ID   KCTD5_BOVIN             Reviewed;         234 AA.
AC   A5PKG7;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=BTB/POZ domain-containing protein KCTD5;
GN   Name=KCTD5;
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=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; BC142481; AAI42482.1; -; mRNA.
DR   RefSeq; NP_001096811.1; NM_001103341.1.
DR   AlphaFoldDB; A5PKG7; -.
DR   SMR; A5PKG7; -.
DR   STRING; 9913.ENSBTAP00000001047; -.
DR   PaxDb; A5PKG7; -.
DR   PRIDE; A5PKG7; -.
DR   Ensembl; ENSBTAT00000001047; ENSBTAP00000001047; ENSBTAG00000040575.
DR   GeneID; 100125308; -.
DR   KEGG; bta:100125308; -.
DR   CTD; 54442; -.
DR   VEuPathDB; HostDB:ENSBTAG00000040575; -.
DR   VGNC; VGNC:30513; KCTD5.
DR   eggNOG; KOG2715; Eukaryota.
DR   GeneTree; ENSGT00940000160374; -.
DR   HOGENOM; CLU_070830_1_0_1; -.
DR   InParanoid; A5PKG7; -.
DR   OMA; ISVGMQY; -.
DR   OrthoDB; 1333587at2759; -.
DR   TreeFam; TF313754; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000040575; Expressed in esophagus and 105 other tissues.
DR   ExpressionAtlas; A5PKG7; baseline and differential.
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: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_0000390462"
FT   DOMAIN          44..146
FT                   /note="BTB"
FT   REGION          211..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;  25986 MW;  DC1219C45BA482EB CRC64;
     MAENHCELLP PAPGGLGAGL GGGLCRRCSA GLGALAQRPG SVSKWVRLNV GGTYFLTTRQ
     TLCRDPKSFL YRLCQADPDL DSDKDETGAY LIDRDPTYFG PVLNYLRHGK LVINKDLAEE
     GVLEEAEFYN ITSLIKLVKD KIRERDSKTS QVPLKHVYRV LQCQEEELTQ MVSTMSDGWK
     FEQLVSIGSS YNYGSEDQAE FLCVVSKELH NSPHGPASEP SEKAKILQER GSRM