DCR1C_RAT
ID DCR1C_RAT Reviewed; 698 AA.
AC Q5XIX3; Q8K4H7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein artemis;
DE EC=3.1.-.-;
DE AltName: Full=DNA cross-link repair 1C protein;
DE AltName: Full=SNM1-like protein;
GN Name=Dclre1c; Synonyms=Snm1l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li L., Zhou Y., Xie G., Cowan M.J.;
RT "The mouse and rat SNM1-like genes, cloning, expression and mapping.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 exhibits single-strand specific 5'-3' exonuclease activity in
CC isolation, and acquires endonucleolytic activity on 5' and 3' hairpins
CC and overhangs when in a complex with PRKDC. The latter activity is
CC required specifically for the resolution of closed hairpins prior to
CC the formation of the coding joint. May also be required for the repair
CC of complex DSBs induced by ionizing radiation, which require
CC substantial end-processing prior to religation by NHEJ (By similarity).
CC {ECO:0000250}.
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 -!- 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 -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM89124.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF395746; AAM89124.1; ALT_FRAME; mRNA.
DR EMBL; BC083546; AAH83546.1; -; mRNA.
DR RefSeq; NP_671486.2; NM_147145.2.
DR AlphaFoldDB; Q5XIX3; -.
DR SMR; Q5XIX3; -.
DR STRING; 10116.ENSRNOP00000021506; -.
DR iPTMnet; Q5XIX3; -.
DR PhosphoSitePlus; Q5XIX3; -.
DR PaxDb; Q5XIX3; -.
DR PRIDE; Q5XIX3; -.
DR GeneID; 259171; -.
DR KEGG; rno:259171; -.
DR UCSC; RGD:708574; rat.
DR CTD; 64421; -.
DR RGD; 708574; Dclre1c.
DR VEuPathDB; HostDB:ENSRNOG00000015980; -.
DR eggNOG; KOG1361; Eukaryota.
DR HOGENOM; CLU_029238_0_0_1; -.
DR InParanoid; Q5XIX3; -.
DR OMA; FLFEGCH; -.
DR OrthoDB; 1441774at2759; -.
DR PhylomeDB; Q5XIX3; -.
DR TreeFam; TF329572; -.
DR Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
DR PRO; PR:Q5XIX3; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000015980; Expressed in thymus and 19 other tissues.
DR Genevisible; Q5XIX3; RN.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISO:RGD.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISO:RGD.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR GO; GO:0051276; P:chromosome organization; ISO:RGD.
DR GO; GO:0006310; P:DNA recombination; ISO:RGD.
DR GO; GO:0006302; P:double-strand break repair; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0000723; P:telomere maintenance; ISO:RGD.
DR GO; GO:0033151; P:V(D)J recombination; ISO:RGD.
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; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW Exonuclease; Hydrolase; Immunity; Magnesium; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..698
FT /note="Protein artemis"
FT /id="PRO_0000209125"
FT REGION 445..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 380
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4J0"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 650
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:Q96SD1"
FT CONFLICT 623
FT /note="P -> S (in Ref. 1; AAM89124)"
FT /evidence="ECO:0000305"
SQ 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
