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Database: UniProt
Entry: D4ADH5_RAT
LinkDB: D4ADH5_RAT
Original site: D4ADH5_RAT 
ID   D4ADH5_RAT              Unreviewed;       260 AA.
AC   D4ADH5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Potassium channel tetramerization domain containing 21 {ECO:0000313|Ensembl:ENSRNOP00000038320.6};
GN   Name=Kctd21 {ECO:0000313|Ensembl:ENSRNOP00000038320.6,
GN   ECO:0000313|RGD:1559529};
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 {ECO:0000313|Ensembl:ENSRNOP00000038320.6, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000038320.6, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000038320.6,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000038320.6}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000038320.6};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   RefSeq; NP_001102621.1; NM_001109151.1.
DR   RefSeq; XP_006229843.1; XM_006229781.3.
DR   AlphaFoldDB; D4ADH5; -.
DR   STRING; 10116.ENSRNOP00000038320; -.
DR   PaxDb; 10116-ENSRNOP00000038320; -.
DR   Ensembl; ENSRNOT00000035743.6; ENSRNOP00000038320.6; ENSRNOG00000024793.6.
DR   GeneID; 499209; -.
DR   KEGG; rno:499209; -.
DR   UCSC; RGD:1559529; rat.
DR   AGR; RGD:1559529; -.
DR   CTD; 283219; -.
DR   RGD; 1559529; Kctd21.
DR   VEuPathDB; HostDB:ENSRNOG00000024793; -.
DR   eggNOG; KOG2723; Eukaryota.
DR   GeneTree; ENSGT00940000160906; -.
DR   HOGENOM; CLU_088122_0_0_1; -.
DR   OMA; ANIFCTS; -.
DR   TreeFam; TF315332; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000024793; Expressed in skeletal muscle tissue and 17 other cell types or tissues.
DR   GO; GO:0097602; F:cullin family protein binding; ISO:RGD.
DR   GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   CDD; cd18395; BTB_POZ_KCTD21; 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   PANTHER; PTHR14499:SF57; BTB_POZ DOMAIN-CONTAINING PROTEIN KCTD21; 1.
DR   PANTHER; PTHR14499; POTASSIUM CHANNEL TETRAMERIZATION DOMAIN-CONTAINING; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF19329; KCTD11_21_C; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   4: Predicted;
KW   Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
SQ   SEQUENCE   260 AA;  29624 MW;  DC79A0D966695868 CRC64;
     MSDPITLNVG GKLYTTSLAT LTSFPDSMLG AMFSGKMPTK RDSQGNCFID RDGKVFRYIL
     NFLRTSHLDL PEDFQEMGLL RREADFYQVQ PLIEALQEKE IELSKAEKNA MLNITLKQHV
     QTVHFTVREA PQIYSLSSSS MEVFNANIFS TSCLFLKLLG SKLFYCSNGN LSSITSHLQD
     PNHLTLDWVA NVEGLPEEEY TKQNLKRLWV VPANKQINSF QAFVEEVLKI ALSDGFCIDS
     SHPHALDFMN NKIIRLIRYR
//
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