 MW;  05CCF56632DE4F3E CRC64;
     MAENHCELLP PAPSGLGAGL GGGLCRRCSA GIGALAQRPS GVSKWVRLNV GGTYFLTTRQ
     TLCRDPKSFL YRLCQADPDL DSDKDETGAY LIDRDPTYFG PVLNYLRHGK LVINRDLAEE
     GVLEEAEFYN ITSLIKLVKD KIRERDSKTS QMPVKHVYRV LQCQEEELTQ MVSTMSDGWK
     FEQLVSIGSS YNYGNEDQAE FLCVVSKELH NTPYGTTSEP SEKAKILQER GSRM