XRCC6_CHICK
ID XRCC6_CHICK Reviewed; 632 AA.
AC O93257;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=X-ray repair cross-complementing protein 5;
DE EC=3.6.4.-;
DE EC=4.2.99.-;
DE AltName: Full=5'-deoxyribose-5-phosphate lyase Ku70;
DE Short=5'-dRP/AP lyase Ku70;
DE AltName: Full=ATP-dependent DNA helicase 2 subunit 1;
DE AltName: Full=ATP-dependent DNA helicase II 70 kDa subunit;
DE AltName: Full=DNA repair protein XRCC6;
DE AltName: Full=Ku autoantigen protein p70 homolog;
DE Short=Ku70;
GN Name=XRCC6; Synonyms=G22P1, KU70;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Intestinal mucosa;
RX PubMed=9736627; DOI=10.1093/emboj/17.18.5497;
RA Takata M., Sasaki M.S., Sonoda E., Morrison C., Hashimoto M., Utsumi H.,
RA Yamaguchi-Iwai Y., Shinohara A., Takeda S.;
RT "Homologous recombination and non-homologous end-joining pathways of DNA
RT double-strand break repair have overlapping roles in the maintenance of
RT chromosomal integrity in vertebrate cells.";
RL EMBO J. 17:5497-5508(1998).
CC -!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase that
CC plays a key role in DNA non-homologous end joining (NHEJ) by recruiting
CC DNA-PK to DNA. Required for double-strand break repair and V(D)J
CC recombination. Also has a role in chromosome translocation. Has a role
CC in chromosome translocation. The DNA helicase II complex binds
CC preferentially to fork-like ends of double-stranded DNA in a cell
CC cycle-dependent manner. It works in the 3'-5' direction. During NHEJ,
CC the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and
CC binds to the broken ends of the DNA and protects them from further
CC resection. Binding to DNA may be mediated by XRCC6. The XRCC5-XRRC6
CC dimer acts as regulatory subunit of the DNA-dependent protein kinase
CC complex DNA-PK by increasing the affinity of the catalytic subunit
CC PRKDC to DNA by 100-fold. The XRCC5-XRRC6 dimer is probably involved in
CC stabilizing broken DNA ends and bringing them together. The assembly of
CC the DNA-PK complex to DNA ends is required for the NHEJ ligation step.
CC Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP
CC lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-
CC phosphate at an abasic site near double-strand breaks. 5'-dRP lyase
CC activity allows to 'clean' the termini of abasic sites, a class of
CC nucleotide damage commonly associated with strand breaks, before such
CC broken ends can be joined. The XRCC5-XRRC6 dimer together with APEX1
CC acts as a negative regulator of transcription (By similarity).
CC {ECO:0000250|UniProtKB:P12956}.
CC -!- SUBUNIT: Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70. Component
CC of the core long-range non-homologous end joining (NHEJ) complex (also
CC named DNA-PK complex) composed of PRKDC, LIG4, XRCC4, XRCC6/Ku70,
CC XRCC5/Ku86 and NHEJ1/XLF. Additional component of the NHEJ complex
CC includes PAXX. Following autophosphorylation, PRKDC dissociates from
CC DNA, leading to formation of the short-range NHEJ complex, composed of
CC LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF.
CC {ECO:0000250|UniProtKB:P12956}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12956}.
CC Chromosome {ECO:0000250|UniProtKB:P12956}.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000250|UniProtKB:P12956}.
CC -!- SIMILARITY: Belongs to the ku70 family. {ECO:0000305}.
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DR EMBL; AB016529; BAA32018.1; -; mRNA.
DR RefSeq; NP_990258.2; NM_204927.2.
DR AlphaFoldDB; O93257; -.
DR SMR; O93257; -.
DR BioGRID; 676041; 2.
DR STRING; 9031.ENSGALP00000037185; -.
DR PaxDb; O93257; -.
DR GeneID; 395767; -.
DR KEGG; gga:395767; -.
DR CTD; 2547; -.
DR VEuPathDB; HostDB:geneid_395767; -.
DR eggNOG; KOG2327; Eukaryota.
DR InParanoid; O93257; -.
DR OrthoDB; 402798at2759; -.
DR PhylomeDB; O93257; -.
DR Reactome; R-GGA-353423; Non-homologous end joining (NHEJ).
DR PRO; PR:O93257; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043564; C:Ku70:Ku80 complex; ISS:UniProtKB.
DR GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
DR GO; GO:0071481; P:cellular response to X-ray; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR Gene3D; 4.10.970.10; -; 1.
DR InterPro; IPR006165; Ku70.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR027388; Ku70_bridge/pillars_dom_sf.
DR InterPro; IPR005160; Ku_C.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03730; Ku_C; 1.
DR Pfam; PF03731; Ku_N; 1.
DR Pfam; PF02037; SAP; 1.
DR PIRSF; PIRSF003033; Ku70; 1.
DR SMART; SM00559; Ku78; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR TIGRFAMs; TIGR00578; ku70; 1.
DR PROSITE; PS50800; SAP; 1.
PE 2: Evidence at transcript level;
KW Activator; ATP-binding; Chromosome; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Lyase;
KW Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..632
FT /note="X-ray repair cross-complementing protein 5"
FT /id="PRO_0000210181"
FT DOMAIN 283..490
FT /note="Ku"
FT DOMAIN 595..629
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 555..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 52
FT /note="Schiff-base intermediate with DNA; for 5'-
FT deoxyribose-5-phosphate lyase activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 632 AA; 72289 MW; 5EB391674459B1C0 CRC64;
MEMWVLGEVG MAVLSAAAMA DWVSYYRGDG PDEEEDGEQQ EEEGPEAVAD YRFSGRDSLI
FLVDASKAMF EPYENEEAAT PFDMTMQCIR NVYTSKIISS DKDLLSVVFY GMENNKNSAD
FKHIYVLQEL DNPGAKRILE LDQYRGDEGR VLFRETFGHN ADYSLGEALW ACSNLFSDVR
VRLSHKRIML FTNEDNPHAN DSAKAKLART RAGDLRDTGI ILDLMHLKKP GGFDISLFYR
DIINVAEDED LGIQPDESGK LEHLMKKVRA KETRKRALSR LNLYLNKDLS FSVGVYNLIQ
KAYKPYPVKL YRETNEPVKT KTRVFNGKTG SLLLPSDTKR AQTYGNRQIA MEKEETEEVK
RFDSPGLFLI GFKPLSMLKQ HHHIRPSQFM YPEESLVTGS TTLFNALLMK CLEKEVMALC
RYIARRNTPP RIVALIPQEE EVDEQKVQIA PPGFHIIFLP YADDKRNVDF TEKVPANREQ
VDKMKGIIQK LRFKYRTDSF ENPVLQQHFR NLEALALDML EPEQAEDLTM PKTEEMSRRL
GNLVEEFKQL VYPPDYSPEG KAAKRKQAGD AQAEKRPKIE ISEDSLRSYV QNGTLGKLTV
SALKDTCRHY GLRSGGKKQE LIDALTEYFS GR
