TONSL_BOVIN
ID TONSL_BOVIN Reviewed; 1374 AA.
AC Q0P5G1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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; Synonyms=IKBR, NFKBIL2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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; BC120084; AAI20085.1; -; mRNA.
DR RefSeq; NP_001068656.1; NM_001075188.1.
DR AlphaFoldDB; Q0P5G1; -.
DR SMR; Q0P5G1; -.
DR STRING; 9913.ENSBTAP00000010191; -.
DR PaxDb; Q0P5G1; -.
DR PRIDE; Q0P5G1; -.
DR Ensembl; ENSBTAT00000010191; ENSBTAP00000010191; ENSBTAG00000007749.
DR GeneID; 505102; -.
DR KEGG; bta:505102; -.
DR CTD; 4796; -.
DR VEuPathDB; HostDB:ENSBTAG00000007749; -.
DR VGNC; VGNC:36220; TONSL.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4308; Eukaryota.
DR GeneTree; ENSGT00940000160188; -.
DR HOGENOM; CLU_002128_0_0_1; -.
DR InParanoid; Q0P5G1; -.
DR OMA; AEICEQQ; -.
DR OrthoDB; 56880at2759; -.
DR TreeFam; TF326440; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000007749; Expressed in nasopharynx and 106 other tissues.
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; 3.
DR Pfam; PF13181; TPR_8; 1.
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; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 2: Evidence at transcript level;
KW ANK repeat; Chromatin regulator; Chromosome; Cytoplasm; DNA damage;
KW DNA repair; Leucine-rich repeat; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..1374
FT /note="Tonsoku-like protein"
FT /id="PRO_0000326633"
FT REPEAT 27..60
FT /note="TPR 1"
FT REPEAT 67..100
FT /note="TPR 2"
FT REPEAT 107..140
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 526..558
FT /note="ANK 1"
FT REPEAT 559..591
FT /note="ANK 2"
FT REPEAT 595..627
FT /note="ANK 3"
FT REPEAT 1065..1089
FT /note="LRR 1"
FT REPEAT 1093..1121
FT /note="LRR 2"
FT REPEAT 1124..1147
FT /note="LRR 3"
FT REPEAT 1184..1207
FT /note="LRR 4"
FT REPEAT 1243..1266
FT /note="LRR 5"
FT REPEAT 1271..1296
FT /note="LRR 6"
FT REPEAT 1327..1350
FT /note="LRR 7"
FT REGION 460..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..502
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HA7"
FT MOD_RES 788
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6NZL6"
SQ SEQUENCE 1374 AA; 150245 MW; D75D0ED6B387DDB6 CRC64;
MSLERELRQL SKAKTKAQRS GQLREEASVC HQLGELLASH GCYAEALREH QQELQLLETT
DDPLGCAVAH RKIGERLAEM EDYSAALQHQ HRYLELACAL SNHVEQQRAW ATIGRTHLDI
YDHHQSQDAL QQAQDAFEKS LAILDEKLQG SLPKRELSEM RTRIYLNLGL TCESLQQVAL
CSAYFKKSIF LAEQNHLYED LFRARYNLGA IHWRRGQHSQ AMRCLEGARE CARVLKQAFL
ESECCLLLSQ VLLDLGDFLA AKRALKKAYR LGSQKPLQKA SVCRTLKYVL AVVQLQQRLE
ESEESDPEVA MGICEQLGDL FSKAGDFPKA AAAYQKQLRF AELLSRPGPE LAVIHVSLAA
TLGDMKDHRQ AVHHYEAELK LQEGNPLEEA KTWLNIALSR EEAGDAYEVL ALCFQKALGC
AQLAGQPQLQ RQILQHLHAV QLRLQPQEAP STETRLQELK AAGDEDEGDG EDEEDEEDDD
ALEATELELS ESENEADASP PLEEDEELRG CLGRQRVNKW SRRNDVGETL LHRACIEGQL
GRVQDLVRQG HPLNPRDYCG WTPLHEACNY GHLDIVRFLL DHGAAVDDPG GQGCDGITPL
HDALNCGHFE VAELLIERGA SVTLRTRKGH NPLETLQQWV KLYGKDLDSE TQEKAAAMGR
LLQAASLGRA PHSSQAPQTL PSNHLFDPET SPPSSPCPGT PEVCEASTRV SQGLAVSTVA
RPRRSRHKVA SSSSSEGEDS AGPSQPTQKR PRHASPSLQT KAPMPGPASD REAATTSTSW
AAYREAIRGV GSAQTCRLGP SPLRGPSEIP IPQAALIPQE ECLAGDWLEE DFPMSPGHRG
RCPARPQSSG DGGRHRASGP GSDTARRPRA QARQSRLPYL ESWSTPVRAD RANSQATEPA
RSPDVPRVVA PTGENPTTGH LPGQVLPPPI RVRVRVQDNL FLIPVPHREA HSVAWLAEQA
AQRHYQASGL LPRLSLQKEG ALLAPQDPIP DVLQSNEEVL AEVTSWDLPP LRDRYRRACQ
TLEQGEHQQV LQAVEHQGSA PTFSACSLAL RQAQLTPLLR ALKLHSALRE LRLAGNRLGD
GCVAELLATL DTVPGLTLLD LSSNHLGPEG LRQLAAGLLG QTTLQNLEEL DLSMNPLGDG
CGQALASILR ACPVLCTLHL QACGFGPGFF LSHQVALGSA FQDTKCLKTL SLSYNGLGPT
ALGPVLGSLP AHSLLRLELS SVVTGKSDVG LTDPVVHYLS QEGCVLEHLS LSANHLGDKD
VRALSRCLPL CPSLVSLDLS ANPEVSSAGL EELLSTLQKR PQGLSFLGLS GCAVQGPLGL
DLWDKVVAQL QELQLCTRRL SAEDRNALHQ LLPSQLGPKV CTLDQGPKLF FRHL
