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APLF_DROME
ID   APLF_DROME              Reviewed;         255 AA.
AC   A8JR14; Q9VF76;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Aprataxin and PNK-like factor;
DE            EC=3.1.1.- {ECO:0000269|PubMed:17396150};
DE   AltName: Full=Apurinic-apyrimidinic endonuclease APLF;
GN   ORFNames=CG6171;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17396150; DOI=10.1038/sj.emboj.7601663;
RA   Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., Yasui A.;
RT   "A novel human AP endonuclease with conserved zinc-finger-like motifs
RT   involved in DNA strand break responses.";
RL   EMBO J. 26:2094-2103(2007).
CC   -!- FUNCTION: Displays apurinic-apyrimidinic (AP) endonuclease and 3'-5'
CC       exonuclease activities in vitro. {ECO:0000269|PubMed:17396150}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B;
CC         IsoId=A8JR14-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=A8JR14-2; Sequence=VSP_038137, VSP_038138;
CC   -!- SIMILARITY: Belongs to the APLF family. {ECO:0000305}.
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DR   EMBL; AE014297; ABW08680.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF55184.1; -; Genomic_DNA.
DR   EMBL; BT004895; AAO47873.1; -; mRNA.
DR   RefSeq; NP_001097801.1; NM_001104331.2. [A8JR14-1]
DR   RefSeq; NP_650455.1; NM_142198.3. [A8JR14-2]
DR   AlphaFoldDB; A8JR14; -.
DR   BioGRID; 66935; 10.
DR   STRING; 7227.FBpp0111839; -.
DR   PaxDb; A8JR14; -.
DR   DNASU; 41872; -.
DR   EnsemblMetazoa; FBtr0083113; FBpp0082567; FBgn0026737. [A8JR14-2]
DR   EnsemblMetazoa; FBtr0112926; FBpp0111839; FBgn0026737. [A8JR14-1]
DR   GeneID; 41872; -.
DR   KEGG; dme:Dmel_CG6171; -.
DR   UCSC; CG6171-RA; d. melanogaster.
DR   UCSC; CG6171-RB; d. melanogaster. [A8JR14-1]
DR   FlyBase; FBgn0026737; CG6171.
DR   VEuPathDB; VectorBase:FBgn0026737; -.
DR   eggNOG; ENOG502R7QZ; Eukaryota.
DR   GeneTree; ENSGT00390000010591; -.
DR   HOGENOM; CLU_079469_0_0_1; -.
DR   InParanoid; A8JR14; -.
DR   OMA; RMSHPPN; -.
DR   PhylomeDB; A8JR14; -.
DR   BioGRID-ORCS; 41872; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 41872; -.
DR   PRO; PR:A8JR14; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0026737; Expressed in ovary and 11 other tissues.
DR   Genevisible; A8JR14; DM.
DR   GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR   GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR   GO; GO:0052720; F:class II DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:FlyBase.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:UniProtKB.
DR   GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:FlyBase.
DR   GO; GO:0006302; P:double-strand break repair; ISS:FlyBase.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:FlyBase.
DR   GO; GO:0000012; P:single strand break repair; ISS:FlyBase.
DR   InterPro; IPR039253; APLF.
DR   InterPro; IPR019406; APLF_PBZ.
DR   PANTHER; PTHR21315; PTHR21315; 1.
DR   Pfam; PF10283; zf-CCHH; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Metal-binding; Reference proteome; Repeat;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..255
FT                   /note="Aprataxin and PNK-like factor"
FT                   /id="PRO_0000385300"
FT   ZN_FING         121..142
FT                   /note="PBZ-type 1"
FT   ZN_FING         161..182
FT                   /note="PBZ-type 2"
FT   REGION          1..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..255
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         186..187
FT                   /note="FN -> CK (in isoform A)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038137"
FT   VAR_SEQ         188..255
FT                   /note="Missing (in isoform A)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038138"
SQ   SEQUENCE   255 AA;  28006 MW;  1CB1AC10524D57F3 CRC64;
     MSATDASTAD SGAKRKSSED ITHNCNANFG AENGLRKRVK SEEPVASIKD ETNPEVPMKI
     KAEPVENADE PTSTTPAIKI KAEPADNGNS PAAAMVKTEP TNSNAQDAAD ESTVSSSSIR
     TSCRFGIRCY RRNPAHRSAE AHPGDQDYRR PNFPAPPLGT PACPFGNACY RRNPVHFQDY
     SHPADFNSAQ NIRNRLRQRR AQRQNDDDSG TDEEDEPFGG DNDRDADYRP GADINEDEDD
     ELEFDSQPIS GDDYD
 
 
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