XRCC1_RAT
ID XRCC1_RAT Reviewed; 631 AA.
AC Q9ESZ0; Q6IRJ9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=DNA repair protein XRCC1;
DE AltName: Full=X-ray repair cross-complementing protein 1;
GN Name=Xrcc1; Synonyms=Xrcc-1;
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].
RC TISSUE=Brain;
RA Chen D., Cao G., Li M., Zhang Y., Glenn G., Chen J.;
RT "Cloning and characterization of rat Xrcc-1, a DNA repair gene in
RT development and aging of rat.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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-446; THR-452; SER-484 AND
RP THR-487, AND IDENTIFICATION BY 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: Involved in DNA single-strand break repair by mediating the
CC assembly of DNA break repair protein complexes. Probably during DNA
CC repair, negatively regulates ADP-ribose levels by modulating ADP-
CC ribosyltransferase PARP1 activity. {ECO:0000250|UniProtKB:P18887}.
CC -!- SUBUNIT: Homodimer. Interacts with polynucleotide kinase (PNK), DNA
CC polymerase-beta (POLB) and DNA ligase III (LIG3). Interacts with APTX
CC and APLF. Interacts with APEX1; the interaction is induced by SIRT1 and
CC increases with the acetylated form of APEX1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18887}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P18887}. Note=Moves from the nucleoli
CC to the global nuclear chromatin upon DNA damage.
CC {ECO:0000250|UniProtKB:P18887}.
CC -!- PTM: Phosphorylation of Ser-371 causes dimer dissociation.
CC Phosphorylation by CK2 promotes interaction with APTX and APLF (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
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DR EMBL; AF290895; AAG02212.1; -; mRNA.
DR EMBL; BC070894; AAH70894.1; -; mRNA.
DR RefSeq; NP_445887.1; NM_053435.1.
DR AlphaFoldDB; Q9ESZ0; -.
DR SMR; Q9ESZ0; -.
DR STRING; 10116.ENSRNOP00000027057; -.
DR iPTMnet; Q9ESZ0; -.
DR PhosphoSitePlus; Q9ESZ0; -.
DR PaxDb; Q9ESZ0; -.
DR PRIDE; Q9ESZ0; -.
DR Ensembl; ENSRNOT00000027057; ENSRNOP00000027057; ENSRNOG00000019915.
DR GeneID; 84495; -.
DR KEGG; rno:84495; -.
DR UCSC; RGD:619823; rat.
DR CTD; 7515; -.
DR RGD; 619823; Xrcc1.
DR eggNOG; KOG3226; Eukaryota.
DR GeneTree; ENSGT00390000004140; -.
DR HOGENOM; CLU_030026_0_0_1; -.
DR InParanoid; Q9ESZ0; -.
DR OMA; LFFNRDN; -.
DR OrthoDB; 539462at2759; -.
DR PhylomeDB; Q9ESZ0; -.
DR Reactome; R-RNO-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
DR Reactome; R-RNO-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR Reactome; R-RNO-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR PRO; PR:Q9ESZ0; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019915; Expressed in esophagus and 20 other tissues.
DR Genevisible; Q9ESZ0; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
DR GO; GO:0070522; C:ERCC4-ERCC1 complex; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:1990599; F:3' overhang single-stranded DNA endodeoxyribonuclease activity; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0032356; F:oxidized DNA binding; ISO:RGD.
DR GO; GO:0006284; P:base-excision repair; IDA:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:RGD.
DR GO; GO:0021587; P:cerebellum morphogenesis; ISO:RGD.
DR GO; GO:0006281; P:DNA repair; ISO:RGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:1905765; P:negative regulation of protection from non-homologous end joining at telomere; ISO:RGD.
DR GO; GO:0010836; P:negative regulation of protein ADP-ribosylation; ISO:RGD.
DR GO; GO:1904877; P:positive regulation of DNA ligase activity; ISO:RGD.
DR GO; GO:1903518; P:positive regulation of single strand break repair; ISO:RGD.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; ISO:RGD.
DR GO; GO:0033194; P:response to hydroperoxide; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0000012; P:single strand break repair; IEA:InterPro.
DR GO; GO:0061819; P:telomeric DNA-containing double minutes formation; ISO:RGD.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; ISO:RGD.
DR CDD; cd17725; BRCT_XRCC1_rpt1; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR045080; BRCT_XRCC1_rpt1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002706; Xrcc1_N.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF01834; XRCC1_N; 1.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50172; BRCT; 2.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..631
FT /note="DNA repair protein XRCC1"
FT /id="PRO_0000066046"
FT DOMAIN 315..403
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 536..627
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 225..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 371
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 456
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 518
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 522
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT CONFLICT 228
FT /note="S -> L (in Ref. 1; AAG02212)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="K -> S (in Ref. 1; AAG02212)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..270
FT /note="PAP -> AAL (in Ref. 1; AAG02212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 68836 MW; BB5A2FD89E0D0B38 CRC64;
MPEISLRHVV SCSSQDSTHR AENLLKADTY RKWRSAKAGE KTISVVLQLE KEEQIHSVDI
GNDGSAFVEV LVGSSAGGAT AGEQDYEVLL VTSSFMSPSE SRSGSNPNRV RIFGPDKLVR
AAAEKRWDRV KIVCSQPYSK DSPYGLSFVK FHSPPDKDEA EAPSQKVTVT KLGQFRVKEE
DDSANSLRPG ALFFNRINKA ASASASDPAG PSYAAATLQA SSAASSASPV PKVGGSSSKL
QEPPKGKRKL DLGLEDKKPP SKPSAGPPAP KRPKLPVPSR TPAATPASTP AQKAVPGKPR
GEGTEPRGAR AGPQELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR PDWTPDSTHL
ICAFANTPKY SQVLGLGGRI VRKEWVLDCY RMRRRLPSRR YLMAGLGSSS EDEGDSHSES
GEDEAPKLPR KRPQPKAKTQ AAGPSSPPRP PTPEETKAPS PGPQDNSDTD GEQSEGRDNG
AEDSGDTEDE LRRVAKQREQ RQPPAPEENG EDPYAGSTDE NTDSEAPSEA DLPIPELPDF
FQGKHFFLYG EFPGDERRKL IRYVTAFNGE LEDYMSDRVQ FVITAQEWDP NFEEALMENP
SLAFVRPRWI YSCNEKQKLL PHQLYGVVPQ A
