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Exonuclease V (Exo V) (hExo5) (EC 3.1.-.-) (Defects in morphology protein 1 homolog)

 EXO5_HUMAN              Reviewed;         373 AA.
Q9H790; D3DPV4; Q5SWM7; Q5SWM8; Q5SWM9; Q5SWN0; Q5SWN1; Q8WTW9;
23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 106.
RecName: Full=Exonuclease V;
Short=Exo V;
Short=hExo5;
EC=3.1.-.-;
AltName: Full=Defects in morphology protein 1 homolog;
Name=EXO5; Synonyms=C1orf176, DEM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Coronary artery;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-172.
TISSUE=Ovary;
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).
[5]
FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, COFACTOR,
INTERACTION WITH THE REPLICATION PROTEIN A (RPA) COMPLEX, MUTAGENESIS
OF GLU-196; CYS-343 AND CYS-346, AND CHARACTERIZATION OF VARIANTS
ASN-115 AND VAL-172.
PubMed=23095756; DOI=10.1074/jbc.M112.422444;
Sparks J.L., Kumar R., Singh M., Wold M.S., Pandita T.K.,
Burgers P.M.;
"Human exonuclease 5 is a novel sliding exonuclease required for
genome stability.";
J. Biol. Chem. 287:42773-42783(2012).
-!- FUNCTION: Single-stranded DNA (ssDNA) bidirectional exonuclease
involved in DNA repair. Probably involved in DNA repair following
ultraviolet (UV) irradiation and interstrand cross-links (ICLs)
damage. Has both 5'-3' and 3'-5' exonuclease activities with a
strong preference for 5'-ends. Acts as a sliding exonuclease that
loads at ssDNA ends and then slides along the ssDNA prior to
cutting; however the sliding and the 3'-5' exonuclease activities
are abolished upon binding to the replication protein A (RPA)
complex that enforces 5'-directionality activity.
{ECO:0000269|PubMed:23095756}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000269|PubMed:23095756};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:23095756};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- SUBUNIT: Monomer; monomeric form has weak exonuclease activity.
Homodimer; homodimeric form is unsure but has much higher
exonuclease activity, suggesting that it could homodimerize upon
DNA-binding. Interacts with the replication protein A (RPA)
complex. {ECO:0000269|PubMed:23095756}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23095756}.
Cytoplasm, cytosol {ECO:0000269|PubMed:23095756}. Note=Localizes
to repair foci in response to DNA damage.
-!- SIMILARITY: Belongs to the EXO5 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK024797; BAB15008.1; -; mRNA.
EMBL; AL603839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07210.1; -; Genomic_DNA.
EMBL; CH471059; EAX07211.1; -; Genomic_DNA.
EMBL; CH471059; EAX07212.1; -; Genomic_DNA.
EMBL; CH471059; EAX07213.1; -; Genomic_DNA.
EMBL; CH471059; EAX07214.1; -; Genomic_DNA.
EMBL; BC021969; AAH21969.1; -; mRNA.
CCDS; CCDS453.1; -.
RefSeq; NP_001333875.1; NM_001346946.1.
RefSeq; NP_001333876.1; NM_001346947.1.
RefSeq; NP_001333877.1; NM_001346948.1.
RefSeq; NP_001333878.1; NM_001346949.1.
RefSeq; NP_001333879.1; NM_001346950.1.
RefSeq; NP_001333880.1; NM_001346951.1.
RefSeq; NP_001333881.1; NM_001346952.1.
RefSeq; NP_001333882.1; NM_001346953.1.
RefSeq; NP_001333883.1; NM_001346954.1.
RefSeq; NP_001333884.1; NM_001346955.1.
RefSeq; NP_001333885.1; NM_001346956.1.
RefSeq; NP_073611.1; NM_022774.2.
RefSeq; XP_016857588.1; XM_017002099.1.
RefSeq; XP_016857591.1; XM_017002102.1.
UniGene; Hs.59584; -.
UniGene; Hs.733167; -.
ProteinModelPortal; Q9H790; -.
BioGrid; 122299; 2.
STRING; 9606.ENSP00000296380; -.
iPTMnet; Q9H790; -.
PhosphoSitePlus; Q9H790; -.
BioMuta; EXO5; -.
DMDM; 74752706; -.
MaxQB; Q9H790; -.
PaxDb; Q9H790; -.
PeptideAtlas; Q9H790; -.
PRIDE; Q9H790; -.
ProteomicsDB; 81089; -.
DNASU; 64789; -.
Ensembl; ENST00000296380; ENSP00000296380; ENSG00000164002.
Ensembl; ENST00000358527; ENSP00000351328; ENSG00000164002.
Ensembl; ENST00000372703; ENSP00000361788; ENSG00000164002.
GeneID; 64789; -.
KEGG; hsa:64789; -.
UCSC; uc001cfp.4; human.
CTD; 64789; -.
EuPathDB; HostDB:ENSG00000164002.11; -.
GeneCards; EXO5; -.
HGNC; HGNC:26115; EXO5.
HPA; HPA028429; -.
neXtProt; NX_Q9H790; -.
OpenTargets; ENSG00000164002; -.
PharmGKB; PA164718736; -.
eggNOG; KOG4760; Eukaryota.
eggNOG; ENOG4111IID; LUCA.
GeneTree; ENSGT00390000015205; -.
HOVERGEN; HBG095898; -.
InParanoid; Q9H790; -.
KO; K17815; -.
OMA; KKKDCFQ; -.
OrthoDB; EOG091G0M7G; -.
PhylomeDB; Q9H790; -.
TreeFam; TF332529; -.
GenomeRNAi; 64789; -.
PRO; PR:Q9H790; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000164002; Expressed in 152 organ(s), highest expression level in secondary oocyte.
CleanEx; HS_DEM1; -.
ExpressionAtlas; Q9H790; baseline and differential.
Genevisible; Q9H790; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; TAS:UniProtKB.
GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; IDA:UniProtKB.
GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB.
InterPro; IPR019190; EXOV.
Pfam; PF09810; Exo5; 2.
1: Evidence at protein level;
4Fe-4S; Complete proteome; Cytoplasm; DNA damage; DNA repair;
DNA-binding; Exonuclease; Hydrolase; Iron; Iron-sulfur; Magnesium;
Metal-binding; Nuclease; Nucleus; Polymorphism; Reference proteome.
CHAIN 1 373 Exonuclease V.
/FTId=PRO_0000307320.
METAL 92 92 Iron-sulfur (4Fe-4S).
METAL 343 343 Iron-sulfur (4Fe-4S).
METAL 346 346 Iron-sulfur (4Fe-4S).
METAL 352 352 Iron-sulfur (4Fe-4S).
VARIANT 115 115 D -> N (polymorphism; does not affect
exonuclease activity; dbSNP:rs1134586).
{ECO:0000269|PubMed:23095756}.
/FTId=VAR_035407.
VARIANT 172 172 G -> V (polymorphism; does not affect
exonuclease activity; dbSNP:rs11208299).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:23095756}.
/FTId=VAR_035408.
MUTAGEN 196 196 E->A: Nearly abolishes exonuclease
activity. {ECO:0000269|PubMed:23095756}.
MUTAGEN 343 343 C->A: Abolishes iron-sulfur-binding and
affects exonuclease activity; when
associated with A-346.
{ECO:0000269|PubMed:23095756}.
MUTAGEN 346 346 C->A: Abolishes iron-sulfur-binding and
affects exonuclease activity; when
associated with A-343.
{ECO:0000269|PubMed:23095756}.
SEQUENCE 373 AA; 41816 MW; EAFB31099EA40FAD CRC64;
MAETREEETV SAEASGFSDL SDSEFLEFLD LEDAQESKAL VNMPGPSSES LGKDDKPISL
QNWKRGLDIL SPMERFHLKY LYVTDLATQN WCELQTAYGK ELPGFLAPEK AAVLDTGASI
HLARELELHD LVTVPVTTKE DAWAIKFLNI LLLIPTLQSE GHIREFPVFG EGEGVLLVGV
IDELHYTAKG ELELAELKTR RRPMLPLEAQ KKKDCFQVSL YKYIFDAMVQ GKVTPASLIH
HTKLCLEKPL GPSVLRHAQQ GGFSVKSLGD LMELVFLSLT LSDLPVIDIL KIEYIHQETA
TVLGTEIVAF KEKEVRAKVQ HYMAYWMGHR EPQGVDVEEA WKCRTCTYAD ICEWRKGSGV
LSSTLAPQVK KAK


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