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Description:
Exonuclease 1 (EC 3.1.-.-) (mExo1) (Exonuclease I).
Molecular weight: 92022
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) base-excision repair( GO:0006284 ) nucleotide-excision repair (and GO:0045001, a synonym)( GO:0006289 )
Important dates:
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 2.
07-MAR-2006, entry version 24.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Sciurognathi Muroidea Muridae Murinae Mus.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein EXO1_MOUSE:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AJ238213 | CAB51863.1 | - |
| EMBL | AK028728 | BAC26086.1 | - |
| EMBL | AK166425 | BAE38768.1 | - |
| EMBL | BC006671 | AAH06671.1 | - |
| Ensembl | ENSMUSG00000039748 | Mus musculus.1 | |
| MGI | MGI:1349427 | Exo1.1 | |
| GO | GO:0003677 | F:DNA binding | RCA. |
| GO | GO:0004518 | F:nuclease activity | RCA. |
| PROSITE | PS00841 | XPG_1 | FALSE_NEG. |
| PROSITE | PS00842 | XPG_2 | FALSE_NEG. |
Keywords:
DNA damage; DNA excision; DNA repair; DNA-binding; Endonuclease; Excision nuclease; Exonuclease; Hydrolase; Immune response; Meiosis; Nuclear protein; Nuclease; Phosphorylation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX MEDLINE=99428667; PubMed=10497278; DOI=10.1093/nar/27.20.4114;
RA Lee B.-I., Shannon M., Stubbs L., Wilson D.M. III;
RT "Expression specificity of the mouse exonuclease I gene (mExo1).";
RL Nucleic Acids Res. 27:4114-4120(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Skin;
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schonbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP FUNCTION.
RX PubMed=12629043; DOI=10.1101/gad.1060603;
RA Wei K., Clark A.B., Wong E., Kane M.F., Mazur D.J., Parris T.,
RA Kolas N.K., Russell R., Hou H. Jr., Kneitz B., Yang G., Kunkel T.A.,
RA Kolodner R.D., Cohen P.E., Edelmann W.;
RT "Inactivation of exonuclease 1 in mice results in DNA mismatch repair
RT defects, increased cancer susceptibility, and male and female
RT sterility.";
RL Genes Dev. 17:603-614(2003).
RN [5]
RP FUNCTION.
RX PubMed=14716311; DOI=10.1038/ni1031;
RA Bardwell P.D., Woo C.J., Wei K., Li Z., Martin A., Sack S.Z.,
RA Parris T., Edelmann W., Scharff M.D.;
RT "Altered somatic hypermutation and reduced class-switch recombination
RT in exonuclease 1-mutant mice.";
RL Nat. Immunol. 5:224-229(2004).
Feature:
CHAIN 1 837 Exonuclease 1.
/FTId=PRO_0000154040.
REGION 1 99 N-domain.
REGION 129 386 Interaction with MSH3 (By similarity).
REGION 138 229 I-domain.
REGION 387 488 Interaction with MLH1 (By similarity).
REGION 591 837 Interaction with MSH2 (By similarity).
REGION 778 837 Interaction with MLH1 (By similarity).
MOD_RES 589 589 Phosphoserine (By similarity).
CONFLICT 366 366 T -> A (in Ref. 1 and 2; BAE38768).
CONFLICT 523 523 P -> T (in Ref. 2; BAE38768).
CONFLICT 557 557 T -> M (in Ref. 1).
CONFLICT 560 560 L -> P (in Ref. 2; BAE38768).
CONFLICT 648 648 K -> Q (in Ref. 1).
CONFLICT 652 652 L -> P (in Ref. 1 and 2; BAE38768).
CONFLICT 666 666 S -> L (in Ref. 1).
Comments:
-!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also
possess a cryptic 3'->5' double-stranded DNA exonuclease activity.
Functions in DNA mismatch repair (MMR) to excise mismatch-
containing DNA tracts directed by strand breaks located either 5'
or 3' to the mismatch. Also exhibits endonuclease activity against
5' overhanging flap structures similar to those generated by
displacement synthesis when DNA polymerase encounters the 5' end
of a downstream Okazaki fragment. Required for somatic
hypermutation (SHM) and class switch recombination (CSR) of
immunoglobulin genes. Essential for male and female meiosis.
-!- SUBUNIT: Interacts with the MLH1-PMS2 heterodimer via MLH1.
Interacts with MSH3. Interacts with the MSH2-MSH6 heterodimer via
MSH2, and this interaction may increase the processivity of the
5'->3' exonuclease activity. Interacts with PCNA, and this
interaction may both stimulate the cryptic 3'->5' exonuclease
activity and suppress the 5'->3' exonuclease activity. Interacts
with WRN, and this interaction stimulates both the 5'->3'
exonuclease activity and cleavage of 5' overhanging flap
structures. Interacts with RECQL/RECQ1, and this interaction
stimulates cleavage of 5' overhanging flap structures (By
similarity).
-!- SUBCELLULAR LOCATION: Nuclear. Colocalizes with PCNA to discrete
nuclear foci in S-phase (By similarity).
-!- TISSUE SPECIFICITY: Highly expressed in the spleen and testis.
Also expressed in the bone marrow, brain, lung, lymph node and
thymus.
-!- DEVELOPMENTAL STAGE: Postnatal expression in the testis is
elevated at the onset of pachytene (day 14).
-!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
subfamily.
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Sequence length: 837
MGIQGLLQFI QEASEPVNVK KYKGQAVAVD TYCWLHKGAI ACAEKLAKGE PTDRYVGFCM
KFVNMLLSYG VKPILIFDGC TLPSKKEVER SRRERRQSNL LKGKQLLREG KVSEARDCFA
RSINITHAMA HKVIKAARAL GVDCLVAPYE ADAQLAYLNK AGIVQAVITE DSDLLAFGCK
KVILKMDQFG NGLEVDQARL GMCKQLGDVF TEEKFRYMCI LSGCDYLASL RGIGLAKACK
VLRLANNPDI VKVIKKIGHY LRMNITVPED YITGFIRANN TFLYQLVFDP IQRKLVPLNA
YGDDVNPETL TYAGQYVGDS VALQIALGNR DVNTFEQIDD YSPDTMPAHS RSHSWNEKAG
QKPPGTNSIW HKNYCPRLEV NSVSHAPQLK EKPSTLGLKQ VISTKGLNLP RKSCVLKRPR
NEALAEDDLL SQYSSVSKKI KENGCGDGTS PNSSKMSKSC PDSGTAHKTD AHTPSKMRNK
FATFLQRRNE ESGAVVVPGT RSRFFCSSQD FDNFIPKKES GQPLNETVAT GKATTSLLGA
LDCPDTEGHK PVDANGTHNL SSQIPGNAAV SPEDEAQSSE TSKLLGAMSP PSLGTLRSCF
SWSGTLREFS RTPSPSASTT LQQFRRKSDP PACLPEASAV VTDRCDSKSE MLGETSQPLH
ELGCSSRSQE SMDSSCGLNT SSLSQPSSRD SGSEESDCNN KSLDNQGEQN SKQHLPHFSK
KDGLRRNKVP GLCRSSSMDS FSTTKIKPLV PARVSGLSKK SGSMQTRKHH DVENKPGLQT
KISELWKNFG FKKDSEKLPS CKKPLSPVKD NIQLTPETED EIFNKPECVR AQRAIFH