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XPF_DROME
ID   XPF_DROME               Reviewed;         961 AA.
AC   Q24087; Q8IHB9; Q9W4L3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=DNA repair endonuclease XPF;
DE            EC=3.1.-.-;
DE   AltName: Full=Protein meiotic 9;
GN   Name=mei-9; ORFNames=CG3697;
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 [GENOMIC DNA].
RX   PubMed=8647398; DOI=10.1093/genetics/141.2.619;
RA   Sekelsky J.J., McKim K.S., Chin G.M., Hawley R.S.;
RT   "The Drosophila meiotic recombination gene mei-9 encodes a homologue of the
RT   yeast excision repair protein Rad1.";
RL   Genetics 141:619-627(1995).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Testis;
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   [5]
RP   INTERACTION WITH HDM.
RX   PubMed=18957705; DOI=10.1534/genetics.108.093104;
RA   Joyce E.F., Tanneti S.N., McKim K.S.;
RT   "Drosophila hold'em is required for a subset of meiotic crossovers and
RT   interacts with the dna repair endonuclease complex subunits MEI-9 and
RT   ERCC1.";
RL   Genetics 181:335-340(2009).
CC   -!- FUNCTION: Implicated in recombination events during meiosis, mostly in
CC       meiotic exchange. May directly resolve Holliday junctions within
CC       recombination intermediates leading to DNA exchange. Also required for
CC       the repair of mismatches within meiotic heteroduplex DNA and for
CC       nucleotide excision repair.
CC   -!- SUBUNIT: Heterodimer (By similarity). Interacts with hdm. {ECO:0000250,
CC       ECO:0000269|PubMed:18957705}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC46917.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U27181; AAC46917.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE014298; AAF45938.1; -; Genomic_DNA.
DR   EMBL; BT001319; AAN71074.1; -; mRNA.
DR   PIR; S58936; S58936.
DR   RefSeq; NP_001284859.1; NM_001297930.1.
DR   RefSeq; NP_525068.1; NM_080329.3.
DR   AlphaFoldDB; Q24087; -.
DR   SMR; Q24087; -.
DR   BioGRID; 57890; 5.
DR   IntAct; Q24087; 2.
DR   STRING; 7227.FBpp0070624; -.
DR   PaxDb; Q24087; -.
DR   EnsemblMetazoa; FBtr0070656; FBpp0070624; FBgn0002707.
DR   EnsemblMetazoa; FBtr0343574; FBpp0310174; FBgn0002707.
DR   GeneID; 31373; -.
DR   KEGG; dme:Dmel_CG3697; -.
DR   CTD; 31373; -.
DR   FlyBase; FBgn0002707; mei-9.
DR   VEuPathDB; VectorBase:FBgn0002707; -.
DR   eggNOG; KOG0442; Eukaryota.
DR   HOGENOM; CLU_002265_1_0_1; -.
DR   InParanoid; Q24087; -.
DR   OMA; FHKILQA; -.
DR   OrthoDB; 324863at2759; -.
DR   PhylomeDB; Q24087; -.
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-6782135; Dual incision in TC-NER.
DR   BioGRID-ORCS; 31373; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 31373; -.
DR   PRO; PR:Q24087; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0002707; Expressed in cleaving embryo and 16 other tissues.
DR   ExpressionAtlas; Q24087; baseline and differential.
DR   Genevisible; Q24087; DM.
DR   GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:FlyBase.
DR   GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase.
DR   GO; GO:0006310; P:DNA recombination; TAS:FlyBase.
DR   GO; GO:0006302; P:double-strand break repair; IMP:FlyBase.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0016321; P:female meiosis chromosome segregation; IMP:FlyBase.
DR   GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR   GO; GO:0045132; P:meiotic chromosome segregation; IMP:FlyBase.
DR   GO; GO:0006298; P:mismatch repair; IMP:FlyBase.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:FlyBase.
DR   GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IBA:GO_Central.
DR   GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
DR   GO; GO:0030716; P:oocyte fate determination; IMP:FlyBase.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:FlyBase.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IMP:FlyBase.
DR   InterPro; IPR006166; ERCC4_domain.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR006167; XPF.
DR   Pfam; PF02732; ERCC4; 1.
DR   SMART; SM00891; ERCC4; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR00596; rad1; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; DNA-binding; Endonuclease; Hydrolase; Meiosis;
KW   Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..961
FT                   /note="DNA repair endonuclease XPF"
FT                   /id="PRO_0000198855"
FT   DOMAIN          697..777
FT                   /note="ERCC4"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        115
FT                   /note="V -> G (in Ref. 1; AAC46917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        286
FT                   /note="S -> T (in Ref. 1; AAC46917 and 4; AAN71074)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        318
FT                   /note="S -> T (in Ref. 1; AAC46917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        594
FT                   /note="A -> P (in Ref. 1; AAC46917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        798
FT                   /note="A -> R (in Ref. 1; AAC46917)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        853
FT                   /note="T -> M (in Ref. 1; AAC46917 and 4; AAN71074)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   961 AA;  109519 MW;  00099A7E52B3FC46 CRC64;
     MADSCAENAA KGTENERPKE VEASADTVPQ VEEGVEEYLK RKNMVLLDYE KQMFLDLVEA
     DGLLVCAKGL SYDRVVISIL KAYSDSGNLV LVINSSDWEE QYYKSKIEPK YVHEVASTAT
     ERERVYLEGG LQFISTRILV VDLLKQRIPI ELISGIIVLR AHTIIESCQE AFALRLFRQK
     NKTGFVKAFS SSPEAFTIGY SHVERTMRNL FVKHLYIWPR FHESVRTVLQ PWKIQSIEMH
     VPISQNITSI QSHILEIMNF LVQEIKRINR TVDMEAVTVE NCVTKSFHKI LQAQLDCIWH
     QLNSQTKLIV ADLKILRSLM ISTMYHDAVS AYAFMKRYRS TEYALSNSGW TLLDAAEQIF
     KLSRQRVFNG QQEFEPEPCP KWQTLTDLLT KEIPGDMRRS RRSEQQPKVL ILCQDARTCH
     QLKQYLTQGG PRFLLQQALQ HEVPVGKLSD NYAKESQTRS APPKNVSSNK ELRREEVSGS
     QPPLAGMDEL AQLLSESETE GQHFEESYML TMTQPVEVGP AAIDIKPDPD VSIFETIPEL
     EQFDVTAALA SVPHQPYICL QTFKTEREGS MALEHMLEQL QPHYVVMYNM NVTAIRQLEV
     FEARRRLPPA DRMKVYFLIH ARTVEEQAYL TSLRREKAAF EFIIDTKSKM VIPKYQDGKT
     DEAFLLLKTY DDEPTDENAK SRQAGGQAPQ ATKETPKVIV DMREFRSDLP CLIHKRGLEV
     LPLTITIGDY ILTPDICVER KSISDLIGSL NSGRLYNQCV QMQRHYAKPI LLIEFDQNKP
     FHLQGKFMLS QQTSMANADI VQKLQLLTLH FPKLRLIWSP SPYATAQLFE ELKLGKPEPD
     PQTAAALGSD EPTAGEQLHF NSGIYDFLLR LPGVHTRNIH GLLRKGGSLR QLLLRSQKEL
     EELLQSQESA KLLYDILHVA HLPEKDEVTG STALLAASKQ FGAGSHNRFR MAAAASRRGR
     R
 
 
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