MRT2_CAEEL
ID MRT2_CAEEL Reviewed; 267 AA.
AC G5EC44;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Cell cycle checkpoint protein RAD1 homolog mrt-2 {ECO:0000305};
DE EC=3.1.11.2 {ECO:0000250|UniProtKB:O60671};
GN Name=mrt-2 {ECO:0000312|WormBase:Y41C4A.14};
GN Synonyms=hpr-1 {ECO:0000312|WormBase:Y41C4A.14};
GN ORFNames=Y41C4A.14 {ECO:0000312|WormBase:Y41C4A.14};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAC95525.1};
RN [1] {ECO:0000312|EMBL:AAC95525.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9878245; DOI=10.1006/geno.1998.5587;
RA Dean F.B., Lian L., O'Donnell M.;
RT "cDNA cloning and gene mapping of human homologs for Schizosaccharomyces
RT pombe rad17, rad1, and hus1 and cloning of homologs from mouse,
RT Caenorhabditis elegans, and Drosophila melanogaster.";
RL Genomics 54:424-436(1998).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=10882129; DOI=10.1016/s1097-2765(00)80438-4;
RA Gartner A., Milstein S., Ahmed S., Hodgkin J., Hengartner M.O.;
RT "A conserved checkpoint pathway mediates DNA damage-induced apoptosis and
RT cell cycle arrest in C. elegans.";
RL Mol. Cell 5:435-443(2000).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=10646593; DOI=10.1038/35003120;
RA Ahmed S., Hodgkin J.;
RT "MRT-2 checkpoint protein is required for germline immortality and telomere
RT replication in C. elegans.";
RL Nature 403:159-164(2000).
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE 9-1-1 COMPLEX, INTERACTION WITH HUS-1, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12445383; DOI=10.1016/s0960-9822(02)01262-9;
RA Hofmann E.R., Milstein S., Boulton S.J., Ye M., Hofmann J.J., Stergiou L.,
RA Gartner A., Vidal M., Hengartner M.O.;
RT "Caenorhabditis elegans HUS-1 is a DNA damage checkpoint protein required
RT for genome stability and EGL-1-mediated apoptosis.";
RL Curr. Biol. 12:1908-1918(2002).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=16951081; DOI=10.1534/genetics.106.058701;
RA Harris J., Lowden M., Clejan I., Tzoneva M., Thomas J.H., Hodgkin J.,
RA Ahmed S.;
RT "Mutator phenotype of Caenorhabditis elegans DNA damage checkpoint
RT mutants.";
RL Genetics 174:601-616(2006).
RN [7]
RP FUNCTION.
RX PubMed=22547822; DOI=10.1073/pnas.1119191109;
RA Cheng C., Shtessel L., Brady M.M., Ahmed S.;
RT "Caenorhabditis elegans POT-2 telomere protein represses a mode of
RT alternative lengthening of telomeres with normal telomere lengths.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7805-7810(2012).
CC -!- FUNCTION: May be a component of the 9-1-1 cell-cycle checkpoint
CC response complex that plays a major role in DNA repair
CC (PubMed:12445383, PubMed:16951081). Promotes DNA double strand break-
CC induced cell cycle arrest and apoptosis, thereby playing a role in
CC genome stability (PubMed:10882129, PubMed:10646593, PubMed:16951081).
CC Also required for telomere length maintenance and germline immortality
CC (PubMed:10646593, PubMed:16951081, PubMed:22547822). May possess 3'->5'
CC double stranded DNA exonuclease activity (By similarity).
CC {ECO:0000250|UniProtKB:O60671, ECO:0000269|PubMed:10646593,
CC ECO:0000269|PubMed:10882129, ECO:0000269|PubMed:12445383,
CC ECO:0000269|PubMed:16951081, ECO:0000269|PubMed:22547822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.2;
CC Evidence={ECO:0000250|UniProtKB:O60671};
CC -!- SUBUNIT: Probable component of the toroidal 9-1-1 (RAD9-RAD1-HUS1)
CC complex, composed of hpr-9, mrt-2 and hus-1 (PubMed:12445383).
CC Interacts with hus-1 (PubMed:12445383). Might associate with hpr-9
CC (Probable). {ECO:0000269|PubMed:12445383, ECO:0000305|PubMed:12445383}.
CC -!- INTERACTION:
CC G5EC44; G5EFI9: hus-1; NbExp=8; IntAct=EBI-323732, EBI-323706;
CC G5EC44; O02115: pcn-1; NbExp=3; IntAct=EBI-323732, EBI-318162;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown disrupts hus-1
CC localization to the nucleus. {ECO:0000269|PubMed:12445383}.
CC -!- SIMILARITY: Belongs to the Rad1 family. {ECO:0000305}.
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DR EMBL; AF076843; AAC95525.1; -; mRNA.
DR EMBL; BX284603; CAB63359.2; -; Genomic_DNA.
DR PIR; T43313; T43313.
DR RefSeq; NP_499521.1; NM_067120.4.
DR AlphaFoldDB; G5EC44; -.
DR SMR; G5EC44; -.
DR ComplexPortal; CPX-1615; Checkpoint clamp complex.
DR IntAct; G5EC44; 27.
DR MINT; G5EC44; -.
DR STRING; 6239.Y41C4A.14; -.
DR EPD; G5EC44; -.
DR PaxDb; G5EC44; -.
DR EnsemblMetazoa; Y41C4A.14.1; Y41C4A.14.1; WBGene00003417.
DR EnsemblMetazoa; Y41C4A.14.2; Y41C4A.14.2; WBGene00003417.
DR GeneID; 176608; -.
DR KEGG; cel:CELE_Y41C4A.14; -.
DR CTD; 176608; -.
DR WormBase; Y41C4A.14; CE29376; WBGene00003417; mrt-2.
DR eggNOG; KOG3194; Eukaryota.
DR GeneTree; ENSGT00500000044913; -.
DR HOGENOM; CLU_035332_2_1_1; -.
DR InParanoid; G5EC44; -.
DR OMA; QITMSPE; -.
DR OrthoDB; 1440961at2759; -.
DR PhylomeDB; G5EC44; -.
DR Reactome; R-CEL-176187; Activation of ATR in response to replication stress.
DR SignaLink; G5EC44; -.
DR PRO; PR:G5EC44; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003417; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030896; C:checkpoint clamp complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:WormBase.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; ISS:WormBase.
DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:WormBase.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:WormBase.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:WormBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:WormBase.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:WormBase.
DR InterPro; IPR003011; Cell_cycle_checkpoint_Rad1.
DR InterPro; IPR003021; Rad1_Rec1_Rad17.
DR PANTHER; PTHR10870; PTHR10870; 1.
DR Pfam; PF02144; Rad1; 1.
DR PRINTS; PR01245; RAD1REC1.
DR PRINTS; PR01246; RAD1REPAIR.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease; Nucleus;
KW Reference proteome.
FT CHAIN 1..267
FT /note="Cell cycle checkpoint protein RAD1 homolog mrt-2"
FT /id="PRO_0000441108"
SQ SEQUENCE 267 AA; 29910 MW; 2150B948D1FAD287 CRC64;
MMELETGQCT IMELKKENVK ELAQVFKTVA FKDTGTWHAS EAGMKITVDD GSYQLASVFI
NPAFFSSFKV REEIVSMKIS IKSISEFLSI SENSSSSVKV SYPGMFQPVK MLVEDADGWV
ARGNFTTTLA DQELDFEFDD AGVLATYLLK TQVLKEIIKD FDDTSRTVRI QFTKNSLCFT
TFGDVGETTV SIPSRSLQME SVKCLEEVEF SYLLSLIQRM TTAFILATKL ILRVDERGVL
SCQFSIDHGE GNASYIEFLT VPADEEE
