DCR1B_RAT
ID DCR1B_RAT Reviewed; 541 AA.
AC Q4KLY6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=5' exonuclease Apollo;
DE EC=3.1.-.-;
DE AltName: Full=Beta-lactamase MBLAC2;
DE EC=3.5.2.6 {ECO:0000250|UniProtKB:Q9H816};
DE AltName: Full=DNA cross-link repair 1B protein;
DE AltName: Full=SNM1 homolog B;
GN Name=Dclre1b; Synonyms=Snm1b;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: 5'-3' exonuclease that plays a central role in telomere
CC maintenance and protection during S-phase. Participates in the
CC protection of telomeres against non-homologous end-joining (NHEJ)-
CC mediated repair, thereby ensuring that telomeres do not fuse. Plays a
CC key role in telomeric loop (T loop) formation by being recruited by
CC TERF2 at the leading end telomeres and by processing leading-end
CC telomeres immediately after their replication via its exonuclease
CC activity: generates 3' single-stranded overhang at the leading end
CC telomeres avoiding blunt leading-end telomeres that are vulnerable to
CC end-joining reactions and expose the telomere end in a manner that
CC activates the DNA repair pathways. Together with TERF2, required to
CC protect telomeres from replicative damage during replication by
CC controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B)
CC needed for telomere replication during fork passage and prevent
CC aberrant telomere topology. Also involved in response to DNA damage:
CC plays a role in response to DNA interstrand cross-links (ICLs) by
CC facilitating double-strand break formation. In case of spindle stress,
CC involved in prophase checkpoint (By similarity). Possesses beta-
CC lactamase activity, catalyzing the hydrolysis of penicillin G and
CC nitrocefin (By similarity). Exhibits no activity towards other beta-
CC lactam antibiotic classes including cephalosporins (cefotaxime) and
CC carbapenems (imipenem) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000250|UniProtKB:Q9H816};
CC -!- SUBUNIT: Interacts with TERF2; the interaction is direct. Interacts
CC with MUS81, MRE11 and FANCD2. Interacts with HSPA2, HSPA8 and HSPA14.
CC Interacts with SPAG5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Note=Mainly localizes to telomeres, recruited
CC via its interaction with TERF2. During mitosis, localizes to the
CC centrosome (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The TBM domain mediates interaction with TERF2. {ECO:0000250}.
CC -!- PTM: Ubiquitinated, leading to its degradation. Interaction with TERF2
CC protects it from ubiquitination (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH98939.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC098939; AAH98939.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001020858.1; NM_001025687.1.
DR AlphaFoldDB; Q4KLY6; -.
DR SMR; Q4KLY6; -.
DR STRING; 10116.ENSRNOP00000026213; -.
DR PhosphoSitePlus; Q4KLY6; -.
DR PaxDb; Q4KLY6; -.
DR GeneID; 310745; -.
DR KEGG; rno:310745; -.
DR UCSC; RGD:1310343; rat.
DR CTD; 64858; -.
DR RGD; 1310343; Dclre1b.
DR eggNOG; KOG1361; Eukaryota.
DR InParanoid; Q4KLY6; -.
DR PhylomeDB; Q4KLY6; -.
DR Reactome; R-RNO-6783310; Fanconi Anemia Pathway.
DR PRO; PR:Q4KLY6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0008800; F:beta-lactamase activity; ISS:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; ISO:RGD.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; ISS:UniProtKB.
DR GO; GO:0016233; P:telomere capping; ISO:RGD.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; ISO:RGD.
DR GO; GO:0031860; P:telomeric 3' overhang formation; ISS:UniProtKB.
DR GO; GO:0031627; P:telomeric loop formation; ISS:UniProtKB.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Exonuclease;
KW Hydrolase; Isopeptide bond; Nuclease; Nucleus; Reference proteome;
KW Telomere; Ubl conjugation.
FT CHAIN 1..541
FT /note="5' exonuclease Apollo"
FT /id="PRO_0000398626"
FT REGION 350..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 492..507
FT /note="TBM"
FT COMPBIAS 459..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H816"
SQ SEQUENCE 541 AA; 60924 MW; C194022A218F9D2C CRC64;
MNGVVIPQTP IAVDFWSLRR AGTARLFFLS HMHCDHTVGL SSTWARPLYC SPITAHLLHR
RLQVSKQWIR ALEIGESHVL LLDEIGQETM TVTLIDANHC PGSVMFLFEG YFGTILYTGD
FRYTPSMLKE PALTLGKQIH TLYLDNTNCN PALVLPSRQE ATQQIIQLIR QFPQHNIKIG
LYSLGKESLL EQLALEFQTW VVLSPQRLEL VQLLGLADVF TVEEEAGRIH AVDHMEICHS
AMLQWNQTHP TIAIFPTSRK IRSPHPSIYS IPYSDHSSYS ELRAFVAALR PCQVVPIVRE
QPCGEFFQDS LSPRLSMPLI PHSVQQYMSS SSRKTNVFWQ LERRLKRPRT QGVVFESPEE
KADQVKVDRD SKKHKKESLS PWAGCLSRLC PHPLQARKQL FPDFCRKEGD EPVLFCDSNK
MATVLTAPLE LSVQLQPVDE FPFPETREEI GLGSPLWSGG GSGSPTRGKQ SNGMGCGSPP
THISRTTHLT PESGGLALKY LLTPVDFLQA GFSSRNFDQQ VEKHQRVQCN NPAVMNTVDD
V
