BACD2_MOUSE
ID BACD2_MOUSE Reviewed; 316 AA.
AC O70479; Q3TH85; Q3UGQ5; Q8BV61; Q8BZK5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
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, alpha-induced protein 1, endothelial;
GN Name=Tnfaip1; Synonyms=Edp1;
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 [GENOMIC DNA].
RX PubMed=9804998; DOI=10.1016/s0167-4781(98)00180-8;
RA Swift S., Blackburn C., Morahan G., Ashworth A.;
RT "Structure and chromosomal mapping of the TNF-alpha inducible endothelial
RT protein 1 (Edp1) gene in the mouse.";
RL Biochim. Biophys. Acta 1442:394-398(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Diencephalon, Lung, and Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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. 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}.
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; AF061346; AAC78826.1; -; Genomic_DNA.
DR EMBL; AF061341; AAC78826.1; JOINED; Genomic_DNA.
DR EMBL; AF061342; AAC78826.1; JOINED; Genomic_DNA.
DR EMBL; AF061343; AAC78826.1; JOINED; Genomic_DNA.
DR EMBL; AF061344; AAC78826.1; JOINED; Genomic_DNA.
DR EMBL; AF061345; AAC78826.1; JOINED; Genomic_DNA.
DR EMBL; AK004593; BAB23395.1; -; mRNA.
DR EMBL; AK034305; BAC28668.1; -; mRNA.
DR EMBL; AK079869; BAC37770.1; -; mRNA.
DR EMBL; AK147809; BAE28152.1; -; mRNA.
DR EMBL; AK168386; BAE40313.1; -; mRNA.
DR EMBL; AK168704; BAE40546.1; -; mRNA.
DR EMBL; AL591177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003906; AAH03906.1; -; mRNA.
DR CCDS; CCDS25110.1; -.
DR RefSeq; NP_001152864.1; NM_001159392.1.
DR RefSeq; NP_033421.3; NM_009395.4.
DR AlphaFoldDB; O70479; -.
DR SMR; O70479; -.
DR MINT; O70479; -.
DR STRING; 10090.ENSMUSP00000103912; -.
DR iPTMnet; O70479; -.
DR PhosphoSitePlus; O70479; -.
DR EPD; O70479; -.
DR MaxQB; O70479; -.
DR PaxDb; O70479; -.
DR PeptideAtlas; O70479; -.
DR PRIDE; O70479; -.
DR ProteomicsDB; 273533; -.
DR Antibodypedia; 2839; 299 antibodies from 32 providers.
DR DNASU; 21927; -.
DR Ensembl; ENSMUST00000017759; ENSMUSP00000017759; ENSMUSG00000017615.
DR Ensembl; ENSMUST00000108277; ENSMUSP00000103912; ENSMUSG00000017615.
DR GeneID; 21927; -.
DR KEGG; mmu:21927; -.
DR UCSC; uc007kjq.2; mouse.
DR CTD; 7126; -.
DR MGI; MGI:104961; Tnfaip1.
DR VEuPathDB; HostDB:ENSMUSG00000017615; -.
DR eggNOG; KOG2716; Eukaryota.
DR GeneTree; ENSGT00950000183143; -.
DR HOGENOM; CLU_060008_0_0_1; -.
DR InParanoid; O70479; -.
DR OMA; EMSGDTC; -.
DR OrthoDB; 1306250at2759; -.
DR PhylomeDB; O70479; -.
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; 21927; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Tnfaip1; mouse.
DR PRO; PR:O70479; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O70479; protein.
DR Bgee; ENSMUSG00000017615; Expressed in paneth cell and 269 other tissues.
DR Genevisible; O70479; MM.
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; ISO:MGI.
DR GO; GO:0042802; F:identical protein 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: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; ISO:MGI.
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_0000331247"
FT DOMAIN 28..96
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 268..288
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"
FT CONFLICT 94
FT /note="L -> H (in Ref. 2; BAC28668)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="E -> G (in Ref. 2; BAE40313)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="R -> G (in Ref. 2; BAE28152)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 36134 MW; 9D8E141B0BE311EC CRC64;
MSGDTCLCPA SGAKPKISGF KGGGLGNKYV QLNVGGSLYY TTVRALTRHD TMLKAMFSGR
MEVLTDKEGW ILIDRCGKHF GTILNYLRDD TITLPQSRQE IQELMAEAKY YLIQGLVSTC
QTALQDKKDS YQPVCNIPII TSLREEDRLI ESSTKPVVKL LYNRSNNKYS YTSNSDDHLL
KNIELFDKLS LRFNGRVLFI KDVIGDEICC WSFYGQGRKL AEVCCTSIVY ATEKKQTKVE
FPEARIYEET LNVLLYETPR VPDNSLLEAT SRSRSQASPS EDEDTFELRD RVRRIHVKRY
STYDDRQLGH QSTHRD
