BACD1_MOUSE
ID BACD1_MOUSE Reviewed; 329 AA.
AC Q8BGV7; Q6AXE9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1;
DE AltName: Full=BTB/POZ domain-containing protein KCTD13;
DE AltName: Full=Polymerase delta-interacting protein 1;
GN Name=Kctd13; Synonyms=Poldip1;
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 [MRNA], AND INDUCTION.
RC STRAIN=KM; TISSUE=Brain;
RA Zhou J., Hu X., Zhang J.;
RT "A tumor necrosis factor alpha-inducible protein.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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).
RN [4]
RP CAUTION.
RX PubMed=22596160; DOI=10.1038/nature11091;
RA Golzio C., Willer J., Talkowski M.E., Oh E.C., Taniguchi Y., Jacquemont S.,
RA Reymond A., Sun M., Sawa A., Gusella J.F., Kamiya A., Beckmann J.S.,
RA Katsanis N.;
RT "KCTD13 is a major driver of mirrored neuroanatomical phenotypes of the
RT 16p11.2 copy number variant.";
RL Nature 485:363-367(2012).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29088697; DOI=10.1038/nature24470;
RA Escamilla C.O., Filonova I., Walker A.K., Xuan Z.X., Holehonnur R.,
RA Espinosa F., Liu S., Thyme S.B., Lopez-Garcia I.A., Mendoza D.B., Usui N.,
RA Ellegood J., Eisch A.J., Konopka G., Lerch J.P., Schier A.F., Speed H.E.,
RA Powell C.M.;
RT "Kctd13 deletion reduces synaptic transmission via increased RhoA.";
RL Nature 551:227-231(2017).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex required for synaptic transmission
CC (PubMed:29088697). The BCR(KCTD13) E3 ubiquitin ligase complex mediates
CC the ubiquitination of RHOA, leading to its degradation by the
CC proteasome, thereby regulating the actin cytoskeleton and promoting
CC synaptic transmission (PubMed:29088697). {ECO:0000269|PubMed:29088697}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8WZ19}.
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. Component of the BCR(KCTD13) E3 ubiquitin ligase
CC complex, at least composed of CUL3, KCTD13/BACURD1 and RBX1. Interacts
CC with RHOA; with a preference for RhoA-GDP. Interacts with POLD2 and
CC PCNA. Interacts with SPRTN. {ECO:0000250|UniProtKB:Q8WZ19}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WZ19}.
CC -!- INDUCTION: By TNF-alpha. {ECO:0000269|Ref.1}.
CC -!- DISRUPTION PHENOTYPE: Reduced synaptic transmission in area CA1 of the
CC hippocampus caused by increased levels of RHOA. Brain size or neural
CC progenitor cell proliferation are not affected.
CC {ECO:0000269|PubMed:29088697}.
CC -!- SIMILARITY: Belongs to the BACURD family. {ECO:0000305}.
CC -!- CAUTION: Down-regulation of Kctd13 was initially reported to cause
CC macrocephaly due to increased proliferation (PubMed:22596160). However,
CC it was later shown that deletion of Kctd13 does not cause any change in
CC brain size, embryonic cell proliferation, neurogenesis, or cortical
CC layering/migration (PubMed:29088697). Experimental conditions used may
CC explain discrepancies. A possible explanation being that shRNAs used in
CC the first study, may have affected off-targets.
CC {ECO:0000269|PubMed:22596160, ECO:0000269|PubMed:29088697}.
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DR EMBL; AF534881; AAO16177.1; -; mRNA.
DR EMBL; AK075722; BAC35910.1; -; mRNA.
DR EMBL; BC079607; AAH79607.1; -; mRNA.
DR CCDS; CCDS21851.1; -.
DR RefSeq; NP_766335.1; NM_172747.2.
DR AlphaFoldDB; Q8BGV7; -.
DR SMR; Q8BGV7; -.
DR IntAct; Q8BGV7; 1.
DR STRING; 10090.ENSMUSP00000032924; -.
DR PhosphoSitePlus; Q8BGV7; -.
DR EPD; Q8BGV7; -.
DR MaxQB; Q8BGV7; -.
DR PaxDb; Q8BGV7; -.
DR PRIDE; Q8BGV7; -.
DR ProteomicsDB; 277172; -.
DR Antibodypedia; 13396; 145 antibodies from 18 providers.
DR DNASU; 233877; -.
DR Ensembl; ENSMUST00000032924; ENSMUSP00000032924; ENSMUSG00000030685.
DR GeneID; 233877; -.
DR KEGG; mmu:233877; -.
DR UCSC; uc009jtm.1; mouse.
DR CTD; 253980; -.
DR MGI; MGI:1923739; Kctd13.
DR VEuPathDB; HostDB:ENSMUSG00000030685; -.
DR eggNOG; KOG2716; Eukaryota.
DR GeneTree; ENSGT00950000183143; -.
DR HOGENOM; CLU_060008_0_0_1; -.
DR InParanoid; Q8BGV7; -.
DR OMA; PPLENCA; -.
DR OrthoDB; 1306250at2759; -.
DR PhylomeDB; Q8BGV7; -.
DR TreeFam; TF315649; -.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 233877; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Kctd13; mouse.
DR PRO; PR:Q8BGV7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BGV7; protein.
DR Bgee; ENSMUSG00000030685; Expressed in primary visual cortex and 173 other tissues.
DR Genevisible; Q8BGV7; MM.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:UniProtKB.
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:0043149; P:stress fiber assembly; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..329
FT /note="BTB/POZ domain-containing adapter for CUL3-mediated
FT RhoA degradation protein 1"
FT /id="PRO_0000191298"
FT DOMAIN 41..109
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 329 AA; 36442 MW; 6B312D8067060747 CRC64;
MSAEASGPAP AAAECLESPS PSSVEPGSPS YSLKPLTPNS KYVKLNVGGS LHYTTLRTLT
GQDTMLKAMF SGRVEVLTDA GGWVLIDRSG RHFGTILNYL RDGSVPLPES ARELGELLGE
ARYYLVQGLI EDCQLALQQK REKLSPLCLI PTVTSPREEQ QLLASTSKPV VKLLHNRSNN
KYSYTSTSDD NLLKNIELFD KLALRFHGRL LFLKDVLGDE ICCWSFYGQG RKIAEVCCTS
IVYATEKKQT KVEFPEARIF EETLNILIYE NSRGPDLALL EATGGAAGGG GAGRGDDEEN
REHRVRRIHV RRHITHDERP HGQQIVFKD
