DCR1C_MOUSE
ID DCR1C_MOUSE Reviewed; 705 AA.
AC Q8K4J0; A2AJG6; A2AJG7; A2AJG8; Q8BG72; Q8BTT1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein artemis {ECO:0000303|PubMed:15699179};
DE Short=mArt {ECO:0000303|PubMed:15699179};
DE EC=3.1.-.-;
DE AltName: Full=DNA cross-link repair 1C protein;
DE AltName: Full=SNM1-like protein;
GN Name=Dclre1c; Synonyms=Art {ECO:0000303|PubMed:15699179}, Snm1l;
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 FUNCTION.
RX PubMed=15699179; DOI=10.4049/jimmunol.174.4.2420;
RA Li L., Salido E., Zhou Y., Bhattacharyya S., Yannone S.M., Dunn E.,
RA Meneses J., Feeney A.J., Cowan M.J.;
RT "Targeted disruption of the Artemis murine counterpart results in SCID and
RT defective V(D)J recombination that is partially corrected with bone marrow
RT transplantation.";
RL J. Immunol. 174:2420-2428(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=NOD; TISSUE=Thymus;
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 [3]
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 [4]
RP FUNCTION.
RX PubMed=12504013; DOI=10.1016/s1097-2765(02)00755-4;
RA Rooney S., Sekiguchi J., Zhu C., Cheng H.-L., Manis J., Whitlow S.,
RA DeVido J., Foy D., Chaudhuri J., Lombard D., Alt F.W.;
RT "Leaky Scid phenotype associated with defective V(D)J coding end processing
RT in Artemis-deficient mice.";
RL Mol. Cell 10:1379-1390(2002).
RN [5]
RP DNA REPAIR METALLO-BETA-LACTAMASE FAMILY.
RX PubMed=12177301; DOI=10.1093/nar/gkf470;
RA Callebaut I., Moshous D., Mornon J.-P., de Villartay J.-P.;
RT "Metallo-beta-lactamase fold within nucleic acids processing enzymes: the
RT beta-CASP family.";
RL Nucleic Acids Res. 30:3592-3601(2002).
RN [6]
RP FUNCTION.
RX PubMed=12615897; DOI=10.1084/jem.20021891;
RA Rooney S., Alt F.W., Lombard D., Whitlow S., Eckersdorff M., Fleming J.,
RA Fugmann S., Ferguson D.O., Schatz D.G., Sekiguchi J.;
RT "Defective DNA repair and increased genomic instability in Artemis-
RT deficient murine cells.";
RL J. Exp. Med. 197:553-565(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-380 AND SER-385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for V(D)J recombination, the process by which exons
CC encoding the antigen-binding domains of immunoglobulins and T-cell
CC receptor proteins are assembled from individual V, (D), and J gene
CC segments. V(D)J recombination is initiated by the lymphoid specific RAG
CC endonuclease complex, which generates site specific DNA double strand
CC breaks (DSBs). These DSBs present two types of DNA end structures:
CC hairpin sealed coding ends and phosphorylated blunt signal ends. These
CC ends are independently repaired by the non homologous end joining
CC (NHEJ) pathway to form coding and signal joints respectively. This
CC protein likely exhibits single-strand specific 5'-3' exonuclease
CC activity in isolation, and may acquire endonucleolytic activity on 5'
CC and 3' hairpins and overhangs when in a complex with PRKDC. The latter
CC activity may be required specifically for the resolution of closed
CC hairpins prior to the formation of the coding joint. May also be
CC required for the repair of complex DSBs induced by ionizing radiation,
CC which require substantial end-processing prior to religation by NHEJ.
CC {ECO:0000269|PubMed:12504013, ECO:0000269|PubMed:12615897,
CC ECO:0000269|PubMed:15699179}.
CC -!- SUBUNIT: Interacts with ATM, BRCA1, PRKDC and TP53BP1. Also exhibits
CC ATM- and phosphorylation-dependent interaction with the MRN complex,
CC composed of MRE11, RAD50, and NBN (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K4J0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K4J0-2; Sequence=VSP_014895, VSP_014896;
CC Name=3;
CC IsoId=Q8K4J0-3; Sequence=VSP_014893, VSP_014894, VSP_014895,
CC VSP_014896;
CC -!- PTM: Phosphorylation on undefined residues by PRKDC may stimulate
CC endonucleolytic activity on 5' and 3' hairpins and overhangs. PRKDC
CC must remain present, even after phosphorylation, for efficient hairpin
CC opening. Also phosphorylated by ATM in response to ionizing radiation
CC (IR) and by ATR in response to ultraviolet (UV) radiation (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
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DR EMBL; AF387731; AAM89119.1; -; mRNA.
DR EMBL; AK037126; BAC29713.1; -; mRNA.
DR EMBL; AK052369; BAC34960.1; -; mRNA.
DR EMBL; AK088810; BAC40586.1; -; mRNA.
DR EMBL; AL732620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15649.1; -. [Q8K4J0-2]
DR CCDS; CCDS15650.1; -. [Q8K4J0-1]
DR CCDS; CCDS79728.1; -. [Q8K4J0-3]
DR RefSeq; NP_001103684.1; NM_001110214.1.
DR RefSeq; NP_001289603.1; NM_001302674.1. [Q8K4J0-3]
DR RefSeq; NP_001289613.1; NM_001302684.1.
DR RefSeq; NP_666226.2; NM_146114.3. [Q8K4J0-1]
DR RefSeq; NP_783614.1; NM_175683.4. [Q8K4J0-2]
DR RefSeq; XP_011237274.1; XM_011238972.2. [Q8K4J0-3]
DR AlphaFoldDB; Q8K4J0; -.
DR SMR; Q8K4J0; -.
DR STRING; 10090.ENSMUSP00000100053; -.
DR iPTMnet; Q8K4J0; -.
DR PhosphoSitePlus; Q8K4J0; -.
DR EPD; Q8K4J0; -.
DR jPOST; Q8K4J0; -.
DR PaxDb; Q8K4J0; -.
DR PRIDE; Q8K4J0; -.
DR ProteomicsDB; 279888; -. [Q8K4J0-1]
DR ProteomicsDB; 279889; -. [Q8K4J0-2]
DR ProteomicsDB; 279890; -. [Q8K4J0-3]
DR Antibodypedia; 24989; 362 antibodies from 34 providers.
DR DNASU; 227525; -.
DR Ensembl; ENSMUST00000061852; ENSMUSP00000054300; ENSMUSG00000026648. [Q8K4J0-2]
DR Ensembl; ENSMUST00000102988; ENSMUSP00000100053; ENSMUSG00000026648. [Q8K4J0-1]
DR Ensembl; ENSMUST00000115066; ENSMUSP00000110718; ENSMUSG00000026648. [Q8K4J0-3]
DR GeneID; 227525; -.
DR KEGG; mmu:227525; -.
DR UCSC; uc008idz.2; mouse. [Q8K4J0-1]
DR UCSC; uc008iea.3; mouse. [Q8K4J0-2]
DR UCSC; uc008ieb.3; mouse. [Q8K4J0-3]
DR CTD; 64421; -.
DR MGI; MGI:2441769; Dclre1c.
DR VEuPathDB; HostDB:ENSMUSG00000026648; -.
DR eggNOG; KOG1361; Eukaryota.
DR GeneTree; ENSGT00940000157779; -.
DR HOGENOM; CLU_029238_0_0_1; -.
DR InParanoid; Q8K4J0; -.
DR OMA; FLFEGCH; -.
DR OrthoDB; 1441774at2759; -.
DR PhylomeDB; Q8K4J0; -.
DR TreeFam; TF329572; -.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR BioGRID-ORCS; 227525; 4 hits in 108 CRISPR screens.
DR ChiTaRS; Dclre1c; mouse.
DR PRO; PR:Q8K4J0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8K4J0; protein.
DR Bgee; ENSMUSG00000026648; Expressed in granulocyte and 93 other tissues.
DR ExpressionAtlas; Q8K4J0; baseline and differential.
DR Genevisible; Q8K4J0; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:MGI.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0006310; P:DNA recombination; IMP:MGI.
DR GO; GO:0006302; P:double-strand break repair; IMP:MGI.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
DR GO; GO:0000723; P:telomere maintenance; IMP:MGI.
DR GO; GO:0033151; P:V(D)J recombination; IMP:MGI.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; DNA damage; DNA recombination;
KW DNA repair; Endonuclease; Exonuclease; Hydrolase; Immunity; Magnesium;
KW Nuclease; Nucleus; Phosphoprotein; Reference proteome; SCID.
FT CHAIN 1..705
FT /note="Protein artemis"
FT /id="PRO_0000209124"
FT REGION 451..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 658
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:Q96SD1"
FT VAR_SEQ 1..130
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014893"
FT VAR_SEQ 131..154
FT /note="VLYTGDFRLAKGEASRMELLHSGG -> MRLRVRRLQTGKRRSFQNGASALW
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014894"
FT VAR_SEQ 503..603
FT /note="GECLEHLPSSIETGGSQSPKLCSDSPKLCSDSPKLCSDSDGDSTHISSQNSS
FT QSTHITDQGSQGWDSQCDTVLLSSQEKSGGDSTSLNKGAYKPKLKESIS -> VDTMIR
FT TPRPRKMKGCGQWSLKMLLQNLEIQEEKHIFENRGWKMAGQVKGSCGLLEGQSSLPTFK
FT LATSLASNSSFWPPWHLHSHAHTQIFTFKKKTKTLL (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014895"
FT VAR_SEQ 604..705
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014896"
FT CONFLICT 103
FT /note="K -> Q (in Ref. 1; AAM89119)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="E -> Q (in Ref. 1; AAM89119)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="V -> G (in Ref. 1; AAM89119)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="A -> P (in Ref. 1; AAM89119)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="G -> R (in Ref. 1; AAM89119)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="M -> V (in Ref. 1; AAM89119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 705 AA; 78834 MW; 7BEA71D61F0B5063 CRC64;
MSSFQGQMAE YPTISIDRFD RENLKARAYF LSHCHKDHMK GLRAPSLKRR LECSLKVFLY
CSPVTKELLL TSPKYRFWEN RIITIEIETP TQISLVDEAS GEKEEVVVTL LPAGHCPGSV
MFLFQGSNGT VLYTGDFRLA KGEASRMELL HSGGRVKDIQ SVYLDTTFCD PRFYQIPSRE
QCLRGILELV RSWVTRSPHH VVWLNCKAAY GYEYLFTNLS EELGVQVHVD KLDMFKNMPD
ILHHLTTDRN TQIHACRHPK AEECFQWNKL PCGITSQNKT ALHTISIKPS TMWFGERTRK
TNVIVRTGES SYRACFSFHS SFSEIKDFLS YICPVNVYPN VIPVGLTVDK VMDVLKPLCR
SPQSVEPKYK PLGKLKRART IHLDSEEDDD LFDDPLPTPL RHKVPYQLTL QPELFSMKAL
PLDQPELRQS PGGCKAESVW SPSLANFIDC EESNSDSGEE LETPPPSLQG GLGPSTLVQQ
NADPDVDIPQ WEVFFKRRDE ITGECLEHLP SSIETGGSQS PKLCSDSPKL CSDSPKLCSD
SDGDSTHISS QNSSQSTHIT DQGSQGWDSQ CDTVLLSSQE KSGGDSTSLN KGAYKPKLKE
SISASQIEQD ALCPQDTHCD LKSRAEVNGA PCLVELDTLS GRKSPPEKTL LSSTRADSQS
SSDFEIPSTP EAELPTPEHL QCLYRKLATG QSIVVEKRKC SLLDS
