ID   XPA_CRIGR               Reviewed;          97 AA.
AC   Q64029;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=DNA repair protein complementing XP-A cells homolog;
DE   AltName: Full=Xeroderma pigmentosum group A-complementing protein homolog;
DE   Flags: Fragment;
GN   Name=XPA; Synonyms=XPAC;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Ovary;
RX   PubMed=7974007; DOI=10.1007/bf02254721;
RA   Cleaver J.E., McDowell M., Jones C., Wood R., Karentz D.;
RT   "Mutation and expression of the XPA gene in revertants and hybrids of a
RT   Xeroderma pigmentosum cell line.";
RL   Somat. Cell Mol. Genet. 20:327-337(1994).
CC   -!- FUNCTION: Involved in DNA excision repair. Initiates repair by binding
CC       to damaged sites with various affinities, depending on the photoproduct
CC       and the transcriptional state of the region. Required for UV-induced
CC       CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane
CC       pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:7974007}.
CC   -!- SUBUNIT: Interacts with GPN1. Interacts with RPA1 and RPA2; the
CC       interaction is direct and associates XPA with the RPA complex.
CC       Interacts (via N-terminus) with CEP164 upon UV irradiation. Interacts
CC       with HERC2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by HERC2 leading to degradation by the proteasome.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the XPA family. {ECO:0000305}.
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DR   EMBL; S74024; AAP21086.1; -; mRNA.
DR   AlphaFoldDB; Q64029; -.
DR   SMR; Q64029; -.
DR   STRING; 10029.XP_007617660.1; -.
DR   eggNOG; KOG4017; Eukaryota.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   Gene3D; 3.90.530.10; -; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR000465; XPA.
DR   InterPro; IPR022656; XPA_C.
DR   InterPro; IPR022658; XPA_CS.
DR   InterPro; IPR037129; XPA_sf.
DR   InterPro; IPR022652; Znf_XPA_CS.
DR   PANTHER; PTHR10142; PTHR10142; 1.
DR   Pfam; PF05181; XPA_C; 1.
DR   Pfam; PF01286; XPA_N; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   TIGRFAMs; TIGR00598; rad14; 1.
DR   PROSITE; PS00753; XPA_2; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA repair; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           <1..>97
FT                   /note="DNA repair protein complementing XP-A cells homolog"
FT                   /id="PRO_0000208647"
FT   ZN_FING         <1..15
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23025"
FT   CROSSLNK        31
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P23025"
FT   NON_TER         1
FT   NON_TER         97
SQ   SEQUENCE   97 AA;  11519 MW;  B55360D5C5C24EEE CRC64;
     SYLMNHFDLP TCDSCRDADD KHKLITKTEA KQEYLLKDCD LEKREPALRF IVKKNPRHSQ
     WGDMKLYLKL QVVKRALEVW GSQDALEDAK EVRQENR