GenomeNet

Database: UniProt
Entry: M3W3P2_FELCA
LinkDB: M3W3P2_FELCA
Original site: M3W3P2_FELCA 
ID   M3W3P2_FELCA            Unreviewed;       631 AA.
AC   M3W3P2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=X-ray repair cross complementing 1 {ECO:0000313|Ensembl:ENSFCAP00000004841.4};
GN   Name=XRCC1 {ECO:0000313|Ensembl:ENSFCAP00000004841.4,
GN   ECO:0000313|VGNC:VGNC:97689};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000004841.4, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000004841.4, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004841.4,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000004841.4, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004841.4,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000004841.4}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004841.4};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AANG04000747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003997757.1; XM_003997708.4.
DR   AlphaFoldDB; M3W3P2; -.
DR   STRING; 9685.ENSFCAP00000004841; -.
DR   PaxDb; 9685-ENSFCAP00000004841; -.
DR   Ensembl; ENSFCAT00000005223.6; ENSFCAP00000004841.4; ENSFCAG00000005222.6.
DR   GeneID; 101091917; -.
DR   KEGG; fca:101091917; -.
DR   CTD; 7515; -.
DR   VGNC; VGNC:97689; XRCC1.
DR   eggNOG; KOG3226; Eukaryota.
DR   GeneTree; ENSGT00390000004140; -.
DR   HOGENOM; CLU_030026_0_0_1; -.
DR   InParanoid; M3W3P2; -.
DR   OMA; PEWIYAI; -.
DR   OrthoDB; 1334125at2759; -.
DR   Proteomes; UP000011712; Chromosome E2.
DR   Bgee; ENSFCAG00000005222; Expressed in embryo and 10 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0070522; C:ERCC4-ERCC1 complex; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0090734; C:site of DNA damage; IEA:Ensembl.
DR   GO; GO:1990599; F:3' overhang single-stranded DNA endodeoxyribonuclease activity; IEA:Ensembl.
DR   GO; GO:0160002; F:ADP-D-ribose modification-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0032356; F:oxidized DNA binding; IEA:Ensembl.
DR   GO; GO:0072572; F:poly-ADP-D-ribose binding; IEA:Ensembl.
DR   GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR   GO; GO:0021587; P:cerebellum morphogenesis; IEA:Ensembl.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR   GO; GO:1905765; P:negative regulation of protection from non-homologous end joining at telomere; IEA:Ensembl.
DR   GO; GO:1903518; P:positive regulation of single strand break repair; IEA:Ensembl.
DR   GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IEA:Ensembl.
DR   GO; GO:0033194; P:response to hydroperoxide; IEA:Ensembl.
DR   GO; GO:0000012; P:single strand break repair; IEA:InterPro.
DR   GO; GO:0061819; P:telomeric DNA-containing double minutes formation; IEA:Ensembl.
DR   GO; GO:0050882; P:voluntary musculoskeletal movement; IEA:Ensembl.
DR   CDD; cd17725; BRCT_XRCC1_rpt1; 1.
DR   CDD; cd17707; BRCT_XRCC1_rpt2; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 2.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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   PANTHER; PTHR11370:SF6; DNA REPAIR PROTEIN XRCC1; 1.
DR   PANTHER; PTHR11370; DNA-REPAIR PROTEIN XRCC1; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF01834; XRCC1_N; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF52113; BRCT domain; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS50172; BRCT; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT   DOMAIN          313..401
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          536..627
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          221..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..281
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..483
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  69024 MW;  F9A6F577046E2163 CRC64;
     MPEIRLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE KEEQIHSVDI
     GNDGSAFVEV LVGSSAGGAG EQDYEVLLVT SSFMSPSESR SGSNPNRVRI FGPDKLVRAA
     AEKRWDRVKI VCSQPYSKDS PYGLSFIRFH SPPDKEEVEA SPQKVTKLGQ FRVKEEDEGA
     NSLRPGALFF SRINKTSPAT ATDPAGPSYA AATLQASSAA SSASPVSRAV GGASKPQESP
     KGKRKLDLNQ EERKMPGKAS AQPSPPALKR PKLPAPTRTP ASSTPVPASA RGTVPGKTRE
     ATEPRGPRAG PQELGKILQG VVVVLSGFQN PFRSELRDKA LELGAKYRPD WTPDSTHLIC
     AFANTPKYSQ VLGLGGRIVR KEWVLDCHRM RRRLPSRRYL MAGPSSSSED EGGSHSGSSG
     DEAPKLPQKR PQTKTKPPQA AGPSSPQRPT TPEETKPASP GPREDTDTEG EQSEELGNGA
     EDSGDTEDEL RRVAEQREQK QPPDQGENGE DPYAGSTDEN TDNEGPPESP DLPVPELPDF
     FQGKHFFLYG EFPGDERRKL SRYVTAFNGE LEDYMSDRVQ FVITAQEWDP SFEEALMDNP
     SLVFVRPRWI YSCNEKQKLL PHQLYGVVPQ A
//
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