XRCC1_ARATH
ID XRCC1_ARATH Reviewed; 353 AA.
AC Q24JK4; F4HS73; Q0WPZ1; Q9FT82; Q9M8L1;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=DNA-repair protein XRCC1 {ECO:0000303|PubMed:11909950};
DE Short=AtXRCC1 {ECO:0000303|PubMed:11909950};
DE AltName: Full=Homolog of X-ray repair cross complementing 1 {ECO:0000303|PubMed:11909950};
GN Name=XRCC1 {ECO:0000303|PubMed:11909950};
GN OrderedLocusNames=At1g80420 {ECO:0000312|Araport:AT1G80420};
GN ORFNames=T21F11.25 {ECO:0000312|EMBL:AAF27125.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:ABD85156.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim J., Kmiec E.;
RT "Cloning and characterization of the gene encoding DNA repair protein XRCC1
RT from Arabidopsis thaliana.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11909950; DOI=10.1128/mcb.22.8.2556-2563.2002;
RA Taylor R.M., Thistlethwaite A., Caldecott K.W.;
RT "Central role for the XRCC1 BRCT I domain in mammalian DNA single-strand
RT break repair.";
RL Mol. Cell. Biol. 22:2556-2563(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ZDP AND ROS1, AND
RP DNA-BINDING.
RC STRAIN=cv. Columbia;
RX PubMed=23316050; DOI=10.1074/jbc.m112.427617;
RA Martinez-Macias M.I., Cordoba-Canero D., Ariza R.R., Roldan-Arjona T.;
RT "The DNA repair protein XRCC1 functions in the plant DNA demethylation
RT pathway by stimulating cytosine methylation (5-meC) excision, gap
RT tailoring, and DNA ligation.";
RL J. Biol. Chem. 288:5496-5505(2013).
CC -!- FUNCTION: Corrects defective DNA strand-break repair and sister
CC chromatid exchange following treatment with ionizing radiation and
CC alkylating agents (By similarity). Involved in DNA demethylation
CC pathway by stimulating cytosine methylation (5-meC) excision, gap
CC tailoring, and DNA ligation. {ECO:0000250|UniProtKB:P18887,
CC ECO:0000269|PubMed:23316050}.
CC -!- SUBUNIT: Homodimer. Interacts with polynucleotide kinase (PNK), DNA
CC polymerase-beta (POLB) and DNA ligase III (LIG3) (By similarity).
CC Interacts with ZDP and ROS1. Binds to various forms of double-stranded
CC DNA (e.g. methylated, unmethylated, with single-nucleotide gap flanked
CC by 3'-phosphate or 5'-phosphate ends). {ECO:0000250|UniProtKB:P18887,
CC ECO:0000269|PubMed:23316050}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18887}.
CC Note=Accumulates at sites of DNA damage.
CC {ECO:0000250|UniProtKB:P18887}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q24JK4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q24JK4-2; Sequence=VSP_057111;
CC -!- DISRUPTION PHENOTYPE: Reduced capacity to complete DNA demethylation
CC initiated by ROS1. {ECO:0000269|PubMed:23316050}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27125.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF324348; AAM08130.1; -; mRNA.
DR EMBL; AJ276506; CAC16136.1; -; mRNA.
DR EMBL; AC018849; AAF27125.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36401.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36402.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36403.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36404.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58866.1; -; Genomic_DNA.
DR EMBL; BT024885; ABD85156.1; -; mRNA.
DR EMBL; AK228919; BAF00808.1; -; mRNA.
DR PIR; A96836; A96836.
DR RefSeq; NP_001077856.1; NM_001084387.2. [Q24JK4-1]
DR RefSeq; NP_001185449.1; NM_001198520.1. [Q24JK4-2]
DR RefSeq; NP_001321272.1; NM_001334987.1. [Q24JK4-1]
DR RefSeq; NP_178158.2; NM_106691.4. [Q24JK4-1]
DR RefSeq; NP_850985.1; NM_180654.3. [Q24JK4-1]
DR AlphaFoldDB; Q24JK4; -.
DR SMR; Q24JK4; -.
DR BioGRID; 29600; 2.
DR STRING; 3702.AT1G80420.1; -.
DR PaxDb; Q24JK4; -.
DR PRIDE; Q24JK4; -.
DR ProteomicsDB; 242494; -. [Q24JK4-1]
DR EnsemblPlants; AT1G80420.1; AT1G80420.1; AT1G80420. [Q24JK4-1]
DR EnsemblPlants; AT1G80420.2; AT1G80420.2; AT1G80420. [Q24JK4-1]
DR EnsemblPlants; AT1G80420.3; AT1G80420.3; AT1G80420. [Q24JK4-1]
DR EnsemblPlants; AT1G80420.4; AT1G80420.4; AT1G80420. [Q24JK4-2]
DR EnsemblPlants; AT1G80420.5; AT1G80420.5; AT1G80420. [Q24JK4-1]
DR GeneID; 844382; -.
DR Gramene; AT1G80420.1; AT1G80420.1; AT1G80420. [Q24JK4-1]
DR Gramene; AT1G80420.2; AT1G80420.2; AT1G80420. [Q24JK4-1]
DR Gramene; AT1G80420.3; AT1G80420.3; AT1G80420. [Q24JK4-1]
DR Gramene; AT1G80420.4; AT1G80420.4; AT1G80420. [Q24JK4-2]
DR Gramene; AT1G80420.5; AT1G80420.5; AT1G80420. [Q24JK4-1]
DR KEGG; ath:AT1G80420; -.
DR Araport; AT1G80420; -.
DR TAIR; locus:2198973; AT1G80420.
DR eggNOG; KOG3226; Eukaryota.
DR HOGENOM; CLU_057218_0_0_1; -.
DR InParanoid; Q24JK4; -.
DR OMA; GKPWRKN; -.
DR OrthoDB; 1220312at2759; -.
DR PhylomeDB; Q24JK4; -.
DR PRO; PR:Q24JK4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q24JK4; baseline and differential.
DR Genevisible; Q24JK4; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:TAIR.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0080111; P:DNA demethylation; IMP:TAIR.
DR GO; GO:0006266; P:DNA ligation; IMP:TAIR.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:TAIR.
DR GO; GO:1901972; P:positive regulation of DNA-5-methylcytosine glycosylase activity; IDA:TAIR.
DR GO; GO:1901969; P:positive regulation of polynucleotide 3'-phosphatase activity; IDA:TAIR.
DR GO; GO:0000012; P:single strand break repair; IEA:InterPro.
DR CDD; cd17725; BRCT_XRCC1_rpt1; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR045080; BRCT_XRCC1_rpt1.
DR Pfam; PF00533; BRCT; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA damage; DNA repair; DNA-binding;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..353
FT /note="DNA-repair protein XRCC1"
FT /id="PRO_0000430949"
FT DOMAIN 58..146
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 266..347
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 240..260
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 166..192
FT /note="REHLSKKPEKQVEKKTETRGTPSTSSK -> SFSYCTASLRCLVDS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:27862469"
FT /id="VSP_057111"
FT CONFLICT 205
FT /note="F -> S (in Ref. 1; AAM08130 and 2; CAC16136)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="Q -> R (in Ref. 6; BAF00808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 39838 MW; 5B47642336AD2BCB CRC64;
MSQKRNLPSW MSSRDPEITP SKSHCKKPKD EGPTEEHNSR NAPSNKSEHA EPSSNTTEFS
KLMEGVVFVL SGFVNPERST LRSQALTMGA TYQPDWNAGS TLLICAFPNT PKFRQVETNG
GTIISKEWIT ECYAQKKLVD IEQYLMHAGK PWRKSSSPQD ANREKREHLS KKPEKQVEKK
TETRGTPSTS SKNRSACNLV KEPFFVTEVK KWARDDLSQT ISWLESQEEK PEPGEIKRIA
AEGVLTCLQD AIDSLEQKQD IGSVTELWSF VPRVVKELGK MESSSKKENS TASKEEVCKQ
AKSWKKIYEA ELAKPGEDES TSRVACGYDS DMTVEMTEEE IELAYRNVSL ECL
