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Protein artemis (mArt) (EC 3.1.-.-) (DNA cross-link repair 1C protein) (SNM1-like protein)

 DCR1C_MOUSE             Reviewed;         705 AA.
Q8K4J0; A2AJG6; A2AJG7; A2AJG8; Q8BG72; Q8BTT1;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 2.
25-OCT-2017, entry version 110.
RecName: Full=Protein artemis;
Short=mArt;
EC=3.1.-.-;
AltName: Full=DNA cross-link repair 1C protein;
AltName: Full=SNM1-like protein;
Name=Dclre1c; Synonyms=Art, Snm1l;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=15699179; DOI=10.4049/jimmunol.174.4.2420;
Li L., Salido E., Zhou Y., Bhattacharyya S., Yannone S.M., Dunn E.,
Meneses J., Feeney A.J., Cowan M.J.;
"Targeted disruption of the Artemis murine counterpart results in SCID
and defective V(D)J recombination that is partially corrected with
bone marrow transplantation.";
J. Immunol. 174:2420-2428(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
FUNCTION.
PubMed=12504013; DOI=10.1016/S1097-2765(02)00755-4;
Rooney S., Sekiguchi J., Zhu C., Cheng H.-L., Manis J., Whitlow S.,
DeVido J., Foy D., Chaudhuri J., Lombard D., Alt F.W.;
"Leaky Scid phenotype associated with defective V(D)J coding end
processing in Artemis-deficient mice.";
Mol. Cell 10:1379-1390(2002).
[5]
DNA REPAIR METALLO-BETA-LACTAMASE FAMILY.
PubMed=12177301; DOI=10.1093/nar/gkf470;
Callebaut I., Moshous D., Mornon J.-P., de Villartay J.-P.;
"Metallo-beta-lactamase fold within nucleic acids processing enzymes:
the beta-CASP family.";
Nucleic Acids Res. 30:3592-3601(2002).
[6]
FUNCTION.
PubMed=12615897; DOI=10.1084/jem.20021891;
Rooney S., Alt F.W., Lombard D., Whitlow S., Eckersdorff M.,
Fleming J., Fugmann S., Ferguson D.O., Schatz D.G., Sekiguchi J.;
"Defective DNA repair and increased genomic instability in Artemis-
deficient murine cells.";
J. Exp. Med. 197:553-565(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-380 AND SER-385, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Required for V(D)J recombination, the process by which
exons encoding the antigen-binding domains of immunoglobulins and
T-cell receptor proteins are assembled from individual V, (D), and
J gene segments. V(D)J recombination is initiated by the lymphoid
specific RAG endonuclease complex, which generates site specific
DNA double strand breaks (DSBs). These DSBs present two types of
DNA end structures: hairpin sealed coding ends and phosphorylated
blunt signal ends. These ends are independently repaired by the
non homologous end joining (NHEJ) pathway to form coding and
signal joints respectively. This protein likely exhibits single-
strand specific 5'-3' exonuclease activity in isolation, and may
acquire endonucleolytic activity on 5' and 3' hairpins and
overhangs when in a complex with PRKDC. The latter activity may be
required specifically for the resolution of closed hairpins prior
to the formation of the coding joint. May also be required for the
repair of complex DSBs induced by ionizing radiation, which
require substantial end-processing prior to religation by NHEJ.
{ECO:0000269|PubMed:12504013, ECO:0000269|PubMed:12615897,
ECO:0000269|PubMed:15699179}.
-!- SUBUNIT: Interacts with ATM, BRCA1, PRKDC and TP53BP1. Also
exhibits ATM- and phosphorylation-dependent interaction with the
MRN complex, composed of MRE11, RAD50, and NBN (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8K4J0-1; Sequence=Displayed;
Name=2;
IsoId=Q8K4J0-2; Sequence=VSP_014895, VSP_014896;
Note=May be due to an intron retention. No experimental
confirmation available.;
Name=3;
IsoId=Q8K4J0-3; Sequence=VSP_014893, VSP_014894, VSP_014895,
VSP_014896;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation on undefined residues by PRKDC may stimulate
endonucleolytic activity on 5' and 3' hairpins and overhangs.
PRKDC must remain present, even after phosphorylation, for
efficient hairpin opening. Also phosphorylated by ATM in response
to ionizing radiation (IR) and by ATR in response to ultraviolet
(UV) radiation (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase
(DRMBL) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF387731; AAM89119.1; -; mRNA.
EMBL; AK037126; BAC29713.1; -; mRNA.
EMBL; AK052369; BAC34960.1; -; mRNA.
EMBL; AK088810; BAC40586.1; -; mRNA.
EMBL; AL732620; CAM16038.1; -; Genomic_DNA.
EMBL; AL732620; CAM16039.1; -; Genomic_DNA.
EMBL; AL732620; CAM16040.1; -; Genomic_DNA.
CCDS; CCDS15649.1; -. [Q8K4J0-2]
CCDS; CCDS15650.1; -. [Q8K4J0-1]
CCDS; CCDS79728.1; -. [Q8K4J0-3]
RefSeq; NP_001103684.1; NM_001110214.1.
RefSeq; NP_001289603.1; NM_001302674.1. [Q8K4J0-3]
RefSeq; NP_001289613.1; NM_001302684.1.
RefSeq; NP_666226.2; NM_146114.3. [Q8K4J0-1]
RefSeq; NP_783614.1; NM_175683.4. [Q8K4J0-2]
RefSeq; XP_011237274.1; XM_011238972.2. [Q8K4J0-3]
UniGene; Mm.23483; -.
UniGene; Mm.413860; -.
UniGene; Mm.442710; -.
ProteinModelPortal; Q8K4J0; -.
SMR; Q8K4J0; -.
STRING; 10090.ENSMUSP00000100053; -.
iPTMnet; Q8K4J0; -.
PhosphoSitePlus; Q8K4J0; -.
PaxDb; Q8K4J0; -.
PRIDE; Q8K4J0; -.
Ensembl; ENSMUST00000061852; ENSMUSP00000054300; ENSMUSG00000026648. [Q8K4J0-2]
Ensembl; ENSMUST00000102988; ENSMUSP00000100053; ENSMUSG00000026648. [Q8K4J0-1]
Ensembl; ENSMUST00000115066; ENSMUSP00000110718; ENSMUSG00000026648. [Q8K4J0-3]
GeneID; 227525; -.
KEGG; mmu:227525; -.
UCSC; uc008idz.2; mouse. [Q8K4J0-1]
UCSC; uc008iea.3; mouse. [Q8K4J0-2]
UCSC; uc008ieb.3; mouse. [Q8K4J0-3]
CTD; 64421; -.
MGI; MGI:2441769; Dclre1c.
eggNOG; KOG1361; Eukaryota.
eggNOG; COG1236; LUCA.
GeneTree; ENSGT00530000063183; -.
HOGENOM; HOG000231568; -.
HOVERGEN; HBG081421; -.
InParanoid; Q8K4J0; -.
KO; K10887; -.
OMA; DKLDMFR; -.
OrthoDB; EOG091G0TAU; -.
PhylomeDB; Q8K4J0; -.
TreeFam; TF329572; -.
Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
PRO; PR:Q8K4J0; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026648; -.
ExpressionAtlas; Q8K4J0; baseline and differential.
Genevisible; Q8K4J0; MM.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IC:MGI.
GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
GO; GO:0008409; F:5'-3' exonuclease activity; ISO:MGI.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISO:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IMP:MGI.
GO; GO:0051276; P:chromosome organization; IMP:MGI.
GO; GO:0006310; P:DNA recombination; IMP:MGI.
GO; GO:0006302; P:double-strand break repair; IMP:MGI.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
GO; GO:0000723; P:telomere maintenance; IMP:MGI.
GO; GO:0033151; P:V(D)J recombination; IMP:MGI.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR011084; DRMBL.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; Metallo-hydrolase/OxRdtase.
Pfam; PF07522; DRMBL; 1.
Pfam; PF12706; Lactamase_B_2; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; Complete proteome;
DNA damage; DNA recombination; DNA repair; Endonuclease; Exonuclease;
Hydrolase; Immunity; Magnesium; Nuclease; Nucleus; Phosphoprotein;
Reference proteome; SCID.
CHAIN 1 705 Protein artemis.
/FTId=PRO_0000209124.
MOD_RES 380 380 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 658 658 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q96SD1}.
VAR_SEQ 1 130 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_014893.
VAR_SEQ 131 154 VLYTGDFRLAKGEASRMELLHSGG -> MRLRVRRLQTGKR
RSFQNGASALW (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_014894.
VAR_SEQ 503 603 GECLEHLPSSIETGGSQSPKLCSDSPKLCSDSPKLCSDSDG
DSTHISSQNSSQSTHITDQGSQGWDSQCDTVLLSSQEKSGG
DSTSLNKGAYKPKLKESIS -> VDTMIRTPRPRKMKGCGQ
WSLKMLLQNLEIQEEKHIFENRGWKMAGQVKGSCGLLEGQS
SLPTFKLATSLASNSSFWPPWHLHSHAHTQIFTFKKKTKTL
L (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_014895.
VAR_SEQ 604 705 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_014896.
CONFLICT 103 103 K -> Q (in Ref. 1; AAM89119).
{ECO:0000305}.
CONFLICT 105 105 E -> Q (in Ref. 1; AAM89119).
{ECO:0000305}.
CONFLICT 107 107 V -> G (in Ref. 1; AAM89119).
{ECO:0000305}.
CONFLICT 113 113 A -> P (in Ref. 1; AAM89119).
{ECO:0000305}.
CONFLICT 118 118 G -> R (in Ref. 1; AAM89119).
{ECO:0000305}.
CONFLICT 121 121 M -> V (in Ref. 1; AAM89119).
{ECO:0000305}.
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


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