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

 DCR1C_RAT               Reviewed;         698 AA.
Q5XIX3; Q8K4H7;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
05-DEC-2018, entry version 104.
RecName: Full=Protein artemis;
EC=3.1.-.-;
AltName: Full=DNA cross-link repair 1C protein;
AltName: Full=SNM1-like protein;
Name=Dclre1c; Synonyms=Snm1l;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Li L., Zhou Y., Xie G., Cowan M.J.;
"The mouse and rat SNM1-like genes, cloning, expression and mapping.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 exhibits single-strand
specific 5'-3' exonuclease activity in isolation, and acquires
endonucleolytic activity on 5' and 3' hairpins and overhangs when
in a complex with PRKDC. The latter activity is 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 (By
similarity). {ECO:0000250}.
-!- 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}.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAM89124.1; Type=Frameshift; Positions=686; Evidence={ECO:0000305};
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EMBL; AF395746; AAM89124.1; ALT_FRAME; mRNA.
EMBL; BC083546; AAH83546.1; -; mRNA.
RefSeq; NP_671486.2; NM_147145.2.
UniGene; Rn.204346; -.
ProteinModelPortal; Q5XIX3; -.
SMR; Q5XIX3; -.
STRING; 10116.ENSRNOP00000021506; -.
iPTMnet; Q5XIX3; -.
PhosphoSitePlus; Q5XIX3; -.
PaxDb; Q5XIX3; -.
PRIDE; Q5XIX3; -.
Ensembl; ENSRNOT00000021506; ENSRNOP00000021506; ENSRNOG00000015980.
GeneID; 259171; -.
KEGG; rno:259171; -.
UCSC; RGD:708574; rat.
CTD; 64421; -.
RGD; 708574; Dclre1c.
eggNOG; KOG1361; Eukaryota.
eggNOG; COG1236; LUCA.
GeneTree; ENSGT00940000157779; -.
HOGENOM; HOG000231568; -.
HOVERGEN; HBG081421; -.
InParanoid; Q5XIX3; -.
KO; K10887; -.
OMA; ICPVNAY; -.
OrthoDB; EOG091G0TAU; -.
PhylomeDB; Q5XIX3; -.
TreeFam; TF329572; -.
Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
PRO; PR:Q5XIX3; -.
Proteomes; UP000002494; Chromosome 17.
Bgee; ENSRNOG00000015980; Expressed in 9 organ(s), highest expression level in spleen.
Genevisible; Q5XIX3; RN.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IEA:Ensembl.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0033151; P:V(D)J recombination; IEA:Ensembl.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR011084; DRMBL.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
Pfam; PF07522; DRMBL; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
Adaptive immunity; Complete proteome; DNA damage; DNA recombination;
DNA repair; Endonuclease; Exonuclease; Hydrolase; Immunity; Magnesium;
Nuclease; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 698 Protein artemis.
/FTId=PRO_0000209125.
MOD_RES 380 380 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8K4J0}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 650 650 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q96SD1}.
CONFLICT 623 623 P -> S (in Ref. 1; AAM89124).
{ECO:0000305}.
SEQUENCE 698 AA; 78189 MW; 28D2F15EAA5ADF85 CRC64;
MSSFQGQMEE YPTISIDRFD RENLKARAYF LSHCHKDHMK GLRAPSMKRR LECSLKVFLY
CSPVTKELLL TSPKYKFWEN RIIAIEIETP TQVSLVDEAS GEKEEVVVTL LPAGHCPGSV
MFLFQGSNGT VLYTGDFRLA KGEVSRMELL HSGGRVKDIQ SVYLDTTFCD PRFYQIPSRE
ECLRGVLELV RSWITRSPKH VVWLNCKAAY GYEYLFTNLS EELGVQVHVD KLDMFKNMPD
ILHHLTTDRN TQIHACRHPK AEEYFQWNKL PCGMASKTKT VLHTISIKPS TMWFGERTRK
TNVIVRTGES SYRACFSFHS SYSEIKDFLS YICPVNAYPN VIPIGLTVDK VMDFLKPLCR
SSQCAEPKYK PLGKLKRART VHLDSEEDDD LFDDPLLTHS RRKVPYQVTL HPEVFSMKAL
PLDQPELGQS PGCCKAESMP SPSLANFVDC DESNSDSEGE LETPPSLQGG LGPTTLPQQN
ADPDVDVPRW EVFFKRKDEI TDECLENLPS SIETGGSQSP KRFSDSPKLG SDSDGESTHI
SSQNSSQSTH ITDQGSQGWD SQCDTVLLSS QEKSGGDSTS LNKDTYKPKP KDSISASQIE
QNALCPQDTH CDLKSGAEVN GVPCIEEPDT VSGRKSSPEK TSLTSTQADS QSSSDFEIPS
TPEAELPKPE HLQFLYGKLA TGESIVLKKE NVHSQIFK


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