ID BACD1_HUMAN Reviewed; 329 AA. AC Q8WZ19; A8K0R5; Q96P93; Q96SA1; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 175. DE RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1 {ECO:0000303|PubMed:19782033}; DE Short=hBACURD1 {ECO:0000303|PubMed:19782033}; DE AltName: Full=BTB/POZ domain-containing protein KCTD13 {ECO:0000305}; DE AltName: Full=Polymerase delta-interacting protein 1 {ECO:0000303|PubMed:11593007}; DE AltName: Full=TNFAIP1-like protein; GN Name=KCTD13; GN Synonyms=BACURD1 {ECO:0000303|PubMed:19782033}, PDIP1 GN {ECO:0000303|PubMed:11593007}, POLDIP1; ORFNames=FKSG86, PP6832; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH PCNA AND RP POLD2, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=11593007; DOI=10.1073/pnas.221452098; RA He H., Tan C.-K., Downey K.M., So A.G.; RT "A tumor necrosis factor alpha- and interleukin 6-inducible protein that RT interacts with the small subunit of DNA polymerase delta and proliferating RT cell nuclear antigen."; RL Proc. Natl. Acad. Sci. U.S.A. 98:11979-11984(2001). RN [2] RP SEQUENCE REVISION. RA He H., Tan C.-K., Downey K.M., So A.G.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wang Y.-G., Gong L.; RT "Cloning and characterization of FKSG86, a novel gene encoding a TNFAIP1- RT like protein."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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 [9] RP FUNCTION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE RP COMPLEX, INTERACTION WITH RHOA, AND MUTAGENESIS OF 84-VAL--ILE-86. RX PubMed=19782033; DOI=10.1016/j.molcel.2009.09.004; RA Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M., RA Peng H.B., Shao F.; RT "Cullin mediates degradation of RhoA through evolutionarily conserved BTB RT adaptors to control actin cytoskeleton structure and cell movement."; RL Mol. Cell 35:841-855(2009). RN [10] RP INTERACTION WITH SPRTN. RX PubMed=22902628; DOI=10.1074/jbc.m112.400135; RA Ghosal G., Leung J.W., Nair B.C., Fong K.W., Chen J.; RT "Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is a RT regulator of translesion synthesis."; RL J. Biol. Chem. 287:34225-34233(2012). RN [11] RP POSSIBLE DISEASE MODIFIER FOR AUTISM AND SCHIZOPHRENIA. 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 [12] RP POSSIBLE DISEASE MODIFIER FOR AUTISM AND SCHIZOPHRENIA. RX PubMed=25695269; DOI=10.1016/j.neuron.2015.01.010; RA Lin G.N., Corominas R., Lemmens I., Yang X., Tavernier J., Hill D.E., RA Vidal M., Sebat J., Iakoucheva L.M.; RT "Spatiotemporal 16p11.2 protein network implicates cortical late mid-fetal RT brain development and KCTD13-Cul3-RhoA pathway in psychiatric diseases."; RL Neuron 85:742-754(2015). RN [13] RP VARIANT ASN-200. RX PubMed=27668412; DOI=10.1097/ypg.0000000000000145; RA Degenhardt F., Heinemann B., Strohmaier J., Pfohl M.A., Giegling I., RA Hofmann A., Ludwig K.U., Witt S.H., Ludwig M., Forstner A.J., Albus M., RA Schwab S.G., Borrmann-Hassenbach M., Lennertz L., Wagner M., Hoffmann P., RA Rujescu D., Maier W., Cichon S., Rietschel M., Noethen M.M.; RT "Identification of rare variants in KCTD13 at the schizophrenia risk locus RT 16p11.2."; RL Psychiatr. Genet. 26:293-296(2016). RN [14] {ECO:0007744|PDB:4UIJ} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 27-144, AND SUBUNIT. RX PubMed=28963344; DOI=10.1042/bcj20170527; RA Pinkas D.M., Sanvitale C.E., Bufton J.C., Sorrell F.J., Solcan N., RA Chalk R., Doutch J., Bullock A.N.; RT "Structural complexity in the KCTD family of Cullin3-dependent E3 ubiquitin RT ligases."; RL Biochem. J. 474:3747-3761(2017). CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 CC ubiquitin-protein ligase complex required for synaptic transmission CC (PubMed:19782033). The BCR(KCTD13) E3 ubiquitin ligase complex mediates CC the ubiquitination of RHOA, leading to its degradation by the CC proteasome (PubMed:19782033) Degradation of RHOA regulates the actin CC cytoskeleton and promotes synaptic transmission (By similarity). CC {ECO:0000250|UniProtKB:Q8BGV7, ECO:0000269|PubMed:19782033}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:19782033}. CC -!- SUBUNIT: Homotetramer; forms a two-fold symmetric tetramer in solution CC (PubMed:28963344). Interacts with CUL3; interaction is direct and forms CC a 5:5 heterodecamer (PubMed:28963344). Component of the BCR(KCTD13) E3 CC ubiquitin ligase complex, at least composed of CUL3, KCTD13/BACURD1 and CC RBX1. Interacts with RHOA; with a preference for RhoA-GDP CC (PubMed:19782033). Interacts with POLD2 and PCNA (PubMed:11593007). CC Interacts with SPRTN (PubMed:22902628). {ECO:0000269|PubMed:11593007, CC ECO:0000269|PubMed:19782033, ECO:0000269|PubMed:22902628, CC ECO:0000269|PubMed:28963344}. CC -!- INTERACTION: CC Q8WZ19; Q9H6L4: ARMC7; NbExp=4; IntAct=EBI-742916, EBI-742909; CC Q8WZ19; O95817: BAG3; NbExp=3; IntAct=EBI-742916, EBI-747185; CC Q8WZ19; Q16543: CDC37; NbExp=3; IntAct=EBI-742916, EBI-295634; CC Q8WZ19; Q13618: CUL3; NbExp=8; IntAct=EBI-742916, EBI-456129; CC Q8WZ19; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-742916, EBI-371876; CC Q8WZ19; P21333-2: FLNA; NbExp=3; IntAct=EBI-742916, EBI-9641086; CC Q8WZ19; P51114: FXR1; NbExp=2; IntAct=EBI-742916, EBI-713291; CC Q8WZ19; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-742916, EBI-739467; CC Q8WZ19; P04792: HSPB1; NbExp=3; IntAct=EBI-742916, EBI-352682; CC Q8WZ19; Q9H3F6: KCTD10; NbExp=4; IntAct=EBI-742916, EBI-2505886; CC Q8WZ19; Q8WZ19: KCTD13; NbExp=6; IntAct=EBI-742916, EBI-742916; CC Q8WZ19; O60333-2: KIF1B; NbExp=3; IntAct=EBI-742916, EBI-10975473; CC Q8WZ19; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-742916, EBI-739832; CC Q8WZ19; P31153: MAT2A; NbExp=3; IntAct=EBI-742916, EBI-1050743; CC Q8WZ19; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-742916, EBI-741158; CC Q8WZ19; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-742916, EBI-473160; CC Q8WZ19; O15160: POLR1C; NbExp=3; IntAct=EBI-742916, EBI-1055079; CC Q8WZ19; P60891: PRPS1; NbExp=3; IntAct=EBI-742916, EBI-749195; CC Q8WZ19; P25786: PSMA1; NbExp=3; IntAct=EBI-742916, EBI-359352; CC Q8WZ19; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-742916, EBI-396669; CC Q8WZ19; Q13829: TNFAIP1; NbExp=11; IntAct=EBI-742916, EBI-2505861; CC Q8WZ19; O76024: WFS1; NbExp=3; IntAct=EBI-742916, EBI-720609; CC Q8WZ19; Q96E35: ZMYND19; NbExp=7; IntAct=EBI-742916, EBI-746595; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11593007}. CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues. CC {ECO:0000269|PubMed:11593007}. CC -!- INDUCTION: By TNF and IL6/interleukin-6. {ECO:0000269|PubMed:11593007}. CC -!- DISEASE: Note=The gene represented in this entry may act as a disease CC modifier for autism and schizophrenia associated with recurrent CC deletions and duplications of chromosome 16p11.2 region CC (PubMed:22596160, PubMed:25695269). {ECO:0000269|PubMed:22596160, CC ECO:0000269|PubMed:25695269}. CC -!- SIMILARITY: Belongs to the BACURD family. {ECO:0000305}. CC -!- CAUTION: Baed on animal models in mouse and zebrafish, it was suggested CC that KCTD13 is the major factor inducing the macrocephaly phenotype CC associated with the 16p11.2 deletion (PubMed:22596160). However, a CC subsequent report showed that KCTD13 does not play a role in brain CC size. {ECO:0000269|PubMed:22596160}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF401315; AAL14962.2; -; mRNA. DR EMBL; AY027918; AAK27301.1; -; mRNA. DR EMBL; AF289573; AAL55757.1; -; mRNA. DR EMBL; AK289630; BAF82319.1; -; mRNA. DR EMBL; AC120114; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471238; EAW79969.1; -; Genomic_DNA. DR EMBL; BC036228; AAH36228.1; -; mRNA. DR CCDS; CCDS10661.1; -. DR RefSeq; NP_849194.1; NM_178863.4. DR PDB; 4UIJ; X-ray; 2.70 A; A/B/C/D=27-144. DR PDBsum; 4UIJ; -. DR AlphaFoldDB; Q8WZ19; -. DR SMR; Q8WZ19; -. DR BioGRID; 129001; 51. DR IntAct; Q8WZ19; 37. DR MINT; Q8WZ19; -. DR STRING; 9606.ENSP00000455785; -. DR iPTMnet; Q8WZ19; -. DR PhosphoSitePlus; Q8WZ19; -. DR BioMuta; KCTD13; -. DR DMDM; 51701604; -. DR EPD; Q8WZ19; -. DR jPOST; Q8WZ19; -. DR MassIVE; Q8WZ19; -. DR MaxQB; Q8WZ19; -. DR PaxDb; 9606-ENSP00000455785; -. DR PeptideAtlas; Q8WZ19; -. DR ProteomicsDB; 75205; -. DR Pumba; Q8WZ19; -. DR Antibodypedia; 13396; 170 antibodies from 18 providers. DR DNASU; 253980; -. DR Ensembl; ENST00000308768.9; ENSP00000311202.5; ENSG00000174943.11. DR Ensembl; ENST00000568000.6; ENSP00000455785.1; ENSG00000174943.11. DR GeneID; 253980; -. DR KEGG; hsa:253980; -. DR MANE-Select; ENST00000568000.6; ENSP00000455785.1; NM_178863.5; NP_849194.1. DR UCSC; uc002duv.5; human. DR AGR; HGNC:22234; -. DR CTD; 253980; -. DR DisGeNET; 253980; -. DR GeneCards; KCTD13; -. DR HGNC; HGNC:22234; KCTD13. DR HPA; ENSG00000174943; Tissue enhanced (testis). DR MIM; 608947; gene. DR neXtProt; NX_Q8WZ19; -. DR OpenTargets; ENSG00000174943; -. DR PharmGKB; PA134907908; -. DR VEuPathDB; HostDB:ENSG00000174943; -. DR eggNOG; KOG2716; Eukaryota. DR GeneTree; ENSGT00950000183143; -. DR HOGENOM; CLU_060008_0_0_1; -. DR InParanoid; Q8WZ19; -. DR OMA; PPLENCA; -. DR OrthoDB; 2912088at2759; -. DR PhylomeDB; Q8WZ19; -. DR TreeFam; TF315649; -. DR PathwayCommons; Q8WZ19; -. DR Reactome; R-HSA-9696264; RND3 GTPase cycle. DR Reactome; R-HSA-9696270; RND2 GTPase cycle. DR SignaLink; Q8WZ19; -. DR SIGNOR; Q8WZ19; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 253980; 14 hits in 1164 CRISPR screens. DR ChiTaRS; KCTD13; human. DR GeneWiki; KCTD13; -. DR GenomeRNAi; 253980; -. DR Pharos; Q8WZ19; Tbio. DR PRO; PR:Q8WZ19; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q8WZ19; Protein. DR Bgee; ENSG00000174943; Expressed in right testis and 160 other cell types or tissues. DR ExpressionAtlas; Q8WZ19; baseline and differential. DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB. DR GO; GO:0016477; P:cell migration; IMP:UniProtKB. DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB. DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISS:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB. DR CDD; cd18400; BTB_POZ_KCTD13_BACURD1; 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; BTB/POZ DOMAIN-CONTAINING ADAPTER FOR CUL3-MEDIATED RHOA DEGRADATION PROTEIN FAMILY MEMBER; 1. DR PANTHER; PTHR11145:SF18; BTB_POZ DOMAIN-CONTAINING ADAPTER FOR CUL3-MEDIATED RHOA DEGRADATION PROTEIN 1; 1. DR Pfam; PF02214; BTB_2; 1. DR SMART; SM00225; BTB; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50097; BTB; 1. DR Genevisible; Q8WZ19; HS. PE 1: Evidence at protein level; KW 3D-structure; Autism; Autism spectrum disorder; Disease variant; Nucleus; KW Reference proteome; Schizophrenia; 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_0000191297" 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" FT REGION 282..303 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 200 FT /note="D -> N (found in a patient with schizophrenia; FT uncertain significance; dbSNP:rs774536350)" FT /evidence="ECO:0000269|PubMed:27668412" FT /id="VAR_080045" FT MUTAGEN 84..86 FT /note="VLI->AAA: Abolishes interaction with CUL3 and FT induces abnormal actin stress fibers." FT /evidence="ECO:0000269|PubMed:19782033" FT CONFLICT 251 FT /note="K -> N (in Ref. 3; AAK27301)" FT /evidence="ECO:0000305" FT CONFLICT 328 FT /note="K -> R (in Ref. 3; AAK27301)" FT /evidence="ECO:0000305" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:4UIJ" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:4UIJ" FT HELIX 56..59 FT /evidence="ECO:0007829|PDB:4UIJ" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:4UIJ" FT HELIX 65..69 FT /evidence="ECO:0007829|PDB:4UIJ" FT TURN 70..72 FT /evidence="ECO:0007829|PDB:4UIJ" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:4UIJ" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:4UIJ" FT HELIX 93..102 FT /evidence="ECO:0007829|PDB:4UIJ" FT HELIX 111..123 FT /evidence="ECO:0007829|PDB:4UIJ" FT HELIX 127..140 FT /evidence="ECO:0007829|PDB:4UIJ" SQ SEQUENCE 329 AA; 36357 MW; 17A8AC2DBE81EE78 CRC64; MSAEASGPAA AAAPSLEAPK PSGLEPGPAA YGLKPLTPNS KYVKLNVGGS LHYTTLRTLT GQDTMLKAMF SGRVEVLTDA GGWVLIDRSG RHFGTILNYL RDGSVPLPES TRELGELLGE ARYYLVQGLI EDCQLALQQK RETLSPLCLI PMVTSPREEQ QLLASTSKPV VKLLHNRSNN KYSYTSTSDD NLLKNIELFD KLALRFHGRL LFLKDVLGDE ICCWSFYGQG RKIAEVCCTS IVYATEKKQT KVEFPEARIF EETLNILIYE TPRGPDPALL EATGGAAGAG GAGRGEDEEN REHRVRRIHV RRHITHDERP HGQQIVFKD //