TONSL_RAT
ID TONSL_RAT Reviewed; 1367 AA.
AC D4A615;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Tonsoku-like protein {ECO:0000305};
DE AltName: Full=Inhibitor of kappa B-related protein;
DE Short=I-kappa-B-related protein;
DE Short=IkappaBR;
DE AltName: Full=NF-kappa-B inhibitor-like protein 2;
DE AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 2;
GN Name=Tonsl {ECO:0000312|RGD:1307483}; Synonyms=Ikbr, Nfkbil2;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the MMS22L-TONSL complex, a complex that
CC promotes homologous recombination-mediated repair of double-strand
CC breaks (DSBs) at stalled or collapsed replication forks. The MMS22L-
CC TONSL complex is required to maintain genome integrity during DNA
CC replication. It mediates the assembly of RAD51 filaments on single-
CC stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs
CC following histone replacement by histone chaperones and eviction of the
CC replication protein A complex (RPA/RP-A) from DSBs. Following
CC recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of
CC RAD51 filaments and subsequent homologous recombination. Within the
CC complex, TONSL acts as histone reader, which recognizes and binds newly
CC synthesized histones following their replacement by histone chaperones.
CC Specifically binds histone H4 lacking methylation at 'Lys-20'
CC (H4K20me0) and histone H3.1. {ECO:0000250|UniProtKB:Q96HA7}.
CC -!- SUBUNIT: Component of the MMS22L-TONSL complex, a complex at least
CC composed of MMS22L and TONSL/NFKBIL2. Interacts with the MCM complex,
CC the FACT complex and the RPA complex. Interacts with MCM5; the
CC interaction is direct. Binds histones, with a strong preference for
CC histone H3.1 (histones H3.1 and H3-4/H3.1t). Interacts (via ANK
CC repeats) with histone H4; specifically binds histone H4 lacking
CC methylation at 'Lys-20' (H4K20me0). May interact with DNAJC9; the
CC interaction seems to be histone-dependent.
CC {ECO:0000250|UniProtKB:Q96HA7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96HA7}.
CC Chromosome {ECO:0000250|UniProtKB:Q96HA7}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96HA7}. Note=Mainly nuclear. Localizes to DNA
CC damage sites, accumulates at stressed replication forks. Recruited to
CC stalled or collapsed replication forks following histone replacement by
CC histone chaperones ASF1A and the CAF-1 complex: TONSL acts as histone
CC reader that recognizes and binds newly synthesized histones.
CC {ECO:0000250|UniProtKB:Q96HA7}.
CC -!- DOMAIN: The ANK repeats mediate the interaction with the MCM complex
CC and histones, while the LRR repeats mediate the interaction with
CC MMS22L. {ECO:0000250|UniProtKB:Q96HA7}.
CC -!- SIMILARITY: Belongs to the Tonsoku 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; CH473950; EDM15953.1; -; Genomic_DNA.
DR RefSeq; NP_001124044.1; NM_001130572.1.
DR AlphaFoldDB; D4A615; -.
DR SMR; D4A615; -.
DR STRING; 10116.ENSRNOP00000019754; -.
DR PaxDb; D4A615; -.
DR PRIDE; D4A615; -.
DR Ensembl; ENSRNOT00000019754; ENSRNOP00000019754; ENSRNOG00000014703.
DR GeneID; 366953; -.
DR KEGG; rno:366953; -.
DR UCSC; RGD:1307483; rat.
DR CTD; 4796; -.
DR RGD; 1307483; Tonsl.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4308; Eukaryota.
DR GeneTree; ENSGT00940000160188; -.
DR HOGENOM; CLU_002128_0_0_1; -.
DR InParanoid; D4A615; -.
DR OMA; AEICEQQ; -.
DR OrthoDB; 56880at2759; -.
DR PhylomeDB; D4A615; -.
DR TreeFam; TF326440; -.
DR PRO; PR:D4A615; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000014703; Expressed in thymus and 15 other tissues.
DR Genevisible; D4A615; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005662; C:DNA replication factor A complex; IEA:Ensembl.
DR GO; GO:0035101; C:FACT complex; IEA:Ensembl.
DR GO; GO:0042555; C:MCM complex; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0140566; F:histone reader activity; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13516; LRR_6; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00367; LRR_CC; 2.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 3: Inferred from homology;
KW ANK repeat; Chromatin regulator; Chromosome; Cytoplasm; DNA damage;
KW DNA repair; Leucine-rich repeat; Methylation; Nucleus; Reference proteome;
KW Repeat; TPR repeat.
FT CHAIN 1..1367
FT /note="Tonsoku-like protein"
FT /id="PRO_0000403775"
FT REPEAT 27..60
FT /note="TPR 1"
FT REPEAT 67..100
FT /note="TPR 2"
FT REPEAT 107..147
FT /note="TPR 3"
FT REPEAT 162..195
FT /note="TPR 4"
FT REPEAT 202..235
FT /note="TPR 5"
FT REPEAT 242..275
FT /note="TPR 6"
FT REPEAT 311..344
FT /note="TPR 7"
FT REPEAT 352..385
FT /note="TPR 8"
FT REPEAT 390..424
FT /note="TPR 9"
FT REPEAT 528..557
FT /note="ANK 1"
FT REPEAT 561..590
FT /note="ANK 2"
FT REPEAT 597..626
FT /note="ANK 3"
FT REPEAT 1062..1086
FT /note="LRR 1"
FT REPEAT 1090..1118
FT /note="LRR 2"
FT REPEAT 1121..1144
FT /note="LRR 3"
FT REPEAT 1181..1205
FT /note="LRR 4"
FT REPEAT 1240..1263
FT /note="LRR 5"
FT REPEAT 1268..1293
FT /note="LRR 6"
FT REPEAT 1324..1347
FT /note="LRR 7"
FT REGION 460..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..505
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 797
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZL6"
SQ SEQUENCE 1367 AA; 151834 MW; 417911B44EB11B17 CRC64;
MTLEQELRQL SKAKARAQRN GQLCEEAVCC HQLGELLASH GRFQEALEEH QQELHLLESV
QDTLGCAVAH RKIGERLAEM ENYSAALKHQ HLYLDLAGSL SNHTELQRAW ATIGRTHLDV
YDHCQSRDSL LQAQAAFEKS LAIVDEKLEG MLTQRELSEM RTRLYLNLGL TCESLQQTAQ
CNNYFKKSIF LAEQNHLYED LFRARYNLGA IHWRGGQHSQ AMRCLEGARE CARAMKMRFM
ESECCMLVSQ VLQDLGDFLA AKRALKKAYR LGSQKPNQRV AICQSLKYVL AVVRLQQQLQ
EAEGNDLQGA MAICEQLGDL FSKADDFPKA SEAYQKQLHF AELLNRPDLE LAVIHESLAT
TLGDMKDYHK AVHHYEEELR LRKGNALEEA KTWFNIGLAR EEAGDAYELL APCFQKAFGC
AQQAQRYQLQ RQILQHLYTV QLKLQPQEAR DTEIRLQELS MAKDTEEEEE EEEEEEEEAS
EALETSEMEL SESEDDADGL SQQLEEEEEL QGCVGRRKIN KWNRRNDMGE TLLHRACIEG
QLRRVQDLVK QGHPLNPRDY CGWTPLHEAC NYGHLEIVRF LLDHGAAVDD PGGQGCDGIT
PLHDALNCGH FEVAELLIER GASVTLRTRK GLSPLETLQQ WVKLYFRDLD LETRQKAASM
ERRLQMASSG QASHSSPALQ TIPNNHLFDP ETSPPSSPCP KPPSYTPRPP EASPAPAKVF
LEETVSAVCR PRKNRHRPAS SSSSSEDDDD NTNPCRPSQK RLRHSTQQGE AKTPDPSKSR
ETAISSACRA AYQAAIRGVG SAQSRRLVPS LPRGSNEVPA PKTALIPEEE FLAEEWLEVD
TPLTRSSSSS RPSTSISDYE RCPARPRTRA KQSRPASLDG WCTRTKAADA SLTAEPTENS
SMPRTTGPNK ENCAAGQPLL LVQPPPIRVR VQIQDNLFLI PVPHSDVHSV AWLAEQAAQR
YFQTCGLLPR LTLRKDGALL APQDPIPDVL QSNDEVMAEV TSWDLPPLKD RYRRACQSLG
QGEHQQVLQA MEHQSSSPSF SACSLALCQA QLTPLLRALK LHTALRELRL SGNRLGDPCA
TELLATLGTM PNLVLLDLSS NHLGPEGLRQ LVEGSLGQTA FQNVEELDLS MNPLGDGCAQ
ALASLLRTCP VLRTLRLQAC GFSPSFFLSH QAALGSAFKD AEHLKTLSLS YNTLGAPALA
RVLQSLPTCT LLHLELSSVA ASKSNSSLIE PVIKYLTKEG CALAHLTLSA NCLSDKAVRE
LSRCLPSCPS LTSLDLSANP EVSCAGLEEL LSALQERPQG LSFFDLSGCS IQGPLNSDLW
DKILSQLQEL QLCSKDLTTK DRDTLCQRLP AGACTLNQGS KLFFKCL
