ZMY10_XENLA
ID ZMY10_XENLA Reviewed; 439 AA.
AC Q5FWU8;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Zinc finger MYND domain-containing protein 10;
GN Name=zmynd10;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=30561330; DOI=10.7554/elife.38497;
RA Huizar R.L., Lee C., Boulgakov A.A., Horani A., Tu F., Marcotte E.M.,
RA Brody S.L., Wallingford J.B.;
RT "A liquid-like organelle at the root of motile ciliopathy.";
RL Elife 7:0-0(2018).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=33263282; DOI=10.7554/elife.58662;
RA Lee C., Cox R.M., Papoulas O., Horani A., Drew K., Devitt C.C., Brody S.L.,
RA Marcotte E.M., Wallingford J.B.;
RT "Functional partitioning of a liquid-like organelle during assembly of
RT axonemal dyneins.";
RL Elife 9:0-0(2020).
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:0000269|PubMed:23891469}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:23891469}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000250|UniProtKB:Q6AXZ5}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q99ML0}. Dynein axonemal particle
CC {ECO:0000269|PubMed:30561330, ECO:0000269|PubMed:33263282}.
CC Note=Localizes both to the basal body and the striated rootlet, an
CC appendage that projects away from the basal body into the cytoplasm.
CC -!- DISRUPTION PHENOTYPE: Ciliopathy phenotypes. Although a large
CC percentage of cells fail to generate cilia because of a substantial
CC defect in ciliogenesis, the numbers of centrioles is apparently normal.
CC {ECO:0000269|PubMed:23891469}.
CC -!- SIMILARITY: Belongs to the ZMYND10 family. {ECO:0000305}.
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; BC089198; AAH89198.1; -; mRNA.
DR RefSeq; NP_001090272.2; NM_001096803.1.
DR AlphaFoldDB; Q5FWU8; -.
DR SMR; Q5FWU8; -.
DR PRIDE; Q5FWU8; -.
DR DNASU; 779178; -.
DR GeneID; 779178; -.
DR KEGG; xla:779178; -.
DR CTD; 779178; -.
DR Xenbase; XB-GENE-961073; zmynd10.L.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 779178; Expressed in testis and 15 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0120293; C:dynein axonemal particle; IDA: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; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Membrane;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..439
FT /note="Zinc finger MYND domain-containing protein 10"
FT /id="PRO_0000424817"
FT ZN_FING 385..421
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 439 AA; 50780 MW; A9B3359CC8429AF1 CRC64;
MVQSLQTFSV RDIASGGWFK QHEYIEKLNM QAILNASAGQ EEMIKDLLVT HGKIPTLIHE
LISVEIWKLK VFHVLCQLQD FQPKSTFPLY MVIHHEATII NLLETIFFHK EVCESAEDLT
LDLIDYCYRK LTLLASQSSD RRTLSQNRLL PHTANEASSL EELKQQAEAL EFDIALKCLS
VTRYISDHID SLPLSVMNRL LNTHNLPCLL VELLHQSPWT QSEKGQLQKY ESGRWYPVPA
EDQLKMTKLD GQAWIALYNL LLRPECQQKY NINSFTKGQL LKLRSFLTEV LLDQLPNLVD
LQRFLSHLSV SEPTPPKKEL ILEQVPEVWD SIINENSGKW KAIAKYQVKQ AFSPSEEDLR
SQAKRWAQTY NMDVMEALVP EKPKCGSCGS EASKRCSRCQ SEWYCKRECQ VKHWQKHKKA
CDMVSEAMKN MQEEIQKEA
