VILYA_DROME
ID VILYA_DROME Reviewed; 237 AA.
AC O76908;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=RING finger protein vilya {ECO:0000303|PubMed:26452093};
GN Name=vilya {ECO:0000303|PubMed:26452093};
GN ORFNames=CG2709 {ECO:0000312|FlyBase:FBgn0283545};
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 {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:CAA16813.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000312|EMBL:CAA16813.1};
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [4] {ECO:0000312|EMBL:ABI34203.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26452093; DOI=10.7554/elife.08287;
RA Lake C.M., Nielsen R.J., Guo F., Unruh J.R., Slaughter B.D., Hawley R.S.;
RT "Vilya, a component of the recombination nodule, is required for meiotic
RT double-strand break formation in Drosophila.";
RL Elife 4:0-0(2015).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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 during
CC meiosis together with narya and nenya. {ECO:0000269|PubMed:26452093,
CC ECO:0000269|PubMed:30615609}.
CC -!- SUBUNIT: May interact with itself and with narya and nenya through
CC their RING-type zinc fingers. {ECO:0000305|PubMed:30615609}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:26452093,
CC ECO:0000269|PubMed:30615609}. Note=During early pachytene, colocalizes
CC with narya to the central region of the synaptonemal complex (SC) in
CC both linear stretches and discrete foci which correspond to
CC recombination nodules. As pachytene progresses, found mainly at
CC recombination nodules. Double-strand break formation is required for
CC recruitment to recombination nodules but not for linear localization to
CC the central region of the SC. {ECO:0000269|PubMed:26452093,
CC ECO:0000269|PubMed:30615609}.
CC -!- TISSUE SPECIFICITY: Expressed in nurse cell and pro-oocytes (at protein
CC level). {ECO:0000269|PubMed:30615609}.
CC -!- DISRUPTION PHENOTYPE: High levels of X chromosome non-disjunction at
CC the first meiotic division, severe failure to initiate DNA double-
CC strand breaks in oocytes in early pachytene and complete failure of
CC meiotic recombination. {ECO:0000269|PubMed:26452093,
CC ECO:0000269|PubMed:30615609}.
CC -!- MISCELLANEOUS: The name 'vilya' derives from the fact that this protein
CC contains a RING-type zinc finger and vilya is the mightiest of the
CC three rings of power given by the elves of Eregion in J.R.R. Tolkien's
CC books. {ECO:0000305|PubMed:26452093}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014298; AAF45818.1; -; Genomic_DNA.
DR EMBL; AL021728; CAA16813.1; -; Genomic_DNA.
DR EMBL; BT028822; ABI34203.1; -; mRNA.
DR EMBL; BT028854; ABI34235.1; -; mRNA.
DR PIR; T13649; T13649.
DR RefSeq; NP_570026.1; NM_130670.2.
DR AlphaFoldDB; O76908; -.
DR SMR; O76908; -.
DR DIP; DIP-18383N; -.
DR IntAct; O76908; 14.
DR STRING; 7227.FBpp0070464; -.
DR PaxDb; O76908; -.
DR DNASU; 31264; -.
DR EnsemblMetazoa; FBtr0070486; FBpp0070464; FBgn0283545.
DR GeneID; 31264; -.
DR KEGG; dme:Dmel_CG2709; -.
DR UCSC; CG2709-RA; d. melanogaster.
DR CTD; 31264; -.
DR FlyBase; FBgn0283545; vilya.
DR VEuPathDB; VectorBase:FBgn0283545; -.
DR eggNOG; KOG4739; Eukaryota.
DR HOGENOM; CLU_1130109_0_0_1; -.
DR InParanoid; O76908; -.
DR OMA; SKLWIHC; -.
DR OrthoDB; 1356483at2759; -.
DR PhylomeDB; O76908; -.
DR SignaLink; O76908; -.
DR GenomeRNAi; 31264; -.
DR PRO; PR:O76908; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0283545; Expressed in female reproductive system and 6 other tissues.
DR GO; GO:0000801; C:central element; IDA:FlyBase.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005713; C:recombination nodule; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:FlyBase.
DR GO; GO:0000795; C:synaptonemal complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; IBA:GO_Central.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP: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; IMP: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; Meiosis; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..237
FT /note="RING finger protein vilya"
FT /id="PRO_0000436008"
FT ZN_FING 21..69
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 172..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 237 AA; 27450 MW; 355DBAA9D92D1831 CRC64;
MAKSQAGQTV EPEASKLWIH CNSCCALFCD KKHTFFLLAC HHVFCERCVK VSAGRTPSDA
PIFECSTCRR SVRGRQLTNS MPNHFKQLFH PEPFTIGNDF VETFQRGNHR HFDKYKERKE
LEMDKLFKDI EVAKSVCQKR FLEAQMLRVE RKKLMQRSRY IKAEVANRKA EMHRMAQAYR
SRSLTSQSSS SAQRSARGRP RGRGTATQSS SRRRSTESAK RQQITSFIHP PNNSFDL
