NARYA_DROME
ID NARYA_DROME Reviewed; 211 AA.
AC Q9VWI4; Q7K4P2;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=RING finger protein narya {ECO:0000303|PubMed:30615609, ECO:0000312|FlyBase:FBgn0031018};
GN Name=narya {ECO:0000303|PubMed:30615609, ECO:0000312|FlyBase:FBgn0031018};
GN ORFNames=CG12200 {ECO:0000312|FlyBase:FBgn0031018};
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:AAK93201.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93201.2};
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-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 46-LEU--VAL-50.
RX PubMed=30615609; DOI=10.1371/journal.pgen.1007886;
RA Lake C.M., Nielsen R.J., Bonner A.M., Eche S., White-Brown S., McKim K.S.,
RA Hawley R.S.;
RT "Narya, a RING finger domain-containing protein, is required for meiotic
RT DNA double-strand break formation and crossover maturation in Drosophila
RT melanogaster.";
RL PLoS Genet. 15:E1007886-E1007886(2019).
CC -!- FUNCTION: Required for the formation of DNA double-strand breaks (DSBs)
CC together with nenya and vilya during the meiotic recombination process
CC (PubMed:30615609). Plays a role in DSBs processing into crossovers
CC (PubMed:30615609). Plays a redundant role with nenya in chromosome
CC segregation during female meiosis (PubMed:30615609).
CC {ECO:0000269|PubMed:30615609}.
CC -!- SUBUNIT: May interact with itself, with nenya and vilya through its
CC RING-type zinc finger. {ECO:0000305|PubMed:30615609}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:30615609}.
CC Note=Localizes to DNA double-strand breaks during female meiosis in
CC both nurse cells and pro-oocytes (PubMed:30615609). During early
CC pachytene, colocalizes with vilya to the central region of the
CC synaptonemal complex (SC) (PubMed:30615609).
CC {ECO:0000269|PubMed:30615609}.
CC -!- TISSUE SPECIFICITY: Expressed in nurse cell and pro-oocytes (at protein
CC level). {ECO:0000269|PubMed:30615609}.
CC -!- MISCELLANEOUS: Nenya, narya and vilya contain a RING-type zinc finger
CC domain and are named after the Three Rings of Power given by the elves
CC of Eregion in J.R.R. Tolkien's books. {ECO:0000305|PubMed:30615609}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93201.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF48955.1; -; Genomic_DNA.
DR EMBL; AY051777; AAK93201.2; ALT_INIT; mRNA.
DR RefSeq; NP_573383.1; NM_133155.4.
DR AlphaFoldDB; Q9VWI4; -.
DR SMR; Q9VWI4; -.
DR IntAct; Q9VWI4; 3.
DR STRING; 7227.FBpp0074479; -.
DR PaxDb; Q9VWI4; -.
DR DNASU; 32932; -.
DR EnsemblMetazoa; FBtr0074710; FBpp0074479; FBgn0031018.
DR GeneID; 32932; -.
DR KEGG; dme:Dmel_CG12200; -.
DR UCSC; CG12200-RA; d. melanogaster.
DR CTD; 32932; -.
DR FlyBase; FBgn0031018; narya.
DR VEuPathDB; VectorBase:FBgn0031018; -.
DR eggNOG; KOG4739; Eukaryota.
DR GeneTree; ENSGT00740000115581; -.
DR HOGENOM; CLU_1268118_0_0_1; -.
DR InParanoid; Q9VWI4; -.
DR OMA; CKMEAQL; -.
DR OrthoDB; 1325661at2759; -.
DR PhylomeDB; Q9VWI4; -.
DR SignaLink; Q9VWI4; -.
DR BioGRID-ORCS; 32932; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32932; -.
DR PRO; PR:Q9VWI4; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0031018; Expressed in adult abdomen and 2 other tissues.
DR Genevisible; Q9VWI4; DM.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0000795; C:synaptonemal complex; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IBA:GO_Central.
DR GO; GO:1903343; P:positive regulation of meiotic DNA double-strand break formation; IGI:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042123; Zip3/RNF212-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22663; PTHR22663; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; Chromosome partition; Meiosis; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..211
FT /note="RING finger protein narya"
FT /evidence="ECO:0000305"
FT /id="PRO_0000447341"
FT ZN_FING 6..47
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 149..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 46..50
FT /note="Missing: Disrupts the RING finger domain. During
FT meiosis, DNA double-strand break formation is normal but
FT their conversion into cross-overs fails."
FT /evidence="ECO:0000269|PubMed:30615609"
SQ SEQUENCE 211 AA; 24623 MW; 2A1E7A507F86DD4B CRC64;
MFRVHCNKCF RHRKTDPAVP FHLTQCRHVI CGPCLGQSSL EKNCPLCGQV LKAIQINRDM
PTSVANYFAD PLRFQQIYRK ISKFQADQRA SDNLGFYRQL QQLEQNKRQL EGFCKMEAQL
NQKVVEEKKR IAELRTYIAY HENAQRMTRR RHSAGERFHT PEFKEAWNTS ISTSDKSPSD
MPSDSSRRSA DLDTQSTRRR SFGSDTKGFR L
