CTIP_XENTR
ID CTIP_XENTR Reviewed; 867 AA.
AC F6SNN2;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
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:Q6GNV6,
CC 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}. Note=Associates with sites
CC of DNA damage in S/G2 phase. {ECO:0000250}.
CC -!- DOMAIN: The damage-recruitment motif is required for DNA binding and
CC translocation to sites of DNA damage. {ECO:0000250}.
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; AAMC01030587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01030588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01030589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6SNN2; -.
DR SMR; F6SNN2; -.
DR STRING; 8364.ENSXETP00000062819; -.
DR PaxDb; F6SNN2; -.
DR eggNOG; ENOG502QTV5; Eukaryota.
DR HOGENOM; CLU_019262_0_0_1; -.
DR InParanoid; F6SNN2; -.
DR OMA; LGECHQN; -.
DR TreeFam; TF106469; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; Unplaced.
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; 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 3: Inferred from homology;
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..867
FT /note="DNA endonuclease RBBP8"
FT /id="PRO_0000417040"
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 141..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..531
FT /note="Damage-recruitment motif"
FT /evidence="ECO:0000250"
FT REGION 843..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..150
FT /evidence="ECO:0000255"
FT MOTIF 489..493
FT /note="PXDLS motif"
FT COMPBIAS 141..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 99332 MW; D4DA7DED8864FDF3 CRC64;
MNISASTCGS PSSSESLPAG DLFKELWSKL KECHDKELQE LLLKINKLKK QRCLDAQRLE
EFYTKNQHLR EQQKTLHDTI KVLEDRLRAG LCDRCTVTEE HMRKKQQEFE NIRQQNLKLI
TELMNDKNAL QDENKRLSEQ LHNMQKSRWK SDEENPADTG EGEDGVIPDS PLSTFSLSMV
SRMRRKKDNK HIRYSEKAPE DTLTLERKIT CIPSQGSAEK NASHSSHRRK GEDILVAETL
ELSPLPNGKS KRKKVYLCSK TSIAFASILL VLLHLFAEQL HSWMNNLSQV SKSLRWCLPL
KGNNKQGYIE YLFRFTEGSM EESQGNDDDG WNTKEASPVF GGPARNIRRS AEMDCISPPL
PVGLNSKLIS KCSRNPSDFL FNSVQAKAED GAQATRLCLG KETDSVISQC SSNGQGVLRC
SPNKSVPGGA QMGKDILDSE HHKQMANRYG KRKNAEAEQE ESCESSFDKE NNIPIKDIGS
ERHSMLDKPL DLSDRFSVLR PQDRSHGSSR GRTKQTFALV PEKPDPKKPL HIDLREDLYH
QTKQKKVFVS GLVERSAFNL HEDKEVTEEG NQLFDDLEIE TVHEPKRNAR SVHRGVQPTS
VLQPNLHMVQ ACPESQQGKP PIDNMQWSID PGADLSQYEM DMTMEDSKGG SPAKPELEDM
DYTYVSESFL LKMKKGDPGD SEDESKGQDS FEKMFDKSEY GEYVLCIKDR SPSQSCKERN
DLSSMVCKNI YTHSVRFDRV KKQKAFVEPY FQRPEQKKPA MDFPHIEVVR KKDERRKMLG
HTCKECELYY ADLPEEERAK KLASCSRHRF RYIPPSTPEN FWEVGFPSTQ TCQDRGYIKE
ELSPCQRPRR RQPYNAKFSS KIKEQKT
