EXO5_MOUSE
ID EXO5_MOUSE Reviewed; 373 AA.
AC Q9CXP9; A2A767; A2A769;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Exonuclease V;
DE Short=Exo V;
DE Short=mExo5;
DE EC=3.1.-.-;
DE AltName: Full=Defects in morphology protein 1 homolog;
GN Name=Exo5; Synonyms=Dem1;
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].
RC STRAIN=C57BL/6J; TISSUE=Head;
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].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 COFACTOR.
RX PubMed=23095756; DOI=10.1074/jbc.m112.422444;
RA Sparks J.L., Kumar R., Singh M., Wold M.S., Pandita T.K., Burgers P.M.;
RT "Human exonuclease 5 is a novel sliding exonuclease required for genome
RT stability.";
RL J. Biol. Chem. 287:42773-42783(2012).
CC -!- FUNCTION: Single-stranded DNA (ssDNA) bidirectional exonuclease
CC involved in DNA repair. Probably involved in DNA repair following
CC ultraviolet (UV) irradiation and interstrand cross-links (ICLs) damage.
CC Has both 5'-3' and 3'-5' exonuclease activities with a strong
CC preference for 5'-ends. Acts as a sliding exonuclease that loads at
CC ssDNA ends and then slides along the ssDNA prior to cutting; however
CC the sliding and the 3'-5' exonuclease activities are abolished upon
CC binding to the replication protein A (RPA) complex that enforces 5'-
CC directionality activity (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P38289};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:23095756};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:23095756};
CC -!- SUBUNIT: Monomer; monomeric form has weak exonuclease activity.
CC Homodimer; homodimeric form is unsure but has much higher exonuclease
CC activity, suggesting that it could homodimerize upon DNA-binding.
CC Interacts with the replication protein A (RPA) complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}. Note=Localizes to repair foci in response to DNA damage.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EXO5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM16720.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM16722.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK014134; BAB29174.1; -; mRNA.
DR EMBL; AL606904; CAM16720.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL606904; CAM16721.1; -; Genomic_DNA.
DR EMBL; AL606904; CAM16722.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC023360; AAH23360.1; -; mRNA.
DR CCDS; CCDS18596.1; -.
DR RefSeq; NP_001153515.1; NM_001160043.1.
DR RefSeq; NP_082733.1; NM_028457.2.
DR AlphaFoldDB; Q9CXP9; -.
DR SMR; Q9CXP9; -.
DR STRING; 10090.ENSMUSP00000030375; -.
DR PhosphoSitePlus; Q9CXP9; -.
DR PaxDb; Q9CXP9; -.
DR PRIDE; Q9CXP9; -.
DR ProteomicsDB; 275790; -.
DR Antibodypedia; 32100; 88 antibodies from 19 providers.
DR DNASU; 73172; -.
DR Ensembl; ENSMUST00000030375; ENSMUSP00000030375; ENSMUSG00000028629.
DR Ensembl; ENSMUST00000177880; ENSMUSP00000136408; ENSMUSG00000028629.
DR GeneID; 73172; -.
DR KEGG; mmu:73172; -.
DR UCSC; uc008unt.1; mouse.
DR CTD; 64789; -.
DR MGI; MGI:1920422; Exo5.
DR VEuPathDB; HostDB:ENSMUSG00000028629; -.
DR eggNOG; KOG4760; Eukaryota.
DR GeneTree; ENSGT00390000015205; -.
DR HOGENOM; CLU_013225_0_2_1; -.
DR InParanoid; Q9CXP9; -.
DR OMA; STQNWCE; -.
DR OrthoDB; 1601909at2759; -.
DR PhylomeDB; Q9CXP9; -.
DR TreeFam; TF332529; -.
DR BioGRID-ORCS; 73172; 0 hits in 107 CRISPR screens.
DR PRO; PR:Q9CXP9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9CXP9; protein.
DR Bgee; ENSMUSG00000028629; Expressed in manus and 191 other tissues.
DR ExpressionAtlas; Q9CXP9; baseline and differential.
DR Genevisible; Q9CXP9; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR Gene3D; 3.90.320.10; -; 1.
DR InterPro; IPR019190; EXOV.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR PANTHER; PTHR14464; PTHR14464; 1.
DR Pfam; PF09810; Exo5; 2.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Cytoplasm; DNA damage; DNA repair; DNA-binding; Exonuclease;
KW Hydrolase; Iron; Iron-sulfur; Magnesium; Metal-binding; Nuclease; Nucleus;
KW Reference proteome.
FT CHAIN 1..373
FT /note="Exonuclease V"
FT /id="PRO_0000307321"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 373 AA; 41624 MW; 7190B447ED0ABB2C CRC64;
MAETGEEETA SAEASGFSDL SDSELVEFLD LEEAKESAVS LSKPGPSAEL PGKDDKPVSL
QNWKGGLDVL SPMERFHLKY LYVTDLCTQN WCELQMVYGK ELPGSLTPEK AAVLDTGASI
HLAKELELHD LVTVPIATKE DAWAVKFLNI LAMIPALQSE GRVREFPVFG EVEGIFLVGV
IDELHYTSKG ELELAELKTR RRPVLPLPAQ KKKDYFQVSL YKYIFDAMVQ GKVTPASLIH
HTKLCLDKPL GPSVLRHARQ GGVSVKSLGD LMELVFLSLT LSDLPAIDTL KLEYIHQETA
TILGTEIVAF EEKEVKSKVQ HYVAYWMGHR DPQGVDVEEA WKCRTCDYVD ICEWRRGSGV
LSSSWEPKAK KFK
