ZMY10_MOUSE
ID ZMY10_MOUSE Reviewed; 440 AA.
AC Q99ML0; Q3V1P0; Q80W73;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Zinc finger MYND domain-containing protein 10;
DE AltName: Full=Protein BLu;
GN Name=Zmynd10; Synonyms=Blu;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvImJ;
RA Dammann R., Pfeifer G.P.;
RT "A mouse locus containing the ortholog of the human RASSF1 tumor suppressor
RT gene.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29601588; DOI=10.1371/journal.pgen.1007316;
RA Cho K.J., Noh S.H., Han S.M., Choi W.I., Kim H.Y., Yu S., Lee J.S.,
RA Rim J.H., Lee M.G., Hildebrandt F., Gee H.Y.;
RT "ZMYND10 stabilizes intermediate chain proteins in the cytoplasmic pre-
RT assembly of dynein arms.";
RL PLoS Genet. 14:E1007316-E1007316(2018).
CC -!- FUNCTION: Plays a role in axonemal structure organization and motility
CC (PubMed:29601588). Involved in axonemal pre-assembly of inner and outer
CC dynein arms (IDA and ODA, respectively) for proper axoneme building for
CC cilia motility (PubMed:29601588). May act by indirectly regulating
CC transcription of dynein proteins (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:29601588}.
CC -!- SUBUNIT: Interacts (via C-terminus) with DNAAF11 (via CS domain); this
CC interaction stabilizes DNAAF11 at the protein level. Interacts (via C-
CC terminus) with DNAL1; this interaction stabilizes DNAL1 at the protein
CC level. Interacts with DNAAF4, HSPA8, IQUB, RUVBL2 and DYNTL5.
CC {ECO:0000250|UniProtKB:O75800}.
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:0000269|PubMed:29601588}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q5FWU8}.
CC -!- TISSUE SPECIFICITY: Expressed in the testis. Expressed in the tracheal
CC epithelium (PubMed:29601588). Restricted to regions containing motile
CC cilia (PubMed:23891471). {ECO:0000269|PubMed:23891471,
CC ECO:0000269|PubMed:29601588}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in the ciliated epithelial
CC layer associated with nasal and lung epithelium in 18.5 dpc embryos.
CC {ECO:0000269|PubMed:23891471}.
CC -!- DISRUPTION PHENOTYPE: Mice neonates exhibit growth retardation dying
CC within 1 month after birth. Show head deformation and situs invertus
CC (heart apex, stomach, liver or spleen). Display lung lobular structures
CC deterioration and collapsed alveolar spaces. Show mucosal congestion in
CC paranasal cavities. Show loss of ciliary motility and axonemal outer
CC and inner dynein arm (IDA and ODA, respectively) components without
CC disruption of ciliogenesis. {ECO:0000269|PubMed:29601588}.
CC -!- SIMILARITY: Belongs to the ZMYND10 family. {ECO:0000305}.
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DR EMBL; AF333027; AAK21199.1; -; Genomic_DNA.
DR EMBL; AK132332; BAE21110.1; -; mRNA.
DR EMBL; CH466560; EDL21195.1; -; Genomic_DNA.
DR EMBL; BC052357; AAH52357.1; -; mRNA.
DR CCDS; CCDS23493.1; -.
DR RefSeq; NP_444483.2; NM_053253.3.
DR AlphaFoldDB; Q99ML0; -.
DR SMR; Q99ML0; -.
DR BioGRID; 227760; 2.
DR STRING; 10090.ENSMUSP00000010188; -.
DR iPTMnet; Q99ML0; -.
DR PhosphoSitePlus; Q99ML0; -.
DR MaxQB; Q99ML0; -.
DR PaxDb; Q99ML0; -.
DR PRIDE; Q99ML0; -.
DR ProteomicsDB; 274997; -.
DR Antibodypedia; 30915; 186 antibodies from 27 providers.
DR DNASU; 114602; -.
DR Ensembl; ENSMUST00000010188; ENSMUSP00000010188; ENSMUSG00000010044.
DR GeneID; 114602; -.
DR KEGG; mmu:114602; -.
DR UCSC; uc009rlo.1; mouse.
DR CTD; 51364; -.
DR MGI; MGI:2387863; Zmynd10.
DR VEuPathDB; HostDB:ENSMUSG00000010044; -.
DR eggNOG; ENOG502QS3F; Eukaryota.
DR GeneTree; ENSGT00940000153820; -.
DR HOGENOM; CLU_034036_1_0_1; -.
DR InParanoid; Q99ML0; -.
DR OMA; LIHEAYC; -.
DR OrthoDB; 685805at2759; -.
DR PhylomeDB; Q99ML0; -.
DR TreeFam; TF324215; -.
DR BioGRID-ORCS; 114602; 5 hits in 73 CRISPR screens.
DR PRO; PR:Q99ML0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q99ML0; protein.
DR Bgee; ENSMUSG00000010044; Expressed in spermatocyte and 67 other tissues.
DR ExpressionAtlas; Q99ML0; baseline and differential.
DR Genevisible; Q99ML0; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:MGI.
DR GO; GO:0044183; F:protein folding chaperone; IMP:MGI.
DR GO; GO:0003341; P:cilium movement; IMP:MGI.
DR GO; GO:0036159; P:inner dynein arm assembly; IMP:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; IMP:MGI.
DR GO; GO:0036158; P:outer dynein arm assembly; IMP:UniProtKB.
DR GO; GO:1905505; P:positive regulation of motile cilium assembly; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IMP:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
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 membrane; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..440
FT /note="Zinc finger MYND domain-containing protein 10"
FT /id="PRO_0000218315"
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 63
FT /note="I -> V (in Ref. 1; AAK21199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 50646 MW; A9449F82B3050CEA CRC64;
MGDLELLLPG EAEVLVRGLR SFQLREMGSE GWNKQHESLE KLNMQAILDA TISQAEPIQE
LLINHGKIPT LVEELIAVEM WKQKVFPVLC RLEDFKPQNT FPIYMVVHHE ASIINLLETV
FFHKEVCESA DDKVLDLVDY CHRKLILLVA RKGGGDLSEE EQFQDSTPMQ ELQKQAEMME
FEISLKALSV LRYITDCVDS LSLSTLNRML RTHNLPCLLV ELLEHSPWSR RVGGKLQHFE
SGRWQTVAPS EQQKLNKLDG QVWIALYNLL LSPEARARYC LTSFAKGQLL KLQAFLTDTL
LDQLPNLADL KGFLAHLSLA ETQPPKKDLV LEQIPEIWDR LERENKGKWQ AIAKHQLQHV
FSLSEKDLRQ QAQRWAETYR LDVLEAVAPE RPRCGYCNAE ASKRCSRCQN VWYCCRECQV
KHWEKHGKTC VLAAQGDRAK
