NHEJ1_RAT
ID NHEJ1_RAT Reviewed; 304 AA.
AC Q6AYI4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Non-homologous end-joining factor 1 {ECO:0000305};
DE AltName: Full=Protein cernunnos {ECO:0000250|UniProtKB:Q9H9Q4};
DE AltName: Full=XRCC4-like factor {ECO:0000250|UniProtKB:Q9H9Q4};
GN Name=Nhej1 {ECO:0000312|RGD:1359338};
GN Synonyms=Xlf {ECO:0000250|UniProtKB:Q9H9Q4};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: DNA repair protein involved in DNA non-homologous end joining
CC (NHEJ); required for double-strand break (DSB) repair and V(D)J
CC recombination. Plays a key role in NHEJ by promoting the ligation of
CC various mismatched and non-cohesive ends. Together with PAXX,
CC collaborates with DNA polymerase lambda (POLL) to promote joining of
CC non-cohesive DNA ends. May act in concert with XRCC5-XRCC6 (Ku) to
CC stimulate XRCC4-mediated joining of blunt ends and several types of
CC mismatched ends that are non-complementary or partially complementary.
CC Associates with XRCC4 to form alternating helical filaments that bridge
CC DNA and act like a bandage, holding together the broken DNA until it is
CC repaired. The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of
CC a DSB in a highly diffusive manner and robustly bridges two independent
CC DNA molecules, holding the broken DNA fragments in close proximity to
CC one other. The mobility of the bridges ensures that the ends remain
CC accessible for further processing by other repair factors. Binds DNA in
CC a length-dependent manner. {ECO:0000250|UniProtKB:Q9H9Q4}.
CC -!- SUBUNIT: Homodimer; mainly exists as a homodimer when not associated
CC with XRCC4. Interacts with XRCC4; the interaction is direct and is
CC mediated via a head-to-head interaction between N-terminal head
CC regions. Component of the core long-range non-homologous end joining
CC (NHEJ) complex (also named DNA-PK complex) composed of PRKDC, LIG4,
CC XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF. Additional component of
CC the NHEJ complex includes PAXX. Following autophosphorylation, PRKDC
CC dissociates from DNA, leading to formation of the short-range NHEJ
CC complex, composed of LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF.
CC Interacts with POLL (DNA polymerase lambda); promoting POLL recruitment
CC to double-strand breaks (DSBs) and stimulation of the end-filling
CC activity of POLL. {ECO:0000250|UniProtKB:Q9H9Q4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H9Q4}.
CC Chromosome {ECO:0000250|UniProtKB:Q9H9Q4}. Note=Localizes to site of
CC double-strand breaks; recruitment is dependent on XRCC5-XRCC6 (Ku)
CC heterodimer. {ECO:0000250|UniProtKB:Q9H9Q4}.
CC -!- DOMAIN: The coiled-coil region mediates homodimerization.
CC {ECO:0000250|UniProtKB:Q9H9Q4}.
CC -!- DOMAIN: The Leu-lock (Leu-120) site inserts into a hydrophobic pocket
CC in XRCC4. {ECO:0000250|UniProtKB:Q9H9Q4}.
CC -!- PTM: Phosphorylated by PRKDC at the C-terminus in response to DNA
CC damage. Phosphorylation by PRKDC at the C-terminus of XRCC4 and
CC NHEJ1/XLF are highly redundant and regulate ability of the XRCC4-
CC NHEJ1/XLF subcomplex to bridge DNA. Phosphorylation does not prevent
CC interaction with XRCC4 but disrupts ability to bridge DNA and promotes
CC detachment from DNA. {ECO:0000250|UniProtKB:Q9H9Q4}.
CC -!- SIMILARITY: Belongs to the XRCC4-XLF family. XLF subfamily.
CC {ECO:0000305}.
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DR EMBL; BC079033; AAH79033.1; -; mRNA.
DR RefSeq; NP_001014239.1; NM_001014217.1.
DR RefSeq; XP_006245302.1; XM_006245240.1.
DR RefSeq; XP_006245303.1; XM_006245241.3.
DR RefSeq; XP_006245304.1; XM_006245242.3.
DR AlphaFoldDB; Q6AYI4; -.
DR SMR; Q6AYI4; -.
DR STRING; 10116.ENSRNOP00000024444; -.
DR iPTMnet; Q6AYI4; -.
DR PhosphoSitePlus; Q6AYI4; -.
DR PaxDb; Q6AYI4; -.
DR GeneID; 363251; -.
DR KEGG; rno:363251; -.
DR UCSC; RGD:1359338; rat.
DR CTD; 79840; -.
DR RGD; 1359338; Nhej1.
DR VEuPathDB; HostDB:ENSRNOG00000018162; -.
DR eggNOG; ENOG502S0R3; Eukaryota.
DR HOGENOM; CLU_076115_1_0_1; -.
DR InParanoid; Q6AYI4; -.
DR OMA; CNLMCPL; -.
DR OrthoDB; 1397591at2759; -.
DR PhylomeDB; Q6AYI4; -.
DR TreeFam; TF328567; -.
DR Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
DR PRO; PR:Q6AYI4; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000018162; Expressed in testis and 19 other tissues.
DR Genevisible; Q6AYI4; RN.
DR GO; GO:0032807; C:DNA ligase IV complex; IBA:GO_Central.
DR GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0045027; F:DNA end binding; ISS:UniProtKB.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:RGD.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:0051103; P:DNA ligation involved in DNA repair; ISO:RGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0033152; P:immunoglobulin V(D)J recombination; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR Gene3D; 2.170.210.10; -; 1.
DR InterPro; IPR015381; XLF_N.
DR InterPro; IPR038051; XRCC4-like_N_sf.
DR Pfam; PF09302; XLF; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Coiled coil; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..304
FT /note="Non-homologous end-joining factor 1"
FT /id="PRO_0000228656"
FT REGION 1..140
FT /note="Globular head"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Q4"
FT REGION 233..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 133..175
FT /evidence="ECO:0000250|UniProtKB:Q9H9Q4"
FT MOTIF 294..304
FT /note="XLM"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Q4"
FT COMPBIAS 233..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 120
FT /note="Leu-lock"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Q4"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Q4"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3KNJ2"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Q4"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Q4"
SQ SEQUENCE 304 AA; 33885 MW; DDB56676EB94B4DD CRC64;
MEELEQGLLM QPWAWLQLAE NSLLAKASIT KHGYALLISD LQQVWHEQVD TLEVSQRAKE
LNKRLTAPPA AFLHHLDEVL RPLFKDSAHQ DAAHPSKATF SCDRGEEVLI LRVRSELSGL
PFNWHFHCLP ASSLLVSQHL ICPLMGVSLA LHSHVRELAA LLRMKDLEIQ AYQESGAVLS
RGRLKTEPFE ENSFLEQFMV EKLPEACAVG DGRPFAMNLQ SLYVAVTKQQ VQARQKHKGS
GEPQTSSSTS PQGTDSQLQN QPEQQISPTP TLSEPECEPM AASGPVHRAQ LVKAKRKKPR
GLFS
