ID H2S0A6_TAKRU Unreviewed; 827 AA.
AC H2S0A6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Nibrin {ECO:0000256|ARBA:ARBA00020013, ECO:0000256|PIRNR:PIRNR011869};
GN Name=nbn {ECO:0000313|Ensembl:ENSTRUP00000005827.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000005827.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000005827.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000005827.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the MRE11-RAD50-NBN (MRN complex) which plays a
CC critical role in the cellular response to DNA damage and the
CC maintenance of chromosome integrity. The complex is involved in double-
CC strand break (DSB) repair, DNA recombination, maintenance of telomere
CC integrity, cell cycle checkpoint control and meiosis.
CC {ECO:0000256|PIRNR:PIRNR011869}.
CC -!- SUBUNIT: Component of the MRN complex. {ECO:0000256|PIRNR:PIRNR011869}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR011869}.
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DR AlphaFoldDB; H2S0A6; -.
DR STRING; 31033.ENSTRUP00000087062; -.
DR Ensembl; ENSTRUT00000005863.3; ENSTRUP00000005827.3; ENSTRUG00000002513.3.
DR eggNOG; ENOG502QQ7Y; Eukaryota.
DR GeneTree; ENSGT00390000000521; -.
DR OrthoDB; 2787263at2759; -.
DR TreeFam; TF101103; -.
DR Proteomes; UP000005226; Chromosome 7.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd17741; BRCT_nibrin; 1.
DR CDD; cd22667; FHA_NBN; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.10980; Nibrin, BRCT2 domain; 1.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR040227; Nibrin-rel.
DR InterPro; IPR032429; Nibrin_BRCT2.
DR InterPro; IPR043014; Nibrin_BRCT2_sf.
DR InterPro; IPR013908; Nibrin_C.
DR InterPro; IPR016592; Nibrin_met.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR12162:SF0; NIBRIN; 1.
DR PANTHER; PTHR12162; NIBRIN-RELATED; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF08599; Nbs1_C; 1.
DR Pfam; PF16508; NIBRIN_BRCT_II; 1.
DR PIRSF; PIRSF011869; Nibrin_animal; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM01348; Nbs1_C; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|PIRNR:PIRNR011869};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|PIRNR:PIRNR011869};
KW DNA repair {ECO:0000256|PIRNR:PIRNR011869};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254, ECO:0000256|PIRNR:PIRNR011869};
KW Nucleus {ECO:0000256|PIRNR:PIRNR011869};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|PIRNR:PIRNR011869}.
FT DOMAIN 22..70
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 358..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..573
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 91246 MW; 4A045970C40FF0B3 CRC64;
MWVLAPLQPG GQTHYLHPGK DYVVGRKNCD ILLTSDQSIS RAHAQLVPSA QALILKDSSK
YGTFINSQRM TENTAVNLNP GDSVTFGVFE SKFIVEHVQP VVCSSCLDNN GKTLLSQSLA
ALGGDLVNSW SLECTHLVMT SVKVTVKTIS ALLCCRPIVK PEFFSELSRC VQQKLPPPKA
ERFIPEIDEP SLIKEDVNVG VIPGRRQLFN GKTFLFLTAK QLKRLSAAVS FGGGRSQLLE
EGSLPRHLLE SPQSCVIDVT TGSSQALLPP STTEWAKSVR NIVHRKGLRV ITESEIGLAA
IYASCGQHCN PSQLAANSEP VLKVHPRIVS ASLSQSAAVD ETVLLAASQN ITAYAVNTET
SQGTQQSKVW EGTVVGETPE KRENRSTCRP HASNTAVQKT TAHLIADNKR PFTAEQADRH
SKQPESSVAG PGSSTSRVQP SLPVTNGGSK RFLGTPSPQK PKASAQVSPQ KQSTLTSFFQ
PVSKKRPLLD EPFMSEPKRA TLDSSISFQA QDASDSRKPP LDSAADLFPE QSAGQRDRIS
LSVQEEPNKR KREKQEEENI EMDELESIMS VDMDFDDELP AVKSQEAQPL TQSSHEKTCG
VDTEGASSAS KRQRLYCEGD GTDRRRQHDV KNENKSETPE RHRSSLKTKE SPPLEHSSTH
QESSKRPQSS SSTTHTNTKA SEDIEDLELL IADDWQPKEE TKRPVKAVAI KQEVQEAPID
QDLPKKLVVV EFRTLTLTEA PEVKPLRMPD TSCEKNFKCF RKHFGPGARG SPHIISGSDL
LVHNRGKNSD LDEWLKDVVE EERQSRRDEN VGDDLFRYNP AKMSRRR
//
