BACD3_MOUSE
ID BACD3_MOUSE Reviewed; 315 AA.
AC Q922M3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3;
DE Short=mBACURD3;
DE AltName: Full=BTB/POZ domain-containing protein KCTD10;
GN Name=Kctd10;
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=Egg, Head, Mammary gland, Skin, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [4]
RP IDENTIFICATION IN THE TECTONIC-LIKE COMPLEX.
RX PubMed=22179047; DOI=10.1038/ncb2410;
RA Chih B., Liu P., Chinn Y., Chalouni C., Komuves L.G., Hass P.E.,
RA Sandoval W., Peterson A.S.;
RT "A ciliopathy complex at the transition zone protects the cilia as a
RT privileged membrane domain.";
RL Nat. Cell Biol. 14:61-72(2012).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex. The BCR(BACURD3) E3 ubiquitin ligase
CC complex mediates the ubiquitination of target proteins, leading to
CC their degradation by the proteasome (By similarity).
CC {ECO:0000250|UniProtKB:Q8WZ19}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9H3F6}.
CC -!- SUBUNIT: Homotetramer; forms a two-fold symmetric tetramer in solution.
CC Interacts with CUL3; interaction is direct and forms a 5:5
CC heterodecamer (By similarity). Component of the BCR(BACURD3) E3
CC ubiquitin ligase complex, at least composed of CUL3, KCTD10/BACURD3 and
CC RBX1 (By similarity). Interacts with DNA polymerase delta subunit
CC 2/POLD2 (By similarity). Interacts with PCNA (By similarity).
CC Associated with the tectonic-like complex (also named B9 complex);
CC however as Kctd10 has not been identified in all tectonic-like
CC complexes purifications it is unclear whether it is really part of the
CC complex (PubMed:22179047). {ECO:0000250|UniProtKB:Q7TPL3,
CC ECO:0000250|UniProtKB:Q8WZ19, ECO:0000250|UniProtKB:Q9H3F6,
CC ECO:0000269|PubMed:22179047}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H3F6}.
CC -!- SIMILARITY: Belongs to the BACURD family. {ECO:0000305}.
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DR EMBL; AK028657; BAC26050.1; -; mRNA.
DR EMBL; AK041516; BAC30969.1; -; mRNA.
DR EMBL; AK145295; BAE26350.1; -; mRNA.
DR EMBL; AK147714; BAE28090.1; -; mRNA.
DR EMBL; AK161199; BAE36235.1; -; mRNA.
DR EMBL; AK163351; BAE37313.1; -; mRNA.
DR EMBL; AK166505; BAE38815.1; -; mRNA.
DR EMBL; BC006935; AAH06935.1; -; mRNA.
DR CCDS; CCDS19563.1; -.
DR RefSeq; NP_001153413.1; NM_001159941.1.
DR RefSeq; NP_080421.2; NM_026145.4.
DR AlphaFoldDB; Q922M3; -.
DR SMR; Q922M3; -.
DR BioGRID; 236914; 3.
DR CORUM; Q922M3; -.
DR IntAct; Q922M3; 3.
DR MINT; Q922M3; -.
DR STRING; 10090.ENSMUSP00000001125; -.
DR iPTMnet; Q922M3; -.
DR PhosphoSitePlus; Q922M3; -.
DR EPD; Q922M3; -.
DR jPOST; Q922M3; -.
DR MaxQB; Q922M3; -.
DR PaxDb; Q922M3; -.
DR PRIDE; Q922M3; -.
DR ProteomicsDB; 277173; -.
DR Antibodypedia; 2841; 125 antibodies from 19 providers.
DR DNASU; 330171; -.
DR Ensembl; ENSMUST00000102581; ENSMUSP00000099641; ENSMUSG00000001098.
DR GeneID; 330171; -.
DR KEGG; mmu:330171; -.
DR UCSC; uc008yzm.2; mouse.
DR CTD; 83892; -.
DR MGI; MGI:2141207; Kctd10.
DR VEuPathDB; HostDB:ENSMUSG00000001098; -.
DR eggNOG; KOG2716; Eukaryota.
DR GeneTree; ENSGT00950000183143; -.
DR InParanoid; Q922M3; -.
DR OrthoDB; 1306250at2759; -.
DR PhylomeDB; Q922M3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 330171; 9 hits in 74 CRISPR screens.
DR ChiTaRS; Kctd10; mouse.
DR PRO; PR:Q922M3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q922M3; protein.
DR Bgee; ENSMUSG00000001098; Expressed in right lung lobe and 265 other tissues.
DR ExpressionAtlas; Q922M3; baseline and differential.
DR Genevisible; Q922M3; MM.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0036038; C:MKS complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005112; F:Notch binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR045068; BACURD1-3.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR PANTHER; PTHR11145; PTHR11145; 1.
DR Pfam; PF02214; BTB_2; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..315
FT /note="BTB/POZ domain-containing adapter for CUL3-mediated
FT RhoA degradation protein 3"
FT /id="PRO_0000247422"
FT DOMAIN 32..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 269..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 239..245
FT /note="PCNA-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 280..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3F6"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3F6"
SQ SEQUENCE 315 AA; 35701 MW; 590AEF2D4F22D2D9 CRC64;
MEEMSGDSVV SSAVPAAATR TTSFKGASPS SKYVKLNVGG ALYYTTMQTL TKQDTMLKAM
FSGRMEVLTD SEGWILIDRC GKHFGTILNY LRDGGVPLPE SRREIEELLA EAKYYLVQGL
LEECQAALQN KDTYEPFCKV PVITSSKEEQ RLIATSNKPA VKLLYNRSNN KYSYTSNSDD
NMLKNIELFD KLSLRFNGRV LFIKDVIGDE ICCWSFYGQG RKIAEVCCTS IVYATEKKQT
KVEFPEARIY EETLNILLYE AQDGRGPDNA LLEATGGAAG RSHHLDEDEE RERERIERVR
RIHIKRPDDR AHLHQ
