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5' exonuclease Apollo (EC 3.1.-.-) (DNA cross-link repair 1B protein) (SNM1 homolog B)

 DCR1B_MOUSE             Reviewed;         541 AA.
Q8C7W7; A0JLW2; B0V3N9; B0V3P0; Q3U4P2; Q3UUC7; Q3UV92; Q6NXL4;
Q8BN95; Q8BQS8; Q921S0;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
16-AUG-2005, sequence version 2.
23-MAY-2018, entry version 113.
RecName: Full=5' exonuclease Apollo;
EC=3.1.-.-;
AltName: Full=DNA cross-link repair 1B protein;
AltName: Full=SNM1 homolog B;
Name=Dclre1b; Synonyms=Snm1b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J, and NOD;
TISSUE=Adipose tissue, Bone, Eye, Spinal cord, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 82-541 (ISOFORM 1).
STRAIN=Czech II; TISSUE=Brain, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
OF ASP-14.
PubMed=20551906; DOI=10.1038/emboj.2010.58;
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.;
"SNMIB/Apollo protects leading-strand telomeres against NHEJ-mediated
repair.";
EMBO J. 29:2230-2241(2010).
[5]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF 31-HIS--ASP-35; HIS-230 AND
500-TYR--PRO-504.
PubMed=20619712; DOI=10.1016/j.molcel.2010.06.031;
Wu P., van Overbeek M., Rooney S., de Lange T.;
"Apollo contributes to G overhang maintenance and protects leading-end
telomeres.";
Mol. Cell 39:606-617(2010).
-!- 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. {ECO:0000269|PubMed:20551906,
ECO:0000269|PubMed:20619712}.
-!- SUBUNIT: Interacts with MUS81, MRE11 and FANCD2. Interacts with
HSPA2, HSPA8 and HSPA14. Interacts with SPAG5 (By similarity).
Interacts with TERF2; the interaction is direct. {ECO:0000250,
ECO:0000269|PubMed:20619712}.
-!- SUBCELLULAR LOCATION: Chromosome, telomere
{ECO:0000269|PubMed:20551906, ECO:0000269|PubMed:20619712}.
Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250}. Note=Mainly localizes
to telomeres, recruited via its interaction with TERF2. During
mitosis, localizes to the centrosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8C7W7-1; Sequence=Displayed;
Name=2;
IsoId=Q8C7W7-2; Sequence=VSP_015174;
Name=3;
IsoId=Q8C7W7-3; Sequence=VSP_015175, VSP_015176;
Note=No experimental confirmation available.;
-!- DOMAIN: The TBM domain mediates interaction with TERF2.
{ECO:0000250}.
-!- PTM: Ubiquitinated, leading to its degradation. Interaction with
TERF2 protects it from ubiquitination (By similarity).
{ECO:0000250}.
-!- 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. {ECO:0000269|PubMed:20551906,
ECO:0000269|PubMed:20619712}.
-!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase
(DRMBL) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH11094.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC39165.1; Type=Frameshift; Positions=55; Evidence={ECO:0000305};
Sequence=BAE23379.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK046571; BAC32791.1; -; mRNA.
EMBL; AK049115; BAC33550.1; -; mRNA.
EMBL; AK084347; BAC39165.1; ALT_FRAME; mRNA.
EMBL; AK134324; BAE22098.1; -; mRNA.
EMBL; AK137495; BAE23379.1; ALT_INIT; mRNA.
EMBL; AK138568; BAE23700.1; -; mRNA.
EMBL; AK154124; BAE32389.1; -; mRNA.
EMBL; CU210953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011094; AAH11094.1; ALT_INIT; mRNA.
EMBL; BC067017; AAH67017.1; -; mRNA.
EMBL; BC125277; AAI25278.1; -; mRNA.
CCDS; CCDS17694.1; -. [Q8C7W7-1]
CCDS; CCDS17695.1; -. [Q8C7W7-2]
RefSeq; NP_001020483.1; NM_001025312.1. [Q8C7W7-2]
RefSeq; NP_598626.2; NM_133865.2. [Q8C7W7-1]
UniGene; Mm.374850; -.
ProteinModelPortal; Q8C7W7; -.
SMR; Q8C7W7; -.
BioGrid; 228331; 10.
IntAct; Q8C7W7; 9.
STRING; 10090.ENSMUSP00000029435; -.
iPTMnet; Q8C7W7; -.
PhosphoSitePlus; Q8C7W7; -.
PaxDb; Q8C7W7; -.
PRIDE; Q8C7W7; -.
Ensembl; ENSMUST00000029435; ENSMUSP00000029435; ENSMUSG00000027845. [Q8C7W7-1]
Ensembl; ENSMUST00000063502; ENSMUSP00000067695; ENSMUSG00000027845. [Q8C7W7-2]
Ensembl; ENSMUST00000106832; ENSMUSP00000102445; ENSMUSG00000027845. [Q8C7W7-3]
Ensembl; ENSMUST00000106834; ENSMUSP00000102447; ENSMUSG00000027845. [Q8C7W7-1]
GeneID; 140917; -.
KEGG; mmu:140917; -.
UCSC; uc008qtl.1; mouse. [Q8C7W7-1]
UCSC; uc008qtp.1; mouse. [Q8C7W7-3]
CTD; 64858; -.
MGI; MGI:2156057; Dclre1b.
eggNOG; KOG1361; Eukaryota.
eggNOG; COG1236; LUCA.
GeneTree; ENSGT00530000063183; -.
HOVERGEN; HBG081420; -.
InParanoid; Q8C7W7; -.
KO; K15341; -.
OMA; PCQVVPI; -.
OrthoDB; EOG091G0DBZ; -.
PhylomeDB; Q8C7W7; -.
TreeFam; TF329572; -.
Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
PRO; PR:Q8C7W7; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027845; -.
ExpressionAtlas; Q8C7W7; baseline and differential.
Genevisible; Q8C7W7; MM.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISA:MGI.
GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
GO; GO:0008409; F:5'-3' exonuclease activity; IMP:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0000075; P:cell cycle checkpoint; ISS:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
GO; GO:0036297; P:interstrand cross-link repair; ISO:MGI.
GO; GO:0006289; P:nucleotide-excision repair; ISA:MGI.
GO; GO:0031848; P:protection from non-homologous end joining at telomere; IMP:UniProtKB.
GO; GO:0016233; P:telomere capping; ISO:MGI.
GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
GO; GO:0010833; P:telomere maintenance via telomere lengthening; ISO:MGI.
GO; GO:0031860; P:telomeric 3' overhang formation; IMP:UniProtKB.
GO; GO:0031627; P:telomeric loop formation; IMP:UniProtKB.
Gene3D; 3.60.15.10; -; 2.
InterPro; IPR011084; DRMBL.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
Pfam; PF07522; DRMBL; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
Alternative splicing; Chromosome; Complete proteome; Cytoplasm;
Cytoskeleton; DNA damage; DNA repair; Exonuclease; Hydrolase;
Isopeptide bond; Nuclease; Nucleus; Reference proteome; Telomere;
Ubl conjugation.
CHAIN 1 541 5' exonuclease Apollo.
/FTId=PRO_0000209120.
MOTIF 492 507 TBM.
CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9H816}.
VAR_SEQ 1 126 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_015174.
VAR_SEQ 181 213 LYSLGKESLLEQLALEFRTWVVLSPQRLELVQL -> ERFP
FFFHSCLVNQNSLKVLIVFQIFVPCSPFL (in isoform
3). {ECO:0000303|PubMed:16141072}.
/FTId=VSP_015175.
VAR_SEQ 214 541 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_015176.
MUTAGEN 14 14 D->A: Abolishes exonuclease activity
without affecting the telomere
localization, leading to impaired 3'-
overhang at the leading end telomeres.
{ECO:0000269|PubMed:20551906}.
MUTAGEN 31 35 HMHCD->AMACN: Abolishes exonuclease
activity, leading to activate the ATM
signaling pathway; when associated with
A-230. {ECO:0000269|PubMed:20619712}.
MUTAGEN 230 230 H->A: Abolishes exonuclease activity,
leading to activate the ATM signaling
pathway; when associated with 31-A--N-35.
{ECO:0000269|PubMed:20619712}.
MUTAGEN 500 504 Missing: Abolishes interaction with TERF2
and localization to telomeres, leading to
activate the ATM signaling pathway.
{ECO:0000269|PubMed:20619712}.
CONFLICT 49 49 Y -> D (in Ref. 1; BAE23379).
{ECO:0000305}.
CONFLICT 162 162 T -> S (in Ref. 1; BAC33550).
{ECO:0000305}.
CONFLICT 327 327 Y -> H (in Ref. 3; AAI25278).
{ECO:0000305}.
CONFLICT 412 412 P -> L (in Ref. 3; AAI25278).
{ECO:0000305}.
CONFLICT 540 540 V -> D (in Ref. 1; BAE23700).
{ECO:0000305}.
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


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