PARIS_DROME
ID PARIS_DROME Reviewed; 346 AA.
AC Q9VR05; Q960V8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Zinc finger protein Paris {ECO:0000303|PubMed:27819722};
DE AltName: Full=Parkin-interacting substrate {ECO:0000303|PubMed:27819722};
GN Name=Paris {ECO:0000303|PubMed:27819722, ECO:0000312|FlyBase:FBgn0031610};
GN ORFNames=CG15436 {ECO:0000312|FlyBase:FBgn0031610};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAK93243.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93243.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAK93243.1};
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] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27819722; DOI=10.4238/gmr15048934;
RA Merzetti E.M., Staveley B.E.;
RT "Identifying potential PARIS homologs in D. melanogaster.";
RL Genet. Mol. Res. 15:0-0(2016).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PARK, PHOSPHORYLATION, UBIQUITINATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=32138754; DOI=10.1186/s13024-020-00363-x;
RA Pirooznia S.K., Yuan C., Khan M.R., Karuppagounder S.S., Wang L., Xiong Y.,
RA Kang S.U., Lee Y., Dawson V.L., Dawson T.M.;
RT "PARIS induced defects in mitochondrial biogenesis drive dopamine neuron
RT loss under conditions of parkin or PINK1 deficiency.";
RL Mol. Neurodegener. 15:17-17(2020).
CC -!- FUNCTION: Transcription repressor that inhibits transcription of
CC srl/PGC-1-alpha to negatively regulate mitochondrial biogenesis and
CC thereby promotes neurodegeneration (PubMed:27819722, PubMed:32138754).
CC In neurons, functions downstream of the Pink1-park pathway and is
CC likely to act as part of the Pink1-park homeostatic mechanism that
CC maintains mitochondrial quality and function through degradation
CC (mitophagy) and synthesis (biogenesis) (PubMed:32138754).
CC {ECO:0000269|PubMed:27819722, ECO:0000269|PubMed:32138754}.
CC -!- SUBUNIT: Interacts with park. {ECO:0000269|PubMed:32138754}.
CC -!- PTM: Phosphorylated by Pink1 leading to ubiquitination by park.
CC {ECO:0000269|PubMed:32138754}.
CC -!- PTM: Ubiquitinated by park. Polyubiquitination by park leads to
CC degradation by the proteasome which likely activates mitochondrial
CC biogenesis to maintain neuron health and function.
CC {ECO:0000269|PubMed:32138754}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in dopamine neurons
CC increases dopaminergic mRNA levels of srl and its downstream
CC transcription factors ewg and TFAM, and also results in a significant
CC increase in mean lifespan (64 days) compared to controls (60 days)
CC (PubMed:27819722, PubMed:32138754). However, it has no effect on
CC mitochondrial abundance, neuronal survival or climbing performance
CC (PubMed:32138754). Double knockdown with park or Pink1 in the dopamine
CC neurons, improves climbing performance defects and rescues decreased
CC mRNA levels of srl, ewg and TFAM in the single park or Pink1 mutants
CC (PubMed:32138754). RNAi-mediated knockdown in the eye has no
CC significant effect on ommatidia or bristle number (PubMed:32138754).
CC {ECO:0000269|PubMed:27819722, ECO:0000269|PubMed:32138754}.
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DR EMBL; AE014134; AAF51003.2; -; Genomic_DNA.
DR EMBL; AY051819; AAK93243.1; -; mRNA.
DR RefSeq; NP_608840.1; NM_134996.4.
DR AlphaFoldDB; Q9VR05; -.
DR SMR; Q9VR05; -.
DR IntAct; Q9VR05; 12.
DR STRING; 7227.FBpp0077132; -.
DR PaxDb; Q9VR05; -.
DR DNASU; 33657; -.
DR EnsemblMetazoa; FBtr0077442; FBpp0077132; FBgn0031610.
DR GeneID; 33657; -.
DR KEGG; dme:Dmel_CG15436; -.
DR UCSC; CG15436-RA; d. melanogaster.
DR FlyBase; FBgn0031610; Paris.
DR VEuPathDB; VectorBase:FBgn0031610; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT01050000244892; -.
DR HOGENOM; CLU_002678_2_2_1; -.
DR InParanoid; Q9VR05; -.
DR OMA; CTRYFIE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9VR05; -.
DR BioGRID-ORCS; 33657; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33657; -.
DR PRO; PR:Q9VR05; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031610; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0140655; P:mitochondrial proliferation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF07776; zf-AD; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00868; zf-AD; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS51915; ZAD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 1: Evidence at protein level;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..346
FT /note="Zinc finger protein Paris"
FT /id="PRO_0000454969"
FT DOMAIN 3..79
FT /note="ZAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT ZN_FING 126..148
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 154..176
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 182..204
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 210..232
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 238..260
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 266..288
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 322..345
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
SQ SEQUENCE 346 AA; 40502 MW; DBEC3B22C67EC467 CRC64;
MAEICRVCMD ISGKLVNIFD ARRRTRVSIA EMIAQCTGFE VKRGDLFSEM ICPQCYEDVK
SAYGIRQTCE ESHQFYCRVR DEGIEDALCA LLEEEDWEIS EDEDARIDSA SAADDDGKSD
SKKVAFECRE CHKKYQRKGT FLRHMRTHMD GQSFPCPYCK RNFRLRVTLK AHMKTHNAAK
PYECSHCAKT FAQQSTLQSH ERTHTGERPF KCSQCSKTFI KSSDLRRHIR THGSERPFKC
SKCTKTFTRK FHLDNHFRSH TGERPFKCSH CPKAFAMKQH LKQHSRLHLP DRPFRCSHCP
KTFRLSSTLK EHKLVHNAER TFKCPHCASF YKQRKTLARH ILEIHK
