CTIP_DANRE
ID CTIP_DANRE Reviewed; 651 AA.
AC F1R983; Q5EAZ7;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=DNA endonuclease RBBP8;
DE EC=3.1.-.-;
GN Name=rbbp8; ORFNames=zgc:113143;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN)
CC complex in DNA-end resection, the first step of double-strand break
CC (DSB) repair through the homologous recombination (HR) pathway.
CC Functions downstream of the MRN complex and ATM, promotes ATR
CC activation and its recruitment to DSBs in the S/G2 phase facilitating
CC the generation of ssDNA. {ECO:0000250|UniProtKB:Q99708}.
CC -!- SUBUNIT: Homodimer; dimerizes via the coiled coil domain. Interacts
CC with the MRN complex; the interaction links DNA sensing to resection
CC (By similarity). Interacts with samhd1 (By similarity).
CC {ECO:0000250|UniProtKB:Q6GNV6, ECO:0000250|UniProtKB:Q99708}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99708}.
CC Note=Associates with sites of DNA damage in S/G2 phase.
CC {ECO:0000250|UniProtKB:Q99708}.
CC -!- SIMILARITY: Belongs to the COM1/SAE2/CtIP family. {ECO:0000305}.
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DR EMBL; CU634022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FP089511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC090186; AAH90186.1; -; mRNA.
DR RefSeq; NP_001012518.1; NM_001012500.1.
DR RefSeq; XP_005174246.1; XM_005174189.3.
DR AlphaFoldDB; F1R983; -.
DR SMR; F1R983; -.
DR STRING; 7955.ENSDARP00000063831; -.
DR PaxDb; F1R983; -.
DR Ensembl; ENSDART00000063832; ENSDARP00000063831; ENSDARG00000043480.
DR GeneID; 503536; -.
DR KEGG; dre:503536; -.
DR CTD; 5932; -.
DR ZFIN; ZDB-GENE-050220-14; rbbp8.
DR eggNOG; ENOG502QTV5; Eukaryota.
DR GeneTree; ENSGT00530000063835; -.
DR HOGENOM; CLU_019262_0_0_1; -.
DR InParanoid; F1R983; -.
DR OMA; LGECHQN; -.
DR OrthoDB; 962036at2759; -.
DR TreeFam; TF106469; -.
DR Reactome; R-DRE-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-DRE-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-DRE-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-DRE-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-DRE-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-DRE-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DRE-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-DRE-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DRE-69473; G2/M DNA damage checkpoint.
DR PRO; PR:F1R983; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000043480; Expressed in mature ovarian follicle and 26 other tissues.
DR ExpressionAtlas; F1R983; baseline.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0000406; F:double-strand/single-strand DNA junction binding; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0070336; F:flap-structured DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000403; F:Y-form DNA binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR019518; CtIP_N.
DR InterPro; IPR013882; Ctp1_C.
DR InterPro; IPR033316; RBBP8-like.
DR PANTHER; PTHR15107; PTHR15107; 1.
DR Pfam; PF10482; CtIP_N; 1.
DR Pfam; PF08573; SAE2; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; DNA damage; DNA repair;
KW DNA-binding; Endonuclease; Hydrolase; Meiosis; Mitosis; Nuclease; Nucleus;
KW Reference proteome.
FT CHAIN 1..651
FT /note="DNA endonuclease RBBP8"
FT /id="PRO_0000417038"
FT REGION 138..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 18..145
FT /evidence="ECO:0000255"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 91
FT /note="R -> C (in Ref. 2; AAH90186)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> T (in Ref. 2; AAH90186)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="V -> F (in Ref. 2; AAH90186)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="E -> V (in Ref. 2; AAH90186)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="E -> V (in Ref. 2; AAH90186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 651 AA; 74390 MW; DBCCC440B8906327 CRC64;
MSITPADLSP ASSSDHREKL QELLTAVRDL HDTALQELQA KIAKLKKERC LDAQKLSEFH
SKNQHLREQQ KIQQEKIRQL EDRLRSGPCD RCTVKEKQIK KTNTELEDNN QRNLSVISEL
EAERKTLTDE NRRLSLELER LRRSGSPQNT SSEAEEGMIP DSPLRPLSLP VASKMKRRKE
QNHVRYTETP LSLSHPESRQ REQSVAFGCN GKGVLVAETC EMDATSVAER DNKRHFRIVV
PETCRPDVYP EQVDDVDDDD LHIPSHTEQN QKPELRDCTN ILIAGQNDDS PLILRCRPLA
SQDHQSSIDD VLRTPANSST CVLTKGKRKH SNGAKKDREI SDCRLDADET DIKGIIFAST
PANGRLQSKN QETSEIETTQ DSKKKCLDGH TPRKSLVQNH HAPFPYDQSW SVDPGADLGQ
YDTESSPQPE HQARTDLETL DTDCTFVSHS LLLRGQKTTG QSQTTGIGQK ANDSLADIFD
KTGYGEYESC PQDDSIDLKQ DSVYEEEREE DDPEEKPEAA VVFRRPADRK PLVSDSDKSS
RNKSFACVEV VRKKDERRKL KGHYCKECEV YYADLPEEER EKKLTSCSRH RYRYIPPSTP
ENFWEVGFPS TQTCVERGYI KEDEQPDVRI RRRRPYLAMF SPKAKSQKKK H
