ZMY10_DROME
ID ZMY10_DROME Reviewed; 451 AA.
AC Q9VU41; Q8MZ82;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Zinc finger MYND domain-containing protein 10 homolog;
GN Name=Zmynd10 {ECO:0000312|FlyBase:FBgn0266709};
GN ORFNames=CG11253 {ECO:0000312|FlyBase:FBgn0266709};
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].
RC STRAIN=Berkeley; TISSUE=Testis;
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].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP INDUCTION, AND MUTAGENESIS OF VAL-14.
RX PubMed=23891471; DOI=10.1016/j.ajhg.2013.07.009;
RA Moore D.J., Onoufriadis A., Shoemark A., Simpson M.A., Zur Lage P.I.,
RA de Castro S.C., Bartoloni L., Gallone G., Petridi S., Woollard W.J.,
RA Antony D., Schmidts M., Didonna T., Makrythanasis P., Bevillard J.,
RA Mongan N.P., Djakow J., Pals G., Lucas J.S., Marthin J.K., Nielsen K.G.,
RA Santoni F., Guipponi M., Hogg C., Antonarakis S.E., Emes R.D., Chung E.M.,
RA Greene N.D., Blouin J.L., Jarman A.P., Mitchison H.M.;
RT "Mutations in ZMYND10, a gene essential for proper axonemal assembly of
RT inner and outer dynein arms in humans and flies, cause primary ciliary
RT dyskinesia.";
RL Am. J. Hum. Genet. 93:346-356(2013).
CC -!- FUNCTION: Plays a role in axonemal structure organization and motility.
CC May be involved in axonemal pre-assembly of inner and outer dynein arms
CC (IDA and ODA, respectively) for proper axoneme building for cilia
CC motility. {ECO:0000269|PubMed:23891471}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23891471}. Cell
CC projection, cilium {ECO:0000269|PubMed:23891471}. Dynein axonemal
CC particle {ECO:0000250|UniProtKB:Q5FWU8}. Note=Localizes mainly to the
CC cytoplasm. Present in the cell bodies of Ch neurons. Present at low
CC level in the cilium.
CC -!- TISSUE SPECIFICITY: Specifically expressed in cells with flagella and
CC motile cilia: chordotonal sensory neurons and sperm.
CC {ECO:0000269|PubMed:23891471}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis expression is restricted to
CC developing Ch neurons and absent from other ciliated sensory neurons.
CC In the pupal antenna, expressed exclusively in the Ch neurons of
CC Johnston's organ.
CC -!- INDUCTION: Expression is dependent on the transcription factors that
CC regulate motile cilia such as Rfx and Fd3F.
CC {ECO:0000269|PubMed:23891471}.
CC -!- DISRUPTION PHENOTYPE: Sensory defects and loss of the axonemal dynein
CC arms. Flies display defective proprioception as a result of
CC malfunctioning Ch neurons caused by inner and outer dynein arms (IDA
CC and ODA, respectively) defects. Males sterility due to immotile sperm.
CC {ECO:0000269|PubMed:23891471}.
CC -!- SIMILARITY: Belongs to the ZMYND10 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49850.1; -; Genomic_DNA.
DR EMBL; AY113309; AAM29314.1; -; mRNA.
DR EMBL; BT044380; ACH92445.1; -; mRNA.
DR RefSeq; NP_648625.1; NM_140368.2.
DR AlphaFoldDB; Q9VU41; -.
DR SMR; Q9VU41; -.
DR BioGRID; 64827; 4.
DR IntAct; Q9VU41; 2.
DR STRING; 7227.FBpp0075628; -.
DR PaxDb; Q9VU41; -.
DR PRIDE; Q9VU41; -.
DR DNASU; 39481; -.
DR EnsemblMetazoa; FBtr0075894; FBpp0075628; FBgn0266709.
DR GeneID; 39481; -.
DR KEGG; dme:Dmel_CG11253; -.
DR UCSC; CG11253-RA; d. melanogaster.
DR CTD; 51364; -.
DR FlyBase; FBgn0266709; Zmynd10.
DR VEuPathDB; VectorBase:FBgn0266709; -.
DR eggNOG; ENOG502QS3F; Eukaryota.
DR GeneTree; ENSGT00940000153820; -.
DR HOGENOM; CLU_034036_1_0_1; -.
DR InParanoid; Q9VU41; -.
DR OMA; LIHEAYC; -.
DR OrthoDB; 685805at2759; -.
DR PhylomeDB; Q9VU41; -.
DR BioGRID-ORCS; 39481; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39481; -.
DR PRO; PR:Q9VU41; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0266709; Expressed in testis and 11 other tissues.
DR Genevisible; Q9VU41; DM.
DR GO; GO:0034451; C:centriolar satellite; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035082; P:axoneme assembly; IMP:FlyBase.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0036159; P:inner dynein arm assembly; IBA:GO_Central.
DR GO; GO:0044458; P:motile cilium assembly; IMP:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; IMP:UniProtKB.
DR GO; GO:0019230; P:proprioception; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR InterPro; IPR017333; UCP037948_Znf-MYND.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF01753; zf-MYND; 1.
DR PIRSF; PIRSF037948; UCP037948_Znf_MYND10; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cytoplasm; Metal-binding; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..451
FT /note="Zinc finger MYND domain-containing protein 10
FT homolog"
FT /id="PRO_0000424818"
FT ZN_FING 412..448
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT MUTAGEN 14
FT /note="V->G: Partially rescues sterility when transfected
FT in a homozygous mutant fly."
FT /evidence="ECO:0000269|PubMed:23891471"
FT CONFLICT 116
FT /note="V -> M (in Ref. 3; AAM29314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 51634 MW; F69EC560494BB623 CRC64;
MVNFVHPEEM YLFVESIRPF EVREVGSPKW LEVHEMILGL SQQAALELSQ NREEEVKEFL
ISRDKLRVLI HEAYCVTLWK TRVLPHLLEI DPNPQATFLI YTVLYHEAAL VALLDVCLYH
PSGCETLQES VLDLIDYCAQ AISQVIGLVS MGYHENETKL DVDEAVLTEL ERQKRDFIYK
IGLRCISVLN YIADNVTLFH LSAARRLLVT HDIPWLMADV LSFRPWQRKT SKGIQKFIDE
KWTNVDDVTK IVKPEAQAWF CVRQLLLNPQ IMENYAFNEA RCKQLHKLLG LMHEPLLDQL
PPLIELKVFL SRLTLSGNTA KTQPLLLEDI PQIQEELLKD VEENGGFYQI AQDQDSVFLS
KNKENICALA TRLSKAYGTD LLCELEQNMD DLKMGEAKDA GAGGDGDTDH TCATCQAKAK
KKCACCKKVH YCSRDCQLKD WPQHKLVCLK T
