BACD2_RAT
ID BACD2_RAT Reviewed; 316 AA.
AC Q7TNY1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2;
DE AltName: Full=BTB/POZ domain-containing protein TNFAIP1;
DE AltName: Full=Tumor necrosis factor-induced protein 1;
GN Name=Tnfaip1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH PCNA.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=15726626; DOI=10.1002/jez.a.150;
RA Zhou J., Hu X., Xiong X., Liu X., Liu Y., Ren K., Jiang T., Hu X.,
RA Zhang J.;
RT "Cloning of two rat PDIP1 related genes and their interactions with
RT proliferating cell nuclear antigen.";
RL J. Exp. Zool. A Comp. Exp. Biol. 303:227-240(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex involved in regulation of cytoskeleton
CC structure. The BCR(TNFAIP1) E3 ubiquitin ligase complex mediates the
CC ubiquitination of RHOA, leading to its degradation by the proteasome,
CC thereby regulating the actin cytoskeleton and cell migration. Its
CC interaction with RHOB may regulate apoptosis (By similarity). May
CC enhance the PCNA-dependent DNA polymerase delta activity. {ECO:0000250,
CC ECO:0000269|PubMed:15726626}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the BCR(TNFAIP1) E3 ubiquitin ligase complex, at
CC least composed of CUL3, TNFAIP1/BACURD2 and RBX1. Interacts with RHOA;
CC with a preference for RhoA-GDP. Interacts with RHOB. Interacts with
CC CSNK2B (By similarity). Interacts with PCNA. {ECO:0000250,
CC ECO:0000269|PubMed:15726626}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Endosome {ECO:0000250}. Note=Colocalizes with RHOB in endosomes.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-280 by CK2 facilitates the nucleus
CC localization and increases interaction with PCNA. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BACURD family. {ECO:0000305}.
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; AY336949; AAP97077.1; -; mRNA.
DR EMBL; BC128704; AAI28705.1; -; mRNA.
DR RefSeq; NP_891995.1; NM_182950.4.
DR AlphaFoldDB; Q7TNY1; -.
DR SMR; Q7TNY1; -.
DR BioGRID; 252226; 1.
DR STRING; 10116.ENSRNOP00000012245; -.
DR iPTMnet; Q7TNY1; -.
DR PhosphoSitePlus; Q7TNY1; -.
DR jPOST; Q7TNY1; -.
DR PaxDb; Q7TNY1; -.
DR Ensembl; ENSRNOT00000012245; ENSRNOP00000012245; ENSRNOG00000009069.
DR GeneID; 287543; -.
DR KEGG; rno:287543; -.
DR CTD; 7126; -.
DR RGD; 3877; Tnfaip1.
DR eggNOG; KOG2716; Eukaryota.
DR GeneTree; ENSGT00950000183143; -.
DR HOGENOM; CLU_060008_0_0_1; -.
DR InParanoid; Q7TNY1; -.
DR OMA; EMSGDTC; -.
DR OrthoDB; 1306250at2759; -.
DR PhylomeDB; Q7TNY1; -.
DR TreeFam; TF315649; -.
DR Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q7TNY1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000009069; Expressed in lung and 19 other tissues.
DR Genevisible; Q7TNY1; RN.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030332; F:cyclin binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:RGD.
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.
PE 1: Evidence at protein level;
KW Cytoplasm; Endosome; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..316
FT /note="BTB/POZ domain-containing adapter for CUL3-mediated
FT RhoA degradation protein 2"
FT /id="PRO_0000331249"
FT DOMAIN 28..96
FT /note="BTB"
FT REGION 268..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13829"
FT MOD_RES 280
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q13829"
SQ SEQUENCE 316 AA; 36046 MW; 9F55209382D736E3 CRC64;
MSGDTCLCPA SGAKPKISGF KGGGLGNKYV QLNVGGSLHY TTVRALTRHD TMLKAMFSGR
MEVLTDKEGW ILIDRCGKHF GTILNYLRDD TVTLPQSRQE IQELMAEAKY YLIQGLVSLC
QAALQDKKDS YQPVCNIPII TSLREEDRLI ESSTKPVVKL LYNRSNNKYS YTSNSDDHLL
KNIELFDKLS LRFNGRVLFI KDVIGDEICC WSFYGQGRKL AEVCCTSIVY ATEKKQTKVE
FPEARIYEET LNVLLYETPR VPDNSLLEAT SRSRSQASPS EDEDTFELRD RVRRIHVKRY
STYDDRQLGH QSAHRD
