APTX_DROME
ID APTX_DROME Reviewed; 662 AA.
AC Q8MSG8; A4V347; L0BID2; Q9VDX2; Q9VDX3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Aprataxin-like protein;
DE EC=3.-.-.-;
GN ORFNames=CG5316;
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.
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=Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-binding protein involved in single-strand DNA break
CC repair, double-strand DNA break repair and base excision repair.
CC Resolves abortive DNA ligation intermediates formed either at base
CC excision sites, or when DNA ligases attempt to repair non-ligatable
CC breaks induced by reactive oxygen species. Catalyzes the release of
CC adenylate groups covalently linked to 5'-phosphate termini, resulting
CC in the production of 5'-phosphate termini that can be efficiently
CC rejoined (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B; Synonyms=C;
CC IsoId=Q8MSG8-1; Sequence=Displayed;
CC Name=D;
CC IsoId=Q8MSG8-2; Sequence=VSP_010547;
CC Name=A;
CC IsoId=Q8MSG8-4; Sequence=VSP_047935, VSP_047936;
CC -!- DOMAIN: The HIT domain is required for enzymatic activity.
CC {ECO:0000250}.
CC -!- DOMAIN: The C2H2-type zinc finger mediates DNA-binding. {ECO:0000250}.
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DR EMBL; AE014297; AAF55666.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF55667.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13800.1; -; Genomic_DNA.
DR EMBL; AY118832; AAM50692.1; -; mRNA.
DR EMBL; BT011192; AFZ88725.1; -; mRNA.
DR EMBL; BT012473; AAS93744.1; -; mRNA.
DR RefSeq; NP_650805.1; NM_142548.2. [Q8MSG8-1]
DR RefSeq; NP_732421.1; NM_169858.1. [Q8MSG8-1]
DR RefSeq; NP_732422.1; NM_169859.3. [Q8MSG8-4]
DR AlphaFoldDB; Q8MSG8; -.
DR SMR; Q8MSG8; -.
DR BioGRID; 67317; 2.
DR IntAct; Q8MSG8; 1.
DR STRING; 7227.FBpp0083172; -.
DR PaxDb; Q8MSG8; -.
DR PRIDE; Q8MSG8; -.
DR EnsemblMetazoa; FBtr0083758; FBpp0083172; FBgn0038704. [Q8MSG8-1]
DR EnsemblMetazoa; FBtr0083759; FBpp0083173; FBgn0038704. [Q8MSG8-4]
DR EnsemblMetazoa; FBtr0083760; FBpp0083174; FBgn0038704. [Q8MSG8-1]
DR GeneID; 42322; -.
DR KEGG; dme:Dmel_CG5316; -.
DR UCSC; CG5316-RA; d. melanogaster. [Q8MSG8-1]
DR UCSC; CG5316-RC; d. melanogaster.
DR FlyBase; FBgn0038704; CG5316.
DR VEuPathDB; VectorBase:FBgn0038704; -.
DR eggNOG; KOG0562; Eukaryota.
DR GeneTree; ENSGT00940000156806; -.
DR HOGENOM; CLU_024713_0_0_1; -.
DR InParanoid; Q8MSG8; -.
DR OMA; HENVVEK; -.
DR PhylomeDB; Q8MSG8; -.
DR BioGRID-ORCS; 42322; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG5316; fly.
DR GenomeRNAi; 42322; -.
DR PRO; PR:Q8MSG8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038704; Expressed in saliva-secreting gland and 27 other tissues.
DR ExpressionAtlas; Q8MSG8; baseline and differential.
DR Genevisible; Q8MSG8; DM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR GO; GO:0033699; F:DNA 5'-adenosine monophosphate hydrolase activity; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030983; F:mismatched DNA binding; IBA:GO_Central.
DR GO; GO:1990165; F:single-strand break-containing DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0000012; P:single strand break repair; ISS:UniProtKB.
DR Gene3D; 3.30.428.10; -; 2.
DR InterPro; IPR026963; Aprataxin-like.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR032566; Znf-C2HE.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12486:SF4; PTHR12486:SF4; 2.
DR Pfam; PF16278; zf-C2HE; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54197; SSF54197; 2.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..662
FT /note="Aprataxin-like protein"
FT /id="PRO_0000109849"
FT DOMAIN 4..108
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT ZN_FING 381..403
FT /note="C2H2-type"
FT REGION 482..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_010547"
FT VAR_SEQ 127
FT /note="K -> SKAIRTRRRLQAS (in isoform A)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047935"
FT VAR_SEQ 128..662
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047936"
FT CONFLICT 44
FT /note="A -> D (in Ref. 3; AAM50692)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="T -> K (in Ref. 3; AAM50692)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="K -> E (in Ref. 5; AAS93744)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="F -> I (in Ref. 3; AAM50692)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="K -> T (in Ref. 3; AAM50692)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="E -> K (in Ref. 3; AAM50692)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="N -> P (in Ref. 3; AAM50692)"
FT /evidence="ECO:0000305"
FT CONFLICT 451..452
FT /note="AA -> GSG (in Ref. 3; AAM50692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 76477 MW; D4DC720076FFB331 CRC64;
MSWSSALIKD ISKPENLIIS SEIAVVIADK FPKAQHHYLV LPLADIPSIF HLNRSHLSLL
EELHLLARNV VEVKGVRWQD FNVGFHAEPS MQRLHLHVIS KDFVSTSLKT KKHWNSFNTE
LFVPYTKLYA QLEKENSISR LPKSLKDELL AKPLICNQCE FVARNLPSLK GHLVGHLQDP
KSVCQRVRLG NQFFPTAGYR TSELAYCFDF VDFYEYKKQM EVDKLAYIRD ELQRKLNDKR
NFLIESDRAV VMKADYPKSQ YHFRVVAKEE FRDITQLTEA QLPLLDHMMD LANQIIEKQK
HLESRNFLIG FKVNTFWNRL NLHVISNDFY SMAMKRISHW NSFNTELFMP FQIAYMMLSV
QGSIESISEE TYNNLQEKTP LRCNQCEFVT NMLLDLKAHL YQHWQRKEDE RDQKKKVDKI
IQMISETKLD EAEAKPKLLN EEEPIQAQPV AAIAQYPNEH LGKPLTPQQQ PGKQQAQNVY
DKNINGPSVN MMNQNNPNNP FRNTPHLNRQ SQKPPHPRSG PRGPMAPWTG PRFPCHQQQN
RFRPPGFNAC RQPYPPYHSG HQQFPNASSV GGGQTGLPGQ GQGPRPKWNS NKIFNQQNRQ
NTVQAQPQAQ NQQTNQQQIQ NSNKNQTPKK KPWKNRLQPV GKVQNQGGAN RDPAPPSNSK
PS
