ID   DCR1B_MOUSE             Reviewed;         541 AA.
AC   Q8C7W7; A0JLW2; B0V3N9; B0V3P0; Q3U4P2; Q3UUC7; Q3UV92; Q6NXL4; Q8BN95;
AC   Q8BQS8; Q921S0;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 142.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Adipose tissue, Bone, Eye, Spinal cord, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 82-541 (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Brain, and Mammary gland;
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   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   ASP-14.
RX   PubMed=20551906; DOI=10.1038/emboj.2010.58;
RA   Lam Y.C., Akhter S., Gu P., Ye J., Poulet A., Giraud-Panis M.J.,
RA   Bailey S.M., Gilson E., Legerski R.J., Chang S.;
RT   "SNMIB/Apollo protects leading-strand telomeres against NHEJ-mediated
RT   repair.";
RL   EMBO J. 29:2230-2241(2010).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF 31-HIS--ASP-35; HIS-230 AND 500-TYR--PRO-504.
RX   PubMed=20619712; DOI=10.1016/j.molcel.2010.06.031;
RA   Wu P., van Overbeek M., Rooney S., de Lange T.;
RT   "Apollo contributes to G overhang maintenance and protects leading-end
RT   telomeres.";
RL   Mol. Cell 39:606-617(2010).
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. Possesses beta-lactamase activity,
CC       catalyzing the hydrolysis of penicillin G and nitrocefin (By
CC       similarity). Exhibits no activity towards other beta-lactam antibiotic
CC       classes including cephalosporins (cefotaxime) and carbapenems
CC       (imipenem) (By similarity). {ECO:0000250|UniProtKB:Q9H816,
CC       ECO:0000269|PubMed:20551906, ECO:0000269|PubMed:20619712}.
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 MUS81, MRE11 and FANCD2. Interacts with HSPA2,
CC       HSPA8 and HSPA14. Interacts with SPAG5 (By similarity). Interacts with
CC       TERF2; the interaction is direct. {ECO:0000250,
CC       ECO:0000269|PubMed:20619712}.
CC   -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC       {ECO:0000269|PubMed:20551906, ECO:0000269|PubMed:20619712}. 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.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C7W7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C7W7-2; Sequence=VSP_015174;
CC       Name=3;
CC         IsoId=Q8C7W7-3; Sequence=VSP_015175, VSP_015176;
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   -!- DISRUPTION PHENOTYPE: Embryos are smaller than wild-type embryos and
CC       neonates die during the first day after birth. Cells activate the ATM
CC       kinase at their telomeres in S phase and show leading-end telomere
CC       fusions which are accompanied by a reduction in the telomeric overhang
CC       signal. {ECO:0000269|PubMed:20551906, ECO:0000269|PubMed:20619712}.
CC   -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH11094.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC39165.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAE23379.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK046571; BAC32791.1; -; mRNA.
DR   EMBL; AK049115; BAC33550.1; -; mRNA.
DR   EMBL; AK084347; BAC39165.1; ALT_FRAME; mRNA.
DR   EMBL; AK134324; BAE22098.1; -; mRNA.
DR   EMBL; AK137495; BAE23379.1; ALT_INIT; mRNA.
DR   EMBL; AK138568; BAE23700.1; -; mRNA.
DR   EMBL; AK154124; BAE32389.1; -; mRNA.
DR   EMBL; CU210953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011094; AAH11094.1; ALT_INIT; mRNA.
DR   EMBL; BC067017; AAH67017.1; -; mRNA.
DR   EMBL; BC125277; AAI25278.1; -; mRNA.
DR   CCDS; CCDS17694.1; -. [Q8C7W7-1]
DR   CCDS; CCDS17695.1; -. [Q8C7W7-2]
DR   RefSeq; NP_001020483.1; NM_001025312.1. [Q8C7W7-2]
DR   RefSeq; NP_598626.2; NM_133865.2. [Q8C7W7-1]
DR   AlphaFoldDB; Q8C7W7; -.
DR   SMR; Q8C7W7; -.
DR   BioGRID; 228331; 10.
DR   IntAct; Q8C7W7; 8.
DR   STRING; 10090.ENSMUSP00000029435; -.
DR   iPTMnet; Q8C7W7; -.
DR   PhosphoSitePlus; Q8C7W7; -.
DR   PaxDb; 10090-ENSMUSP00000029435; -.
DR   ProteomicsDB; 279394; -. [Q8C7W7-1]
DR   ProteomicsDB; 279395; -. [Q8C7W7-2]
DR   ProteomicsDB; 279396; -. [Q8C7W7-3]
DR   Antibodypedia; 46943; 175 antibodies from 24 providers.
DR   DNASU; 140917; -.
DR   Ensembl; ENSMUST00000029435.15; ENSMUSP00000029435.9; ENSMUSG00000027845.16. [Q8C7W7-1]
DR   Ensembl; ENSMUST00000063502.13; ENSMUSP00000067695.7; ENSMUSG00000027845.16. [Q8C7W7-2]
DR   Ensembl; ENSMUST00000106832.2; ENSMUSP00000102445.2; ENSMUSG00000027845.16. [Q8C7W7-3]
DR   Ensembl; ENSMUST00000106834.8; ENSMUSP00000102447.2; ENSMUSG00000027845.16. [Q8C7W7-1]
DR   GeneID; 140917; -.
DR   KEGG; mmu:140917; -.
DR   UCSC; uc008qtl.1; mouse. [Q8C7W7-1]
DR   UCSC; uc008qtp.1; mouse. [Q8C7W7-3]
DR   AGR; MGI:2156057; -.
DR   CTD; 64858; -.
DR   MGI; MGI:2156057; Dclre1b.
DR   VEuPathDB; HostDB:ENSMUSG00000027845; -.
DR   eggNOG; KOG1361; Eukaryota.
DR   GeneTree; ENSGT00940000158175; -.
DR   HOGENOM; CLU_034741_0_0_1; -.
DR   InParanoid; Q8C7W7; -.
DR   OMA; VQQYMNS; -.
DR   OrthoDB; 23465at2759; -.
DR   PhylomeDB; Q8C7W7; -.
DR   TreeFam; TF329572; -.
DR   Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR   BioGRID-ORCS; 140917; 23 hits in 112 CRISPR screens.
DR   PRO; PR:Q8C7W7; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8C7W7; Protein.
DR   Bgee; ENSMUSG00000027845; Expressed in granulocyte and 232 other cell types or tissues.
DR   ExpressionAtlas; Q8C7W7; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISA:MGI.
DR   GO; GO:0035312; F:5'-3' DNA exonuclease activity; IBA:GO_Central.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; IMP: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:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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:MGI.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISA:MGI.
DR   GO; GO:0031848; P:protection from non-homologous end joining at telomere; IMP:UniProtKB.
DR   GO; GO:0016233; P:telomere capping; ISO:MGI.
DR   GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR   GO; GO:0010833; P:telomere maintenance via telomere lengthening; ISO:MGI.
DR   GO; GO:0031860; P:telomeric 3' overhang formation; IMP:UniProtKB.
DR   GO; GO:0031627; P:telomeric loop formation; IMP:UniProtKB.
DR   CDD; cd16273; SNM1A-1C-like_MBL-fold; 1.
DR   Gene3D; 3.40.50.12650; -; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR011084; DRMBL.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR23240:SF8; 5' EXONUCLEASE APOLLO; 1.
DR   PANTHER; PTHR23240; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1.
DR   Pfam; PF07522; DRMBL; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   Genevisible; Q8C7W7; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW   DNA repair; Exonuclease; Hydrolase; Isopeptide bond; Nuclease; Nucleus;
KW   Reference proteome; Telomere; Ubl conjugation.
FT   CHAIN           1..541
FT                   /note="5' exonuclease Apollo"
FT                   /id="PRO_0000209120"
FT   REGION          455..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           492..507
FT                   /note="TBM"
FT   CROSSLNK        334
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H816"
FT   VAR_SEQ         1..126
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015174"
FT   VAR_SEQ         181..213
FT                   /note="LYSLGKESLLEQLALEFRTWVVLSPQRLELVQL -> ERFPFFFHSCLVNQN
FT                   SLKVLIVFQIFVPCSPFL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015175"
FT   VAR_SEQ         214..541
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015176"
FT   MUTAGEN         14
FT                   /note="D->A: Abolishes exonuclease activity without
FT                   affecting the telomere localization, leading to impaired
FT                   3'-overhang at the leading end telomeres."
FT                   /evidence="ECO:0000269|PubMed:20551906"
FT   MUTAGEN         31..35
FT                   /note="HMHCD->AMACN: Abolishes exonuclease activity,
FT                   leading to activate the ATM signaling pathway; when
FT                   associated with A-230."
FT                   /evidence="ECO:0000269|PubMed:20619712"
FT   MUTAGEN         230
FT                   /note="H->A: Abolishes exonuclease activity, leading to
FT                   activate the ATM signaling pathway; when associated with
FT                   31-A--N-35."
FT                   /evidence="ECO:0000269|PubMed:20619712"
FT   MUTAGEN         500..504
FT                   /note="Missing: Abolishes interaction with TERF2 and
FT                   localization to telomeres, leading to activate the ATM
FT                   signaling pathway."
FT                   /evidence="ECO:0000269|PubMed:20619712"
FT   CONFLICT        49
FT                   /note="Y -> D (in Ref. 1; BAE23379)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="T -> S (in Ref. 1; BAC33550)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="Y -> H (in Ref. 3; AAI25278)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412
FT                   /note="P -> L (in Ref. 3; AAI25278)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        540
FT                   /note="V -> D (in Ref. 1; BAE23700)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   541 AA;  61069 MW;  884FB1A8E452A76C CRC64;
     MNGVVIPQTP IAVDFWSLRR AGSARLFFLT HMHCDHTVGL SSTWARPLYC SPITACLLHR
     RLQVSKHWIR ALEVGESHVL PLDEIGQETM TVTLIDANHC PGSVMFLFEG YFGTILYTGD
     FRYTPSMLKE PALILGKQIH TLYLDNTNCN PALVLPSRQE ATQQIVQLIR QFPQHNIKIG
     LYSLGKESLL EQLALEFRTW VVLSPQRLEL VQLLGLADVF TVEEEAGRIH AVDHTEICHS
     AMLQWNQSHP TIAIFPTSRK VRSPHPSIYT VPYSDHSSYS ELRAFVAALR PCQVVPIVHQ
     KPCGEFFQDS LSPRLAMPLI PHSVQQYMSS SSRKTNVLWQ LERRLKRPRT QGVVFESPEE
     KANQVKVDRD SKKHKKENLS PWAGHLERLC PHPLQARKQL FPDFCRKERD EPVLFCDSNK
     MATVLTAPLE FSVQLQPIDE FLFPETREKI GLESPLLSRG DSGSPARGNQ SDCVGCGSPP
     AHISRAVPLT PESRGLALKY LLTPVHFLQA GFSSRNFDKQ VEKHQRVQRS SPAVLSPVDV
     G
//