ZMY10_DANRE
ID ZMY10_DANRE Reviewed; 448 AA.
AC F1QN74; Q7SZ57;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Zinc finger MYND domain-containing protein 10;
GN Name=zmynd10;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=23891469; DOI=10.1016/j.ajhg.2013.06.007;
RA Zariwala M.A., Gee H.Y., Kurkowiak M., Al-Mutairi D.A., Leigh M.W.,
RA Hurd T.W., Hjeij R., Dell S.D., Chaki M., Dougherty G.W., Adan M.,
RA Spear P.C., Esteve-Rudd J., Loges N.T., Rosenfeld M., Diaz K.A.,
RA Olbrich H., Wolf W.E., Sheridan E., Batten T.F., Halbritter J.,
RA Porath J.D., Kohl S., Lovric S., Hwang D.Y., Pittman J.E., Burns K.A.,
RA Ferkol T.W., Sagel S.D., Olivier K.N., Morgan L.C., Werner C., Raidt J.,
RA Pennekamp P., Sun Z., Zhou W., Airik R., Natarajan S., Allen S.J.,
RA Amirav I., Wieczorek D., Landwehr K., Nielsen K., Schwerk N., Sertic J.,
RA Kohler G., Washburn J., Levy S., Fan S., Koerner-Rettberg C., Amselem S.,
RA Williams D.S., Mitchell B.J., Drummond I.A., Otto E.A., Omran H.,
RA Knowles M.R., Hildebrandt F.;
RT "ZMYND10 is mutated in primary ciliary dyskinesia and interacts with
RT LRRC6.";
RL Am. J. Hum. Genet. 93:336-345(2013).
CC -!- FUNCTION: Plays a role in axonemal structure organization and motility.
CC Involved in axonemal pre-assembly of inner and outer dynein arms (IDA
CC and ODA, respectively) for proper axoneme building for cilia motility
CC (By similarity). May act by indirectly regulating transcription of
CC dynein proteins (By similarity). {ECO:0000250|UniProtKB:Q99ML0}.
CC -!- SUBUNIT: Interacts with LRRC6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6AXZ5}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriolar satellite {ECO:0000250|UniProtKB:Q6AXZ5}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q99ML0}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q5FWU8}. Note=Localizes to sites proximal to the
CC axoneme. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Ciliopathy phenotypes: appearance of 3 otoliths,
CC kidney cysts and dilated kidney tubules at 2.5 days post-fertilization
CC (dpf). Motile cilia in the kidney show disorganized cilia bundles with
CC either severely reduced beat amplitude or paralysis. Olfactory motile
CC cilia are nearly completely paralyzed. {ECO:0000269|PubMed:23891469}.
CC -!- SIMILARITY: Belongs to the ZMYND10 family. {ECO:0000305}.
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DR EMBL; FP245458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054130; AAH54130.1; -; mRNA.
DR RefSeq; NP_956691.1; NM_200397.1.
DR AlphaFoldDB; F1QN74; -.
DR SMR; F1QN74; -.
DR STRING; 7955.ENSDARP00000006141; -.
DR PaxDb; F1QN74; -.
DR PRIDE; F1QN74; -.
DR Ensembl; ENSDART00000017413; ENSDARP00000006141; ENSDARG00000002406.
DR GeneID; 393368; -.
DR KEGG; dre:393368; -.
DR CTD; 51364; -.
DR ZFIN; ZDB-GENE-040426-1218; zmynd10.
DR eggNOG; ENOG502QS3F; Eukaryota.
DR GeneTree; ENSGT00940000153820; -.
DR HOGENOM; CLU_034036_1_0_1; -.
DR InParanoid; F1QN74; -.
DR OMA; LIHEAYC; -.
DR OrthoDB; 685805at2759; -.
DR PhylomeDB; F1QN74; -.
DR TreeFam; TF324215; -.
DR PRO; PR:F1QN74; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000002406; Expressed in testis and 12 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036159; P:inner dynein arm assembly; ISS:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; ISS:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB.
DR GO; GO:1905505; P:positive regulation of motile cilium assembly; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..448
FT /note="Zinc finger MYND domain-containing protein 10"
FT /id="PRO_0000424816"
FT ZN_FING 394..430
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT CONFLICT 8
FT /note="E -> G (in Ref. 2; AAH54130)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="D -> E (in Ref. 2; AAH54130)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="I -> V (in Ref. 2; AAH54130)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="K -> I (in Ref. 2; AAH54130)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="S -> P (in Ref. 2; AAH54130)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="F -> S (in Ref. 2; AAH54130)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="P -> L (in Ref. 2; AAH54130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 51635 MW; 7464AB6C7B10EEB2 CRC64;
MDSVLLHEEA EGYIQSLEKM SLRDIGSPRW FRQHEFIEKL NMQAILNASA NQEEFIKDLF
VSLGKIPTLV HAMILTEVWK HKVFPKICKL QDFNPKSTFL LYMVIHHEAT IINLLETIMY
HKESSEAAGD CVLDLVDYCH RKLTLLVGRS VSGEISTQDR ITHTQISGTA SVQDLQKQSD
MLEFEISIKA LSVLCYITDH VESLSLSVLS RMLCTHNMPC VLVQLVENCP WKRGTQEKYT
EGKWRAVLPE DQLKLSKHDG QVWIALLNLM LKPDCQRKYD FNSFNKTQLL KLRGFLTDVV
IDQLPNLLDL KHFLSQLALT DPVAPKKDLI LEQLPEIWNN IVMENDKKWK AIAKYQVTNV
FNPSESELRE QASRLAQTYN LDVMENLIPD KPKCGACGRT GVKRCSRCQG EWYCNRECQV
KHWPKHKPSC NLMAEAFQKL QEEMKISS
