ODAD4_XENLA
ID ODAD4_XENLA Reviewed; 531 AA.
AC Q32NU8; Q6NTM4;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Outer dynein arm-docking complex subunit 4;
DE AltName: Full=Tetratricopeptide repeat protein 25;
DE Short=TPR repeat protein 25;
GN Name=odad4; Synonyms=ttc25;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17961536; DOI=10.1016/j.ydbio.2007.09.031;
RA Hayes J.M., Kim S.K., Abitua P.B., Park T.J., Herrington E.R., Kitayama A.,
RA Grow M.W., Ueno N., Wallingford J.B.;
RT "Identification of novel ciliogenesis factors using a new in vivo model for
RT mucociliary epithelial development.";
RL Dev. Biol. 312:115-130(2007).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27486780; DOI=10.1016/j.ajhg.2016.06.014;
RA Wallmeier J., Shiratori H., Dougherty G.W., Edelbusch C., Hjeij R.,
RA Loges N.T., Menchen T., Olbrich H., Pennekamp P., Raidt J., Werner C.,
RA Minegishi K., Shinohara K., Asai Y., Takaoka K., Lee C., Griese M.,
RA Memari Y., Durbin R., Kolb-Kokocinski A., Sauer S., Wallingford J.B.,
RA Hamada H., Omran H.;
RT "TTC25 deficiency results in defects of the outer dynein arm docking
RT machinery and primary ciliary dyskinesia with left-right body asymmetry
RT randomization.";
RL Am. J. Hum. Genet. 99:460-469(2016).
CC -!- FUNCTION: Component of the outer dynein arm-docking complex (ODA-DC)
CC that mediates outer dynein arms (ODA) binding onto the doublet
CC microtubule. Plays an essential role for the assembly of ODA-DC and in
CC the docking of ODA in ciliary axoneme. {ECO:0000250|UniProtKB:Q96NG3}.
CC -!- FUNCTION: Required for the docking of the outer dynein arm to cilia,
CC hence plays an essential role in cilia motility.
CC {ECO:0000269|PubMed:27486780}.
CC -!- SUBUNIT: Component of the outer dynein arm-docking complex.
CC {ECO:0000250|UniProtKB:Q96NG3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:17961536}. Note=In addition to ciliary axonemes,
CC also detected in foci, presumably basal bodies, at the apical cell
CC surface. {ECO:0000269|PubMed:17961536}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q32NU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q32NU8-2; Sequence=VSP_024550;
CC -!- TISSUE SPECIFICITY: In the mucociliary epithelium, specifically
CC expressed in ciliated cells. {ECO:0000269|PubMed:17961536}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the ventral midline of the developing
CC neural plate during neural tube closure. {ECO:0000269|PubMed:17961536}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC disruption of the neural tube closure (PubMed:17961536). Morphants show
CC defects in ciliogenesis at early stages of embryonic development
CC (PubMed:17961536, PubMed:27486780). More mature multiciliated cells
CC display normal cilium length, but exhibit severe defects in ciliary
CC beating, retaining only a twitching motility, but no organized beating.
CC Outer dynein arms are absent in morphant axonemes (PubMed:27486780).
CC {ECO:0000269|PubMed:17961536, ECO:0000269|PubMed:27486780}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH68935.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC108468; AAI08469.1; -; mRNA.
DR EMBL; BC068935; AAH68935.1; ALT_INIT; mRNA.
DR RefSeq; NP_001084612.2; NM_001091143.2.
DR AlphaFoldDB; Q32NU8; -.
DR SMR; Q32NU8; -.
DR DNASU; 414568; -.
DR GeneID; 414568; -.
DR KEGG; xla:414568; -.
DR CTD; 414568; -.
DR Xenbase; XB-GENE-5960311; odad4.L.
DR OrthoDB; 1417967at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 414568; Expressed in testis and 16 other tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0003341; P:cilium movement; ISS:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR040111; ODAD4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR23040; PTHR23040; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..531
FT /note="Outer dynein arm-docking complex subunit 4"
FT /id="PRO_0000284510"
FT REPEAT 15..48
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 50..82
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 83..116
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 275..307
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 320..353
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 360..393
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 397..430
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REPEAT 437..470
FT /note="TPR 8"
FT /evidence="ECO:0000255"
FT REGION 161..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 515
FT /note="D -> DEE (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_024550"
FT CONFLICT 74
FT /note="A -> T (in Ref. 1; AAH68935)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="D -> N (in Ref. 1; AAH68935)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 60954 MW; F55A238D0427D446 CRC64;
MAEETDEQQA PQSTFSTYMA EGEQLYHKAE YKKASDSFTA ALQLQPEEKN CLVARSKCFL
KLGEPECALK DAEASLQIEN DFFKGLYQKA EALYAMGDFE FALVHYHRGY KLRPEFQGFR
LGIQKAQEAI ENSVGTPASV KLENKTDLQF ISRQEESKKA KQKAQVKVQK KDSKQQKKVD
PERSQKTVRQ LLGELYSDKE YLESLLRDEA LVKGNTRGGV KLHDLIINGI LYLDTRSEFW
RQQKPIYARQ RDRKIMQQKW KRDKNKSADP SQYIVKSLEE IDQLLSSGKA EESYKKAQLV
LKKVERWTSV DIHNREELTG SLHSCIGNAQ MDMGQIEAAL QSHKKDLAIA EKYKLLEAKS
RALDNIGRVY ARIGKFNEAI KVWEEKIPLA NSSLEKTWLY HEIGRCYLEL EQTAEAKEYG
EKSQQEADAA EDIEWQLNAC VLLAQAEVKL KHYQSAISSF ENALERARLL HNKDAEQAIL
VALEDAKQGM EEQQESEQNN DENDNLRADG NTARDEEEED VHVQRTEEDE G
