RAD1_MOUSE
ID RAD1_MOUSE Reviewed; 280 AA.
AC Q9QWZ1; O70452; O88391; Q3TGU1; Q3UG66; Q9QWZ3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cell cycle checkpoint protein RAD1;
DE Short=mRAD1;
DE EC=3.1.11.2;
DE AltName: Full=DNA repair exonuclease rad1 homolog;
DE AltName: Full=Rad1-like DNA damage checkpoint protein;
GN Name=Rad1; Synonyms=Rec1;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9716408; DOI=10.1101/gad.12.16.2560;
RA Freire R., Murguia J.R., Tarsounas M., Lowndes N.F., Moens P.B.,
RA Jackson S.P.;
RT "Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and
RT Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian
RT meiosis.";
RL Genes Dev. 12:2560-2573(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9828137; DOI=10.1006/geno.1998.5582;
RA Bluyssen H.A.R., van Os R.I., Naus N.C., Jaspers I., Hoeijmakers J.H.J.,
RA de Klein A.;
RT "A human and mouse homolog of the Schizosaccharomyces pombe rad1+ cell
RT cycle checkpoint control gene.";
RL Genomics 54:331-337(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9660799; DOI=10.1074/jbc.273.29.18332;
RA Parker A.E., Van de Weyer I., Laus M.C., Oostveen I., Yon J.,
RA Verhasselt P., Luyten W.H.M.L.;
RT "A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene
RT encodes an exonuclease.";
RL J. Biol. Chem. 273:18332-18339(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9705507; DOI=10.1093/nar/26.17.3971;
RA Udell C.M., Lee S.K., Davey S.;
RT "HRAD1 and MRad1 encode mammalian homologues of the fission yeast rad1+
RT cell cycle checkpoint control gene.";
RL Nucleic Acids Res. 26:3971-3976(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hao L., Chang M., Liu J., Chen L.B.;
RT "Identification and cloning of Hrad1, a human homolog of the
RT SchizosaCCharomyces pombe checkpoint protein.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Shannon M.E., Naureckiene S., Stubbs L., Holloman W.K., Thelen M.P.;
RT "Mammalian REC1, encoding a 3'-5' exonuclease, is differentially expressed
RT during meiosis.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Fetal kidney, and Heart;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Limb;
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).
CC -!- FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex
CC that plays a major role in DNA repair. The 9-1-1 complex is recruited
CC to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp
CC loader complex. Acts then as a sliding clamp platform on DNA for
CC several proteins involved in long-patch base excision repair (LP-BER).
CC The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by
CC increasing its affinity for the 3'-OH end of the primer-template and
CC stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1
CC cleavage activity on substrates with double, nick, or gap flaps of
CC distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch
CC base excision repair substrates. The 9-1-1 complex is necessary for the
CC recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring
CC during the S phase. Isoform 1 possesses 3'->5' double stranded DNA
CC exonuclease activity (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex,
CC composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with
CC LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex
CC associates with the RAD17-RFC complex. RAD1 interacts with POLB, FEN1,
CC HUS1, HUS1B, RAD9A and RAD9B. Interacts with DNAJC7 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QWZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QWZ1-2; Sequence=VSP_017337;
CC -!- TISSUE SPECIFICITY: Expressed in testis, uterus, bladder, spleen,
CC ovaries, lung, brain and muscle (at protein level). Expressed in brain,
CC testis, kidney, heart, liver and lung. {ECO:0000269|PubMed:9660799,
CC ECO:0000269|PubMed:9716408, ECO:0000269|PubMed:9828137}.
CC -!- SIMILARITY: Belongs to the rad1 family. {ECO:0000305}.
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DR EMBL; AF074718; AAC98094.1; -; mRNA.
DR EMBL; AF073523; AAC95465.1; -; mRNA.
DR EMBL; AF076842; AAC95524.1; -; mRNA.
DR EMBL; AJ004976; CAA06250.1; -; mRNA.
DR EMBL; AF038841; AAC27248.1; -; mRNA.
DR EMBL; AF058394; AAC14139.1; -; mRNA.
DR EMBL; AF084514; AAC35551.1; -; mRNA.
DR EMBL; AK146533; BAE27240.1; -; mRNA.
DR EMBL; AK148098; BAE28343.1; -; mRNA.
DR EMBL; AK150466; BAE29583.1; -; mRNA.
DR EMBL; AK168588; BAE40457.1; -; mRNA.
DR EMBL; BC048693; AAH48693.1; -; mRNA.
DR CCDS; CCDS27379.1; -. [Q9QWZ1-1]
DR CCDS; CCDS70618.1; -. [Q9QWZ1-2]
DR RefSeq; NP_001276376.1; NM_001289447.1. [Q9QWZ1-1]
DR RefSeq; NP_001276377.1; NM_001289448.1. [Q9QWZ1-2]
DR RefSeq; NP_035362.2; NM_011232.3. [Q9QWZ1-1]
DR AlphaFoldDB; Q9QWZ1; -.
DR SMR; Q9QWZ1; -.
DR STRING; 10090.ENSMUSP00000022856; -.
DR iPTMnet; Q9QWZ1; -.
DR PhosphoSitePlus; Q9QWZ1; -.
DR EPD; Q9QWZ1; -.
DR MaxQB; Q9QWZ1; -.
DR PaxDb; Q9QWZ1; -.
DR PeptideAtlas; Q9QWZ1; -.
DR PRIDE; Q9QWZ1; -.
DR ProteomicsDB; 255022; -. [Q9QWZ1-1]
DR ProteomicsDB; 255023; -. [Q9QWZ1-2]
DR Antibodypedia; 10031; 358 antibodies from 33 providers.
DR DNASU; 19355; -.
DR Ensembl; ENSMUST00000022856; ENSMUSP00000022856; ENSMUSG00000022248. [Q9QWZ1-1]
DR Ensembl; ENSMUST00000100775; ENSMUSP00000098338; ENSMUSG00000022248. [Q9QWZ1-2]
DR GeneID; 19355; -.
DR KEGG; mmu:19355; -.
DR UCSC; uc007vgh.2; mouse. [Q9QWZ1-1]
DR UCSC; uc033gtc.1; mouse. [Q9QWZ1-2]
DR CTD; 5810; -.
DR MGI; MGI:1316678; Rad1.
DR VEuPathDB; HostDB:ENSMUSG00000022248; -.
DR eggNOG; KOG3194; Eukaryota.
DR GeneTree; ENSGT00500000044913; -.
DR HOGENOM; CLU_035332_2_0_1; -.
DR InParanoid; Q9QWZ1; -.
DR OMA; QITMSPE; -.
DR OrthoDB; 1440961at2759; -.
DR PhylomeDB; Q9QWZ1; -.
DR TreeFam; TF101211; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 19355; 27 hits in 110 CRISPR screens.
DR ChiTaRS; Rad1; mouse.
DR PRO; PR:Q9QWZ1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9QWZ1; protein.
DR Bgee; ENSMUSG00000022248; Expressed in epiblast (generic) and 241 other tissues.
DR ExpressionAtlas; Q9QWZ1; baseline and differential.
DR Genevisible; Q9QWZ1; MM.
DR GO; GO:0030896; C:checkpoint clamp complex; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; ISO:MGI.
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 Alternative splicing; DNA damage; DNA repair; Exonuclease; Hydrolase;
KW Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..280
FT /note="Cell cycle checkpoint protein RAD1"
FT /id="PRO_0000225006"
FT VAR_SEQ 223..280
FT /note="YKLSLLKPSTKALALSCKVSIRTDNRGFLSLQYMIRNEDGQICFVEYYCCPD
FT EEVPES -> ISDVKYSCKTWLQLPEGVGYDPLSGLEWTLSERDGEQEVAQWVNVVPVQ
FT A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017337"
FT CONFLICT 28
FT /note="S -> F (in Ref. 3, 4, 6 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="Q -> E (in Ref. 8; BAE28343)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="P -> T (in Ref. 8; BAE40457)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="N -> S (in Ref. 2; AAC95465)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="D -> N (in Ref. 5; AAC27248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 31610 MW; F9D6ED292C5D4361 CRC64;
MPLLTQYNEE EYEQYCLVAS LDNVRNLSTV LKAIHFREHA TCFATKNGIK VTVENAKCVQ
ANAFIQADVF QEFVIQEESV TFRINLTILL DCLSIFGSSP TPGTLTALRM CYQGYGHPLM
LFLEEGGVVT VCKITTQEPE ETLDFDFCST NVMNKIILQS EGLREAFSEL DMTGDVLQIT
VSPDKPYFRL STFGNAGNSH LDYPKDSDLV EAFHCDKTQV NRYKLSLLKP STKALALSCK
VSIRTDNRGF LSLQYMIRNE DGQICFVEYY CCPDEEVPES
