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Q8C7W7 (DCR1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5' exonuclease Apollo

EC=3.1.-.-
Alternative name(s):
DNA cross-link repair 1B protein
SNM1 homolog B
Gene names
Name:Dclre1b
Synonyms:Snm1b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

5'-3' exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity: generates 3' single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomeres that are vulnerable to end-joining reactions and expose the telomere end in a manner that activates the DNA repair pathways. Together with TERF2, required to protect telomeres from replicative damage during replication by controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Also involved in response to DNA damage: plays a role in response to DNA interstrand cross-links (ICLs) by facilitating double-strand break formation. In case of spindle stress, involved in prophase checkpoint. Ref.4 Ref.5

Subunit structure

Interacts with MUS81, MRE11 and FANCD2. Interacts with HSPA2, HSPA8 and HSPA14. Interacts with SPAG5 By similarity. Interacts with TERF2; the interaction is direct. Ref.5

Subcellular location

Chromosometelomere. Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Mainly localizes to telomeres, recruited via its interaction with TERF2. During mitosis, localizes to the centrosome. Ref.4 Ref.5

Domain

The TBM domain mediates interaction with TERF2 By similarity.

Post-translational modification

Ubiquitinated, leading to its degradation. Interaction with TERF2 protects it from ubiquitination By similarity.

Disruption phenotype

Embryos are smaller than wild-type embryos and neonates die at postnatal day 0 (P0). Cells activate the ATM kinase at their telomeres in S phase and show leading-end telomere fusions which are accompanied by a reduction in the telomeric overhang signal. Ref.4 Ref.5

Sequence similarities

Belongs to the DNA repair metallo-beta-lactamase (DRMBL) family.

Sequence caution

The sequence AAH11094.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC39165.1 differs from that shown. Reason: Frameshift at position 55.

The sequence BAE23379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentChromosome
Cytoplasm
Cytoskeleton
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
   Molecular functionExonuclease
Hydrolase
Nuclease
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

nucleic acid phosphodiester bond hydrolysis

Inferred from mutant phenotype Ref.4Ref.5. Source: GOC

nucleotide-excision repair

Inferred from sequence alignment PubMed 10848582. Source: MGI

protection from non-homologous end joining at telomere

Inferred from mutant phenotype Ref.4Ref.5. Source: UniProtKB

telomere maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

telomeric 3' overhang formation

Inferred from mutant phenotype Ref.4Ref.5. Source: UniProtKB

telomeric loop formation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome, telomeric region

Inferred from direct assay Ref.4Ref.5. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from sequence alignment PubMed 10848582. Source: MGI

   Molecular_function5'-3' exonuclease activity

Inferred from mutant phenotype Ref.4Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8C7W7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8C7W7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-126: Missing.
Isoform 3 (identifier: Q8C7W7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     181-213: LYSLGKESLLEQLALEFRTWVVLSPQRLELVQL → ERFPFFFHSCLVNQNSLKVLIVFQIFVPCSPFL
     214-541: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5415415' exonuclease Apollo
PRO_0000209120

Regions

Motif492 – 50716TBM

Natural variations

Alternative sequence1 – 126126Missing in isoform 2.
VSP_015174
Alternative sequence181 – 21333LYSLG…ELVQL → ERFPFFFHSCLVNQNSLKVL IVFQIFVPCSPFL in isoform 3.
VSP_015175
Alternative sequence214 – 541328Missing in isoform 3.
VSP_015176

Experimental info

Mutagenesis141D → A: Abolishes exonuclease activity without affecting the telomere localization, leading to impaired 3'-overhang at the leading end telomeres. Ref.4
Mutagenesis31 – 355HMHCD → AMACN: Abolishes exonuclease activity, leading to activate the ATM signaling pathway; when associated with A-230. Ref.5
Mutagenesis2301H → A: Abolishes exonuclease activity, leading to activate the ATM signaling pathway; when associated with 31-A--N-35. Ref.5
Mutagenesis500 – 5045Missing: Abolishes interaction with TERF2 and localization to telomeres, leading to activate the ATM signaling pathway. Ref.5
Sequence conflict491Y → D in BAE23379. Ref.1
Sequence conflict1621T → S in BAC33550. Ref.1
Sequence conflict3271Y → H in AAI25278. Ref.3
Sequence conflict4121P → L in AAI25278. Ref.3
Sequence conflict5401V → D in BAE23700. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: 884FB1A8E452A76C

FASTA54161,069
        10         20         30         40         50         60 
MNGVVIPQTP IAVDFWSLRR AGSARLFFLT HMHCDHTVGL SSTWARPLYC SPITACLLHR 

        70         80         90        100        110        120 
RLQVSKHWIR ALEVGESHVL PLDEIGQETM TVTLIDANHC PGSVMFLFEG YFGTILYTGD 

       130        140        150        160        170        180 
FRYTPSMLKE PALILGKQIH TLYLDNTNCN PALVLPSRQE ATQQIVQLIR QFPQHNIKIG 

       190        200        210        220        230        240 
LYSLGKESLL EQLALEFRTW VVLSPQRLEL VQLLGLADVF TVEEEAGRIH AVDHTEICHS 

       250        260        270        280        290        300 
AMLQWNQSHP TIAIFPTSRK VRSPHPSIYT VPYSDHSSYS ELRAFVAALR PCQVVPIVHQ 

       310        320        330        340        350        360 
KPCGEFFQDS LSPRLAMPLI PHSVQQYMSS SSRKTNVLWQ LERRLKRPRT QGVVFESPEE 

       370        380        390        400        410        420 
KANQVKVDRD SKKHKKENLS PWAGHLERLC PHPLQARKQL FPDFCRKERD EPVLFCDSNK 

       430        440        450        460        470        480 
MATVLTAPLE FSVQLQPIDE FLFPETREKI GLESPLLSRG DSGSPARGNQ SDCVGCGSPP 

       490        500        510        520        530        540 
AHISRAVPLT PESRGLALKY LLTPVHFLQA GFSSRNFDKQ VEKHQRVQRS SPAVLSPVDV 


G 

« Hide

Isoform 2 [UniParc].

Checksum: D887FB35BE7747E3
Show »

FASTA41546,864
Isoform 3 [UniParc].

Checksum: 56845E3156F33971
Show »

FASTA21324,254

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Adipose tissue, Bone, Eye, Spinal cord and Testis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-541 (ISOFORM 1).
Strain: Czech II.
Tissue: Brain and Mammary gland.
[4]"SNMIB/Apollo protects leading-strand telomeres against NHEJ-mediated repair."
Lam Y.C., Akhter S., Gu P., Ye J., Poulet A., Giraud-Panis M.J., Bailey S.M., Gilson E., Legerski R.J., Chang S.
EMBO J. 29:2230-2241(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-14.
[5]"Apollo contributes to G overhang maintenance and protects leading-end telomeres."
Wu P., van Overbeek M., Rooney S., de Lange T.
Mol. Cell 39:606-617(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2, DISRUPTION PHENOTYPE, MUTAGENESIS OF 31-HIS--ASP-35; HIS-230 AND 500-TYR--PRO-504.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK046571 mRNA. Translation: BAC32791.1.
AK049115 mRNA. Translation: BAC33550.1.
AK084347 mRNA. Translation: BAC39165.1. Frameshift.
AK134324 mRNA. Translation: BAE22098.1.
AK137495 mRNA. Translation: BAE23379.1. Different initiation.
AK138568 mRNA. Translation: BAE23700.1.
AK154124 mRNA. Translation: BAE32389.1.
CU210953 Genomic DNA. Translation: CAQ12168.1.
CU210953 Genomic DNA. Translation: CAQ12169.1.
BC011094 mRNA. Translation: AAH11094.1. Different initiation.
BC067017 mRNA. Translation: AAH67017.1.
BC125277 mRNA. Translation: AAI25278.1.
CCDSCCDS17694.1. [Q8C7W7-1]
CCDS17695.1. [Q8C7W7-2]
RefSeqNP_001020483.1. NM_001025312.1. [Q8C7W7-2]
NP_598626.2. NM_133865.2. [Q8C7W7-1]
UniGeneMm.374850.

3D structure databases

ProteinModelPortalQ8C7W7.
SMRQ8C7W7. Positions 1-314.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ8C7W7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029435; ENSMUSP00000029435; ENSMUSG00000027845. [Q8C7W7-1]
ENSMUST00000063502; ENSMUSP00000067695; ENSMUSG00000027845. [Q8C7W7-2]
ENSMUST00000106832; ENSMUSP00000102445; ENSMUSG00000027845. [Q8C7W7-3]
ENSMUST00000106834; ENSMUSP00000102447; ENSMUSG00000027845. [Q8C7W7-1]
GeneID140917.
KEGGmmu:140917.
UCSCuc008qtl.1. mouse. [Q8C7W7-1]
uc008qto.1. mouse. [Q8C7W7-3]

Organism-specific databases

CTD64858.
MGIMGI:2156057. Dclre1b.

Phylogenomic databases

eggNOGCOG1236.
GeneTreeENSGT00530000063183.
HOVERGENHBG081420.
InParanoidB0V3P0.
KOK15341.
OMAPCQVVPI.
OrthoDBEOG71VSSC.
PhylomeDBQ8C7W7.
TreeFamTF329572.

Gene expression databases

ArrayExpressQ8C7W7.
BgeeQ8C7W7.
GenevestigatorQ8C7W7.

Family and domain databases

Gene3D3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
IPR011084. DRMBL.
[Graphical view]
PfamPF07522. DRMBL. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMSSF56281. SSF56281. 1 hit.
ProtoNetSearch...

Other

NextBio370035.
PROQ8C7W7.
SOURCESearch...

Entry information

Entry nameDCR1B_MOUSE
AccessionPrimary (citable) accession number: Q8C7W7
Secondary accession number(s): A0JLW2 expand/collapse secondary AC list , B0V3N9, B0V3P0, Q3U4P2, Q3UUC7, Q3UV92, Q6NXL4, Q8BN95, Q8BQS8, Q921S0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: July 9, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot