DCR1C_PONAB
ID DCR1C_PONAB Reviewed; 692 AA.
AC Q5R6Z9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Protein artemis;
DE EC=3.1.-.-;
DE AltName: Full=DNA cross-link repair 1C protein;
GN Name=DCLRE1C;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CR860324; CAH92461.1; -; mRNA.
DR RefSeq; NP_001126451.1; NM_001132979.1.
DR AlphaFoldDB; Q5R6Z9; -.
DR SMR; Q5R6Z9; -.
DR STRING; 9601.ENSPPYP00000002445; -.
DR PRIDE; Q5R6Z9; -.
DR GeneID; 100173437; -.
DR KEGG; pon:100173437; -.
DR CTD; 64421; -.
DR eggNOG; KOG1361; Eukaryota.
DR InParanoid; Q5R6Z9; -.
DR OrthoDB; 1441774at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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..692
FT /note="Protein artemis"
FT /id="PRO_0000209123"
FT REGION 503..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
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:0000250|UniProtKB:Q8K4J0"
FT MOD_RES 645
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:Q96SD1"
SQ SEQUENCE 692 AA; 78624 MW; 46176FD31BE1C657 CRC64;
MSSFEGQMAE YPTISIDRFD RENLRARAYF LSHCHKDHMK GLRAPTLKRR LECSLKVYLY
CSPVTKELLL TSPKYRFWKK RIISIEIETP TQISLVDEAS GEKEEIVVTL LPAGHCPGSV
MFLFQGNNGT VLYTGDFRLA QGEAARMELL HSGGRIKDIQ SVYLDTTFCD PRFYQIPSRE
ECLSGILELV RSWITRSPYH VVWLNCKAAY GYEYLFTNLS EELGVQVHVN KLDMFRNMPE
ILHHLTTDRN TQIHACRHPK AEEYFQWSKL PCGITSRNRI PLHIISIKPS TMWFGERSRK
TNVIVRTGES SYRACFSFHS SYSEIKDFLS YLCPVNAYPN VIPVGTTMDK VVEILKPLCR
SSQSMEPKYK PLGKLKRART VHRDSEEEDD YLFDDPLPIP LRHKVPYQET LHPEVFSMTV
VSEKQPEKLR QTPGCCRAES MQSSRFTNFV DCEESNSESE EEVGIPASLQ GDLGSVLHLQ
KADGDVPQWK VFFKRNDEIT DERLENFPSS TEAGGSQSPK LFSDSDGEST HISSQNSSQS
THITEQGSQG WDSQSDTVLL SSQERNSGDI TSLDKVDYRP TIKENIPASL MEQNVICPKH
TYSDLKSRDQ DVTVVPSTGE PTTLSSETHI PEEKSLLNLS TNADSQSSSD FEVPSTPEAE
LPKREHLQYL YEKLATGESI AVKKRKCSLS DI
