ID   CTIP_XENLA              Reviewed;         856 AA.
AC   Q6GNV6;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=DNA endonuclease RBBP8;
DE            EC=3.1.-.-;
DE   AltName: Full=CtBP-interacting protein;
DE            Short=CtIP;
GN   Name=rbbp8; Synonyms=ctip;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION,
RP   AND MUTAGENESIS OF ARG-496 AND LYS-498.
RX   PubMed=20064462; DOI=10.1016/j.molcel.2009.12.002;
RA   You Z., Shi L.Z., Zhu Q., Wu P., Zhang Y.W., Basilio A., Tonnu N.,
RA   Verma I.M., Berns M.W., Hunter T.;
RT   "CtIP links DNA double-strand break sensing to resection.";
RL   Mol. Cell 36:954-969(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH SAMHD1.
RX   PubMed=29670289; DOI=10.1038/s41586-018-0050-1;
RA   Coquel F., Silva M.J., Techer H., Zadorozhny K., Sharma S.,
RA   Nieminuszczy J., Mettling C., Dardillac E., Barthe A., Schmitz A.L.,
RA   Promonet A., Cribier A., Sarrazin A., Niedzwiedz W., Lopez B., Costanzo V.,
RA   Krejci L., Chabes A., Benkirane M., Lin Y.L., Pasero P.;
RT   "SAMHD1 acts at stalled replication forks to prevent interferon
RT   induction.";
RL   Nature 557:57-61(2018).
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       ECO:0000269|PubMed:20064462}.
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 (PubMed:29670289).
CC       {ECO:0000250|UniProtKB:Q99708, ECO:0000269|PubMed:29670289}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20064462}.
CC       Note=Associates with sites of DNA damage in S/G2 phase. Binds
CC       chromatin. {ECO:0000250|UniProtKB:Q99708}.
CC   -!- DOMAIN: The damage-recruitment motif is required for DNA binding and
CC       translocation to sites of DNA damage.
CC   -!- DOMAIN: The PXDLS motif binds to a cleft in CtBP proteins.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the COM1/SAE2/CtIP family. {ECO:0000305}.
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DR   EMBL; BC073395; AAH73395.1; -; mRNA.
DR   EMBL; GU207840; ACZ97554.1; -; mRNA.
DR   RefSeq; NP_001085825.1; NM_001092356.1.
DR   AlphaFoldDB; Q6GNV6; -.
DR   SMR; Q6GNV6; -.
DR   MaxQB; Q6GNV6; -.
DR   DNASU; 444252; -.
DR   GeneID; 444252; -.
DR   KEGG; xla:444252; -.
DR   CTD; 444252; -.
DR   Xenbase; XB-GENE-5953161; rbbp8.L.
DR   OrthoDB; 962036at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 444252; Expressed in egg cell and 18 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019518; CtIP_N.
DR   InterPro; IPR013882; Ctp1_C.
DR   InterPro; IPR033594; RBBP8.
DR   InterPro; IPR033316; RBBP8-like.
DR   PANTHER; PTHR15107; PTHR15107; 1.
DR   PANTHER; PTHR15107:SF4; PTHR15107:SF4; 1.
DR   Pfam; PF10482; CtIP_N; 1.
DR   Pfam; PF08573; SAE2; 1.
PE   1: Evidence at protein 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..856
FT                   /note="DNA endonuclease RBBP8"
FT                   /id="PRO_0000417039"
FT   REGION          25..48
FT                   /note="Essential for binding to the MRN complex and for RPA
FT                   focus formation on DNA damage"
FT                   /evidence="ECO:0000250"
FT   REGION          143..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..478
FT                   /note="PXDLS motif"
FT   REGION          493..515
FT                   /note="Damage-recruitment motif"
FT                   /evidence="ECO:0000250"
FT   REGION          695..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          31..153
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        143..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..730
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         496
FT                   /note="R->A: Abolishes chromatin binding. Abolishes DNA-
FT                   binding activity in vitro."
FT                   /evidence="ECO:0000269|PubMed:20064462"
FT   MUTAGEN         498
FT                   /note="K->A: Abolishes chromatin binding. Abolishes DNA-
FT                   binding activity in vitro."
FT                   /evidence="ECO:0000269|PubMed:20064462"
SQ   SEQUENCE   856 AA;  98292 MW;  BDC955F018E86BBE CRC64;
     MSITASTCGS PSSSESLPNG DLFKELWSKL KECHDKDLQE LLMKIGKLKK ERCLDAQRLE
     EFYTKNQHLR EQQKTLHDTI KVLEDRLRAG LCDRCTVTEE HMRKKQQEFE NIRQQNLKLI
     TELMNDKNAL QDENKRLSEQ LHDMQKNRHR RKSDEENPAD TGDGEDGVIP DSPLSTFSLS
     MVSRMRRKKE NKHVRYTEQT QEDALTFDRK ISSGTRPQIS TQVNMRKGED VLVAETLELA
     PLPNKYEVCT EKPVFNLATV VAETLGLDAM EESQSQSVFN QPGITCAPLF HKSEDSSPRQ
     VKVEFTEGSM EGFQTNDDDT EWNRREASPV FGEPVRNIRR GTDMDCSSPP LPVGLSSKLK
     SHCSRNAPDF SVHAKAEDGA LLTRLSHCIE TDSVISQCSS NRQDVLRPSP NKSDAQMGKY
     IFDSEQHKQT GNRYGKRKNA EAEQEESCES SFDKENNIPL KDISGARHSM LDKPLDLSDR
     FSVLRPQDRS HESSSRTKLT ISLVPEKPDT KTILHIDLKE NLHQQTRQKK VFVSGLVEHS
     AFNLHEDNEV TEEDNKPFHD SETEIMCHVP KRKPRAVHRG VQPTSVLQPN LHMVHACLES
     QGRPPIDNMQ WSIDPGADLS QYEMDMTMED SKSGSPAKPE LEDMDYTYVN ESCLLKLKMG
     DPDDSEAESK DQDSFGEMFD KTEYGEYASY IKDKSPSQSI SCKERSDIPS IENKKITSEK
     EHESKGEPYQ KQKAFVEPYF QRPERKKPAI DFPHIEVVRN KEERRKMLGH TCKECELYYA
     DLPEEERAKK LASCSRHRFR YIPPSTPENF WEVGFPSTQT CKDRGYIKEE LSPCQRPRRR
     QPYNAIFTSK IKEQKT