XPA_DROME
ID XPA_DROME Reviewed; 296 AA.
AC P28518; Q24594; Q9V3V8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=DNA repair protein complementing XP-A cells homolog;
DE AltName: Full=Xeroderma pigmentosum group A-complementing protein homolog;
GN Name=Xpac; Synonyms=Xpa; ORFNames=CG6358;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [GENOMIC DNA].
RX PubMed=7673233; DOI=10.1074/jbc.270.38.22452;
RA Shimamoto T., Tanimura T., Yoneda Y., Kobayakawa Y., Sugasawa K.,
RA Hanaoka F., Oka M., Okada Y., Tanaka K., Kohno K.;
RT "Expression and functional analyses of the Dxpa gene, the Drosophila
RT homolog of the human excision repair gene XPA.";
RL J. Biol. Chem. 270:22452-22459(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
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 -!- TISSUE SPECIFICITY: Strongly expressed in the central nervous system
CC and muscles.
CC -!- DEVELOPMENTAL STAGE: Continuously expressed in all stages of
CC development.
CC -!- SIMILARITY: Belongs to the XPA family. {ECO:0000305}.
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DR EMBL; D31893; BAA06691.1; -; mRNA.
DR EMBL; D31892; BAA06690.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45917.1; -; Genomic_DNA.
DR EMBL; AL033125; CAA21834.1; -; Genomic_DNA.
DR PIR; JQ1325; JQ1325.
DR RefSeq; NP_476866.1; NM_057518.4.
DR AlphaFoldDB; P28518; -.
DR SMR; P28518; -.
DR BioGRID; 57875; 14.
DR DIP; DIP-17686N; -.
DR IntAct; P28518; 14.
DR STRING; 7227.FBpp0070638; -.
DR PaxDb; P28518; -.
DR PRIDE; P28518; -.
DR EnsemblMetazoa; FBtr0070670; FBpp0070638; FBgn0004832.
DR GeneID; 31357; -.
DR KEGG; dme:Dmel_CG6358; -.
DR CTD; 31357; -.
DR FlyBase; FBgn0004832; Xpac.
DR VEuPathDB; VectorBase:FBgn0004832; -.
DR eggNOG; KOG4017; Eukaryota.
DR GeneTree; ENSGT00390000002721; -.
DR HOGENOM; CLU_053731_1_0_1; -.
DR InParanoid; P28518; -.
DR OMA; VWKRETV; -.
DR OrthoDB; 1542306at2759; -.
DR PhylomeDB; P28518; -.
DR Reactome; R-DME-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DME-5696400; Dual Incision in GG-NER.
DR Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR BioGRID-ORCS; 31357; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31357; -.
DR PRO; PR:P28518; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004832; Expressed in secondary oocyte and 20 other tissues.
DR ExpressionAtlas; P28518; baseline and differential.
DR Genevisible; P28518; DM.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:FlyBase.
DR GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IBA:GO_Central.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IBA:GO_Central.
DR GO; GO:0070914; P:UV-damage excision repair; IBA:GO_Central.
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..296
FT /note="DNA repair protein complementing XP-A cells homolog"
FT /id="PRO_0000208652"
FT ZN_FING 126..150
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 26..47
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 10
FT /note="S -> A (in Ref. 2; BAA06690)"
FT /evidence="ECO:0000305"
FT CONFLICT 224..226
FT /note="QHE -> HEQ (in Ref. 1; BAA06691)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 33875 MW; 54C58F924955E2A4 CRC64;
MSAEVSTNES APPAEKKSKL TNAQKARIER NQAKAQKLRE AKLVSHPFKE LASNKEGGTH
PEAALSQGSS VIKVQGTKYI DSGGGFLLEQ PVMPTGVGPA GLNKSGEEAP PILDDAIAIP
VQYEECLECG DMFADSYLFN NFGHSVCDKC RDKDERYALI TRTEAKAEYL LKDCDFDKRE
PKLRYISRKN PHNVRWGEMK LYLHLQIHQR ALEVWGSEEE LVRQHEARED KREEGKARKY
NKKMKQLRME VRSSIYTKKT HEVHEHEFGP DTYDEEEDTY THTCITCPYS ETYEKM
