Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5XIX3 (DCR1C_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein artemis

EC=3.1.-.-
Alternative name(s):
DNA cross-link repair 1C protein
SNM1-like protein
Gene names
Name:Dclre1c
Synonyms:Snm1l
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length698 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Subunit structure

Interacts with ATM, BRCA1, PRKDC and TP53BP1. Also exhibits ATM- and phosphorylation-dependent interaction with the MRN complex, composed of MRE11A/MRE11, RAD50, and NBN By similarity.

Subcellular location

Nucleus By similarity.

Post-translational modification

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.

Sequence similarities

Belongs to the DNA repair metallo-beta-lactamase (DRMBL) family.

Sequence caution

The sequence AAM89124.1 differs from that shown. Reason: Frameshift at position 686.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 698698Protein artemis
PRO_0000209125

Amino acid modifications

Modified residue6501Phosphoserine; by ATM By similarity

Experimental info

Sequence conflict6231P → S in AAM89124. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5XIX3 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 28D2F15EAA5ADF85

FASTA69878,189
        10         20         30         40         50         60 
MSSFQGQMEE YPTISIDRFD RENLKARAYF LSHCHKDHMK GLRAPSMKRR LECSLKVFLY 

        70         80         90        100        110        120 
CSPVTKELLL TSPKYKFWEN RIIAIEIETP TQVSLVDEAS GEKEEVVVTL LPAGHCPGSV 

       130        140        150        160        170        180 
MFLFQGSNGT VLYTGDFRLA KGEVSRMELL HSGGRVKDIQ SVYLDTTFCD PRFYQIPSRE 

       190        200        210        220        230        240 
ECLRGVLELV RSWITRSPKH VVWLNCKAAY GYEYLFTNLS EELGVQVHVD KLDMFKNMPD 

       250        260        270        280        290        300 
ILHHLTTDRN TQIHACRHPK AEEYFQWNKL PCGMASKTKT VLHTISIKPS TMWFGERTRK 

       310        320        330        340        350        360 
TNVIVRTGES SYRACFSFHS SYSEIKDFLS YICPVNAYPN VIPIGLTVDK VMDFLKPLCR 

       370        380        390        400        410        420 
SSQCAEPKYK PLGKLKRART VHLDSEEDDD LFDDPLLTHS RRKVPYQVTL HPEVFSMKAL 

       430        440        450        460        470        480 
PLDQPELGQS PGCCKAESMP SPSLANFVDC DESNSDSEGE LETPPSLQGG LGPTTLPQQN 

       490        500        510        520        530        540 
ADPDVDVPRW EVFFKRKDEI TDECLENLPS SIETGGSQSP KRFSDSPKLG SDSDGESTHI 

       550        560        570        580        590        600 
SSQNSSQSTH ITDQGSQGWD SQCDTVLLSS QEKSGGDSTS LNKDTYKPKP KDSISASQIE 

       610        620        630        640        650        660 
QNALCPQDTH CDLKSGAEVN GVPCIEEPDT VSGRKSSPEK TSLTSTQADS QSSSDFEIPS 

       670        680        690 
TPEAELPKPE HLQFLYGKLA TGESIVLKKE NVHSQIFK 

« Hide

References

« Hide 'large scale' references
[1]"The mouse and rat SNM1-like genes, cloning, expression and mapping."
Li L., Zhou Y., Xie G., Cowan M.J.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF395746 mRNA. Translation: AAM89124.1. Frameshift.
BC083546 mRNA. Translation: AAH83546.1.
RefSeqNP_671486.2. NM_147145.2.
UniGeneRn.204346.

3D structure databases

ProteinModelPortalQ5XIX3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000021506.

PTM databases

PhosphoSiteQ5XIX3.

Proteomic databases

PRIDEQ5XIX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000021506; ENSRNOP00000021506; ENSRNOG00000015980.
GeneID259171.
KEGGrno:259171.
UCSCRGD:708574. rat.

Organism-specific databases

CTD64421.
RGD708574. Dclre1c.

Phylogenomic databases

eggNOGCOG1236.
GeneTreeENSGT00530000063183.
HOGENOMHOG000231568.
HOVERGENHBG081421.
InParanoidQ5XIX3.
KOK10887.
OMAMFRNMPD.
OrthoDBEOG70CR8F.
PhylomeDBQ5XIX3.
TreeFamTF329572.

Gene expression databases

GenevestigatorQ5XIX3.

Family and domain databases

Gene3D3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
IPR011084. DRMBL.
[Graphical view]
PfamPF07522. DRMBL. 1 hit.
[Graphical view]
SUPFAMSSF56281. SSF56281. 1 hit.
ProtoNetSearch...

Other

NextBio624222.
PROQ5XIX3.

Entry information

Entry nameDCR1C_RAT
AccessionPrimary (citable) accession number: Q5XIX3
Secondary accession number(s): Q8K4H7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 23, 2004
Last modified: April 16, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families