BACD1_DANRE
ID BACD1_DANRE Reviewed; 330 AA.
AC A9ULR9; A8WGJ2; Q0P444;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1;
DE AltName: Full=BTB/POZ domain-containing protein KCTD13;
GN Name=kctd13 {ECO:0000312|ZFIN:ZDB-GENE-060825-162};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 (By
CC similarity). The BCR(KCTD13) E3 ubiquitin ligase complex mediates the
CC ubiquitination of RHOA, leading to its degradation by the proteasome,
CC thereby regulating the actin cytoskeleton and promoting synaptic
CC transmission (PubMed:29088697). {ECO:0000250|UniProtKB:Q8BGV7,
CC ECO:0000305|PubMed:29088697}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WZ19}.
CC -!- DISRUPTION PHENOTYPE: Increased levels of RHOA. N ochange in brain size
CC or neural progenitor cell proliferation is observed.
CC {ECO:0000269|PubMed:29088697}.
CC -!- SIMILARITY: Belongs to the BACURD family. {ECO:0000305}.
CC -!- CAUTION: According to a first report, morpholino-mediated knockdown of
CC kctd13 leads to increased brain size and cell proliferation
CC (PubMed:22596160). However, it was later shown that deletion of kctd13
CC does not cause any change in brain size or cell proliferation
CC (PubMed:29088697). Experimental conditions used may explain
CC discrepancies. A possible explanation being that morpholinos 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; CR855387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC122284; AAI22285.1; -; mRNA.
DR EMBL; BC154733; AAI54734.1; -; mRNA.
DR EMBL; BC157374; AAI57375.1; -; mRNA.
DR RefSeq; NP_001070619.1; NM_001077151.1.
DR AlphaFoldDB; A9ULR9; -.
DR SMR; A9ULR9; -.
DR STRING; 7955.ENSDARP00000065806; -.
DR PaxDb; A9ULR9; -.
DR Ensembl; ENSDART00000065807; ENSDARP00000065806; ENSDARG00000044769.
DR GeneID; 100000647; -.
DR KEGG; dre:100000647; -.
DR CTD; 253980; -.
DR ZFIN; ZDB-GENE-060825-162; kctd13.
DR eggNOG; KOG2716; Eukaryota.
DR GeneTree; ENSGT00950000183143; -.
DR HOGENOM; CLU_060008_0_0_1; -.
DR InParanoid; A9ULR9; -.
DR OMA; IYENNRR; -.
DR OrthoDB; 1306250at2759; -.
DR PhylomeDB; A9ULR9; -.
DR TreeFam; TF315649; -.
DR Reactome; R-DRE-9696264; RND3 GTPase cycle.
DR Reactome; R-DRE-9696270; RND2 GTPase cycle.
DR PRO; PR:A9ULR9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000044769; Expressed in brain and 22 other tissues.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:ZFIN.
DR GO; GO:0060322; P:head development; IMP:ZFIN.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:ZFIN.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:ZFIN.
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 GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..330
FT /note="BTB/POZ domain-containing adapter for CUL3-mediated
FT RhoA degradation protein 1"
FT /id="PRO_0000442771"
FT DOMAIN 40..108
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 29
FT /note="E -> D (in Ref. 2; AAI54734)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="S -> T (in Ref. 2; AAI54734)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="T -> I (in Ref. 2; AAI22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="K -> E (in Ref. 2; AAI54734)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="K -> E (in Ref. 2; AAI54734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 36385 MW; 18996790CC5D2AC9 CRC64;
MSAEASGSSG GHAVTVSGSS PSSSSHVGEE KPGRSLVSSK YVKLNVGGTL HYTTVQTLSK
EDSLLRSICD GSTEVSIDSE GWVVLDRCGR HFSLVLNFLR DGTVPLPDST RELEEVLKEA
QYYRLQGLVQ HCLSTLQKRR DVCRGCHIPM ITSAKEEQRM IATCRKPVVK LQNNRGNNKY
SYTSNSDDNL LKNIELFDKL GLRFNGRVLF IKDVLGDEIC CWSFYGEGRK IAEVCCTSIV
YATEKKQTKV EFPEARIFEE TLNILIYENG RGSGGMALLE SGGVSSSGAG QSEEEGAGAG
GGDRRVRRIH VRRHIMHDER GHGQQTVYKD
