BACD2_PONAB
ID BACD2_PONAB Reviewed; 316 AA.
AC Q5RBH4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2;
DE AltName: Full=BTB/POZ domain-containing protein TNFAIP1;
GN Name=TNFAIP1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. May enhance the PCNA-
CC dependent DNA polymerase delta activity (By similarity). {ECO:0000250}.
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 PCNA. Interacts with CSNK2B (By similarity). {ECO:0000250}.
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}.
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DR EMBL; CR858674; CAH90886.1; -; mRNA.
DR RefSeq; NP_001125505.1; NM_001132033.1.
DR AlphaFoldDB; Q5RBH4; -.
DR SMR; Q5RBH4; -.
DR STRING; 9601.ENSPPYP00000009095; -.
DR Ensembl; ENSPPYT00000009465; ENSPPYP00000009095; ENSPPYG00000008088.
DR GeneID; 100172414; -.
DR KEGG; pon:100172414; -.
DR CTD; 7126; -.
DR eggNOG; KOG2716; Eukaryota.
DR GeneTree; ENSGT00950000183143; -.
DR InParanoid; Q5RBH4; -.
DR OrthoDB; 1306250at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Chromosome 17.
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:0042802; F:identical protein binding; IEA:Ensembl.
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: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 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_0000331248"
FT DOMAIN 28..96
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
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; 36151 MW; D20B954F14157DCF CRC64;
MSGDTCLCPA SGAKPKLSGF KGGGLGNKYV QLNVGGSLYY TTVRALTRHD TMLKAMFSGR
MEVLTDKEGW ILIDRCGKHF GTILNYLRDD TITLPQNRQE IKELMAEAKY YLIQGLVNMC
QSALQDKKDS YQPVCNIPII TSLKEEERLI ESSTKPVVKL LYNRSNNKYS YTSNSDDHLL
KNIELFDKLS LRFNGRVLFI KDVIGDEICC WSFYGQGRKL AEVCCTSIVY ATEKKQTKVE
FPEARIYEET LNVLLYETPR VPDNSLLEAT SRSCSQASPS EDEETFELRD RVRRIHVKRY
STYDDRQLGH QSTHRD