XPC_DROME
ID XPC_DROME Reviewed; 1293 AA.
AC Q24595; Q7KJI5; Q8MLA1; Q8MLA2; Q9U3Z0; Q9U3Z1; Q9V7A8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=DNA repair protein complementing XP-C cells homolog;
DE AltName: Full=Mutagen-sensitive 209 protein;
DE AltName: Full=XPCDM;
DE AltName: Full=Xeroderma pigmentosum group C-complementing protein homolog;
GN Name=Xpc {ECO:0000312|FlyBase:FBgn0004698};
GN Synonyms=mus210 {ECO:0000312|FlyBase:FBgn0004698}, Xpcc;
GN ORFNames=CG8153 {ECO:0000312|FlyBase:FBgn0004698};
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] (ISOFORM 1).
RC STRAIN=DP CN BW; TISSUE=Embryo;
RX PubMed=8127661; DOI=10.1093/nar/22.3.257;
RA Henning K.A., Peterson C., Legerski R., Friedberg E.C.;
RT "Cloning the Drosophila homolog of the Xeroderma pigmentosum
RT complementation group C gene reveals homology between the predicted human
RT and Drosophila polypeptides and that encoded by the yeast RAD4 gene.";
RL Nucleic Acids Res. 22:257-261(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=10812334; DOI=10.1016/s0921-8777(99)00075-0;
RA Sekelsky J.J., Hollis K.J., Eimerl A.I., Burtis K.C., Hawley R.S.;
RT "Nucleotide excision repair endonuclease genes in Drosophila
RT melanogaster.";
RL Mutat. Res. 459:219-228(2000).
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, AND ALTERNATIVE SPLICING.
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 MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-32; SER-37; SER-533;
RP SER-537; SER-908 AND SER-911, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Involved in DNA excision repair. May play a part in DNA
CC damage recognition and/or in altering chromatin structure to allow
CC access by damage-processing enzymes (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Involved in nucleotide excision repair of DNA damaged with UV
CC light, bulky adducts, or cross-linking agents.
CC -!- SUBUNIT: Heterodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A;
CC IsoId=Q24595-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q24595-2; Sequence=VSP_015197;
CC Name=3; Synonyms=C;
CC IsoId=Q24595-3; Sequence=VSP_015198;
CC -!- SIMILARITY: Belongs to the XPC family. {ECO:0000305}.
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DR EMBL; Z28622; CAA82262.1; -; mRNA.
DR EMBL; AF209743; AAF24766.1; -; Genomic_DNA.
DR EMBL; AF209743; AAF24767.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58150.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68530.1; -; Genomic_DNA.
DR EMBL; AY070566; AAL48037.1; -; mRNA.
DR PIR; S42402; S42402.
DR RefSeq; NP_476861.1; NM_057513.4. [Q24595-1]
DR RefSeq; NP_725451.1; NM_166087.2. [Q24595-3]
DR AlphaFoldDB; Q24595; -.
DR SMR; Q24595; -.
DR BioGRID; 62434; 6.
DR IntAct; Q24595; 13.
DR STRING; 7227.FBpp0086505; -.
DR iPTMnet; Q24595; -.
DR PaxDb; Q24595; -.
DR PRIDE; Q24595; -.
DR EnsemblMetazoa; FBtr0087373; FBpp0086505; FBgn0004698. [Q24595-3]
DR EnsemblMetazoa; FBtr0087374; FBpp0086506; FBgn0004698. [Q24595-1]
DR GeneID; 36697; -.
DR KEGG; dme:Dmel_CG8153; -.
DR CTD; 7508; -.
DR FlyBase; FBgn0004698; Xpc.
DR VEuPathDB; VectorBase:FBgn0004698; -.
DR eggNOG; KOG2179; Eukaryota.
DR GeneTree; ENSGT00390000005194; -.
DR HOGENOM; CLU_009925_0_0_1; -.
DR InParanoid; Q24595; -.
DR OMA; PMYDGFV; -.
DR PhylomeDB; Q24595; -.
DR Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DME-5696395; Formation of Incision Complex in GG-NER.
DR SignaLink; Q24595; -.
DR BioGRID-ORCS; 36697; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36697; -.
DR PRO; PR:Q24595; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004698; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q24595; baseline and differential.
DR Genevisible; Q24595; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:0000111; C:nucleotide-excision repair factor 2 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR GO; GO:0071942; C:XPC complex; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; ISS:FlyBase.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0010777; P:meiotic mismatch repair involved in reciprocal meiotic recombination; IGI:FlyBase.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:FlyBase.
DR Gene3D; 3.30.70.2460; -; 1.
DR Gene3D; 3.90.260.10; -; 2.
DR InterPro; IPR018327; BHD_2.
DR InterPro; IPR004583; DNA_repair_Rad4.
DR InterPro; IPR018026; DNA_repair_Rad4_subgr.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR018326; Rad4_beta-hairpin_dom1.
DR InterPro; IPR018328; Rad4_beta-hairpin_dom3.
DR InterPro; IPR042488; Rad4_BHD3_sf.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR PANTHER; PTHR12135; PTHR12135; 1.
DR Pfam; PF10403; BHD_1; 1.
DR Pfam; PF10404; BHD_2; 1.
DR Pfam; PF10405; BHD_3; 1.
DR Pfam; PF03835; Rad4; 1.
DR SMART; SM01030; BHD_1; 1.
DR SMART; SM01031; BHD_2; 1.
DR SMART; SM01032; BHD_3; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR TIGRFAMs; TIGR00605; rad4; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1293
FT /note="DNA repair protein complementing XP-C cells homolog"
FT /id="PRO_0000218295"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 922..938
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1195..1211
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1275..1291
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..331
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..782
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015197"
FT VAR_SEQ 63
FT /note="G -> GS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_015198"
FT CONFLICT 109
FT /note="K -> Q (in Ref. 1; CAA82262 and 2; AAF24766)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="G -> D (in Ref. 1; CAA82262)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="Y -> H (in Ref. 1; CAA82262)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="P -> S (in Ref. 1; CAA82262)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="D -> A (in Ref. 1; CAA82262)"
FT /evidence="ECO:0000305"
FT CONFLICT 945
FT /note="D -> E (in Ref. 2; AAF24766/AAF24767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1245
FT /note="E -> D (in Ref. 1; CAA82262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1293 AA; 144224 MW; C3F2BFE7A8DE6A57 CRC64;
MSDEEEDSVS EGFSASEDEW KPSKDVKGGE SSDDDDSDFD ELQAEGGAAG SSGRSSAVAG
KRGDHKAPSG IKGSSVKKRK PTGQSLRSKL YNKYRPPPKT FPTSPSQQKE NTPRASGSKN
AKTPNESGAR NQHGPADSSS ESSVEDYLVN PADLDLHSTF FAGGQKEKSP APQFDCNAGI
TNLSDSGSED NNESSFEDKA GNAFDFRGLL ENANSLERTR DALSKRNVTA TPPRSQAATM
DVNALLALGE NQNYQSVEVE EREGNQRKKA GRGAPAAPPT LDEPSRLSKT KSTRIKRHTK
TRPVSTVVAN AGDTDDSDFE EVADADLSSD QDDGETPNIS GDLEIRVGLE GLRPTKEQKT
QHELEMALKR RLNRDIKDRQ ILLHKVSLMC QIARSLKYNR LLSESDSLMQ ATLKLLPSRN
AYPTERGTEL KYLQSFVTWF KTSIKLLSPN LYSAQSPATK EAILEALLEQ VKRKEARCKQ
DMIFIFIALA RGMGMHCRLI VNLQPMPLRP AASDLIPIKL RPDDKNKSQT VESERESEDE
KPKKDKKAGK PAEKESSKST ISKEAEKKNN AKKAEAKPLS KSTTKGSETT KSGTVPKVKK
ELSLSSKLVE KSKHQKAYTS SKSDTSFDEK PSTSSSSKCL KEEYSELGLS KKLLKPTLSS
KLVLKSKNQS SFSSNKSDTS FEENPSTSSS SKSLKEETAK LSSSKLEDKK VASPAETKTK
VQSSLLKRVT TQNISESGDS KKPKVAPVDT FSPVAGRTRR ATVKPKTEEK PQVVGSPVIP
KLMLSKVKQL NAKHSDTENA SPANKHLQEQ RNTRETRSRS KSPKVLISPS FLKKKSDGAD
STSDPQKHQM APETKARISP NFLSEALPAR QLRSRGQKAS SLAIPQLDGG DDVPLPKKRP
KLEKLKNSQD SDEVFEPAKP VKKAPVLPKS VQNLRKDRRV MSTDDEGGSR LNRKTDASDM
WVEVWSDVEE QWICIDLFKG KLHCVDTIRK NATPGLAYVF AFQDDQSLKD VTARYCASWS
TTVRKARVEK AWLDETIAPY LGRRTKRDIT EDDQLRRIHS DKPLPKSISE FKDHPLYVLE
RHLLKFQGLY PPDAPTLGFI RGEAVYSRDC VHLLHSREIW LKSARVVKLG EQPYKVVKAR
PKWDRLTRTV IKDQPLEIFG YWQTQEYEPP TAENGIVPRN AYGNVELFKD CMLPKKTVHL
RLPGLMRICK KLNIDCANAV VGFDFHQGAC HPMYDGFIVC EEFREVVTAA WEEDQQVQVL
KEQEKYETRV YGNWKKLIKG LLIRERLKKK YNF
