KCD21_MOUSE
ID KCD21_MOUSE Reviewed; 260 AA.
AC Q3URF8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=BTB/POZ domain-containing protein KCTD21;
DE AltName: Full=KCASH2 protein {ECO:0000303|PubMed:21472142};
DE AltName: Full=Potassium channel tetramerization domain-containing protein 21;
GN Name=Kctd21;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=21472142; DOI=10.1593/neo.101630;
RA De Smaele E., Di Marcotullio L., Moretti M., Pelloni M., Occhione M.A.,
RA Infante P., Cucchi D., Greco A., Pietrosanti L., Todorovic J., Coni S.,
RA Canettieri G., Ferretti E., Bei R., Maroder M., Screpanti I., Gulino A.;
RT "Identification and characterization of KCASH2 and KCASH3, 2 novel Cullin3
RT adaptors suppressing histone deacetylase and Hedgehog activity in
RT medulloblastoma.";
RL Neoplasia 13:374-385(2011).
CC -!- FUNCTION: Probable substrate-specific adapter of a BCR (BTB-CUL3-RBX1)
CC E3 ubiquitin-protein ligase complex mediating the ubiquitination and
CC subsequent proteasomal degradation of target proteins. Promotes the
CC ubiquitination of HDAC1. Can function as antagonist of the Hedgehog
CC pathway by affecting the nuclear transfer of transcription factor GLI1;
CC the function probably occurs via HDAC1 down-regulation, keeping GLI1
CC acetylated and inactive. Inhibits cell growth and tumorigenicity of
CC medulloblastoma (MDB). {ECO:0000250|UniProtKB:Q4G0X4}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homopentamer. Interacts with KCTD11; KCTD21 and KCTD11 may
CC associate in pentameric assemblies. Interacts (via BTB domain) with
CC CUL3; indicative for a participation in a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex (PubMed:21472142).
CC {ECO:0000250|UniProtKB:Q4G0X4, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in cerebellum and brain. Expressed
CC in adult cerebellum (at protein level). {ECO:0000269|PubMed:21472142}.
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DR EMBL; AK141547; BAE24730.1; -; mRNA.
DR CCDS; CCDS21456.1; -.
DR RefSeq; NP_001034128.2; NM_001039039.3.
DR AlphaFoldDB; Q3URF8; -.
DR SMR; Q3URF8; -.
DR STRING; 10090.ENSMUSP00000051316; -.
DR PhosphoSitePlus; Q3URF8; -.
DR MaxQB; Q3URF8; -.
DR PaxDb; Q3URF8; -.
DR PRIDE; Q3URF8; -.
DR ProteomicsDB; 301762; -.
DR GeneID; 622320; -.
DR KEGG; mmu:622320; -.
DR CTD; 283219; -.
DR MGI; MGI:3643121; Kctd21.
DR eggNOG; KOG2723; Eukaryota.
DR InParanoid; Q3URF8; -.
DR OrthoDB; 1426852at2759; -.
DR PhylomeDB; Q3URF8; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 622320; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Kctd21; mouse.
DR PRO; PR:Q3URF8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3URF8; protein.
DR GO; GO:0097602; F:cullin family protein binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:MGI.
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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
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 SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Growth regulation; Reference proteome; Tumor suppressor;
KW Ubl conjugation pathway.
FT CHAIN 1..260
FT /note="BTB/POZ domain-containing protein KCTD21"
FT /id="PRO_0000281152"
FT DOMAIN 3..72
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT COILED 88..112
FT /evidence="ECO:0000255"
SQ SEQUENCE 260 AA; 29623 MW; 61A8F5FCCCF8D622 CRC64;
MSDPITLNVG GKLYTTSLAT LTSFPDSMLG AMFSGKMPTK RDSQGNCFID RDGKVFRYIL
NFLRTSHLDL PEDFQEMGLL RREADFYQVQ PLIEALQEKE VELSKAEKNA MLNITLKQRV
QTVHFTVREA PQIYSLSSSS MEVFNANIFS TSCLFLKLLG SKLLYCSNGN LSSITSHLQD
PNHLTLDWVA NVEGLPEEEY TKQNLKRLWV VPANKQINSF QVFVEEVLKI ALSDGFCIDS
SHPHALDFMN NKIIRLIRYR
