XPA_XENLA
ID XPA_XENLA Reviewed; 267 AA.
AC P27088; Q05AX5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=DNA repair protein complementing XP-A cells homolog;
DE AltName: Full=Xeroderma pigmentosum group A-complementing protein homolog;
GN Name=xpa; Synonyms=xpac;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT 3-PRO-GLU-4 DEL.
RX PubMed=1764072; DOI=10.1016/0006-291x(91)92070-z;
RA Shimamoto T., Kohno K., Tanaka K., Okada Y.;
RT "Molecular cloning of human XPAC gene homologs from chicken, Xenopus laevis
RT and Drosophila melanogaster.";
RL Biochem. Biophys. Res. Commun. 181:1231-1237(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT 3-PRO-GLU-4 DEL.
RC TISSUE=Fat body;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the XPA family. {ECO:0000305}.
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DR EMBL; D31894; BAA06692.1; -; mRNA.
DR EMBL; BC123173; AAI23174.1; -; mRNA.
DR PIR; JG0191; JG0191.
DR PIR; JQ1324; JQ1324.
DR RefSeq; NP_001081354.1; NM_001087885.1.
DR AlphaFoldDB; P27088; -.
DR SMR; P27088; -.
DR BioGRID; 99129; 1.
DR IntAct; P27088; 1.
DR DNASU; 397790; -.
DR GeneID; 397790; -.
DR KEGG; xla:397790; -.
DR CTD; 397790; -.
DR Xenbase; XB-GENE-977987; xpa.L.
DR OrthoDB; 1542306at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 397790; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:1990391; C:DNA repair complex; IDA:CAFA.
DR GO; GO:0005662; C:DNA replication factor A complex; IDA:CAFA.
DR GO; GO:0005634; C:nucleus; IMP:CAFA.
DR GO; GO:0003684; F:damaged DNA binding; IDA:CAFA.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:CAFA.
DR GO; GO:0070914; P:UV-damage excision repair; IDA:CAFA.
DR DisProt; DP00091; -.
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; PS00752; XPA_1; 1.
DR PROSITE; PS00753; XPA_2; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..267
FT /note="DNA repair protein complementing XP-A cells homolog"
FT /id="PRO_0000208651"
FT ZN_FING 99..123
FT MOTIF 25..46
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT VARIANT 3..4
FT /note="Missing (in one isoform)"
FT /evidence="ECO:0000269|PubMed:1764072, ECO:0000269|Ref.2"
SQ SEQUENCE 267 AA; 31180 MW; 094DEEF160657199 CRC64;
MEPEPEPEQE ANKEEEKILS AAVRAKIERN RQRALMLRQA RLACRPYPTG EGISTVKAPP
KVIDSGGGFF IEEEEAEEQH VENVVRQPGP VLECDYLICE ECGKDFMDSY LSNHFDLAVC
DSCRDAEEKH KLITRTEAKQ EYLLKDCDID KREPVLKFIL KKNPHNTHWG DMKLYLKAQV
IKRSLEVWGS EEALEEAKEV RKDNRDKMKQ KKFDKKVKEL RRTVRSSLWK KEASGHQHEY
GPEEHVEEDS YKKTCITCGY EMNYEKM