ODAD4_MOUSE
ID ODAD4_MOUSE Reviewed; 624 AA.
AC Q9D4B2; A2BI62; Q80X58;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 139.
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 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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 [4]
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 [5]
RP INTERACTION WITH COMPONENTS OF THE IFT A AND B COMPLEXES, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=25860617; DOI=10.1371/journal.pone.0124378;
RA Xu Y., Cao J., Huang S., Feng D., Zhang W., Zhu X., Yan X.;
RT "Characterization of tetratricopeptide repeat-containing proteins critical
RT for cilia formation and function.";
RL PLoS ONE 10:E0124378-E0124378(2015).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, 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 for
CC the docking of ODA in ciliary axoneme. {ECO:0000269|PubMed:27486780}.
CC -!- SUBUNIT: Component of the outer dynein arm-docking complex along with
CC ODAD1, ODAD2, and ODAD3 (By similarity). Interacts with ODAD1; this
CC interaction may facilitate the recruitment and/or attachment of outer
CC dynein arm docking complex proteins, including ODAD1, ODAD3 and ODAD2,
CC to ciliary axonemes (By similarity). Interacts with components of the
CC IFT complex A, including IFT140, TTC21B/IFT139 and WDR19/IFT144, and
CC the IFT complex B, including IFT46, IFT52 and IFT57 (PubMed:25860617).
CC {ECO:0000250|UniProtKB:Q96NG3, ECO:0000269|PubMed:25860617}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:25860617}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q96NG3}.
CC -!- DEVELOPMENTAL STAGE: At 7.5 dpc, strong expression restricted to the
CC ventral node, the left-right organizer (PubMed:27486780). Up-regulated
CC in tracheal epithelial cells during in vitro differentiation into
CC multiciliated cells (PubMed:25860617). {ECO:0000269|PubMed:25860617,
CC ECO:0000269|PubMed:27486780}.
CC -!- DISRUPTION PHENOTYPE: Heterozygous intercrosses reveal deviation from
CC the Mendelian distribution, with only 6 homozygous out of 53 born mice,
CC suggesting increased death in utero. Most surviving homozygous mice
CC present with small body size, some with hydrocephalus at the age of 2
CC weeks. They display a variety of left-right body asymmetry defects,
CC including reversal of lung lobation or dextrocardia. At the cell level,
CC the trachea and fallopian tubes of mutant animals show absence of outer
CC dynein arms from the ciliary axonemes, and consequently severe
CC reduction of cilia beating. There is no evidence of short cilia or a
CC reduction in cilia number. {ECO:0000269|PubMed:27486780}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50805.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK016657; BAB30363.1; -; mRNA.
DR EMBL; BX842667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050805; AAH50805.2; ALT_FRAME; mRNA.
DR CCDS; CCDS36331.1; -.
DR RefSeq; NP_083194.2; NM_028918.2.
DR AlphaFoldDB; Q9D4B2; -.
DR SMR; Q9D4B2; -.
DR BioGRID; 216725; 2.
DR STRING; 10090.ENSMUSP00000090355; -.
DR iPTMnet; Q9D4B2; -.
DR PhosphoSitePlus; Q9D4B2; -.
DR MaxQB; Q9D4B2; -.
DR PaxDb; Q9D4B2; -.
DR PRIDE; Q9D4B2; -.
DR ProteomicsDB; 300149; -.
DR Antibodypedia; 8054; 18 antibodies from 11 providers.
DR Ensembl; ENSMUST00000092684; ENSMUSP00000090355; ENSMUSG00000006784.
DR GeneID; 74407; -.
DR KEGG; mmu:74407; -.
DR UCSC; uc007lln.1; mouse.
DR CTD; 83538; -.
DR MGI; MGI:1921657; Odad4.
DR VEuPathDB; HostDB:ENSMUSG00000006784; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00390000007911; -.
DR InParanoid; Q9D4B2; -.
DR OMA; WDHIEDE; -.
DR OrthoDB; 1417967at2759; -.
DR PhylomeDB; Q9D4B2; -.
DR TreeFam; TF323661; -.
DR BioGRID-ORCS; 74407; 5 hits in 70 CRISPR screens.
DR PRO; PR:Q9D4B2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D4B2; protein.
DR Bgee; ENSMUSG00000006784; Expressed in seminiferous tubule of testis and 98 other tissues.
DR ExpressionAtlas; Q9D4B2; baseline and differential.
DR Genevisible; Q9D4B2; MM.
DR GO; GO:0097728; C:9+0 motile cilium; IDA:MGI.
DR GO; GO:0097729; C:9+2 motile cilium; IDA:MGI.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0120228; C:outer dynein arm docking complex; ISO:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0090660; P:cerebrospinal fluid circulation; IMP:MGI.
DR GO; GO:0003341; P:cilium movement; ISS:UniProtKB.
DR GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0120197; P:mucociliary clearance; ISO:MGI.
DR GO; GO:0036158; P:outer dynein arm assembly; IMP:MGI.
DR GO; GO:0120229; P:protein localization to motile cilium; ISO:MGI.
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; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Cytoskeleton; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..624
FT /note="Outer dynein arm-docking complex subunit 4"
FT /id="PRO_0000284508"
FT REPEAT 11..44
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 46..78
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 79..112
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 273..309
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 318..351
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 358..391
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 395..428
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REPEAT 435..468
FT /note="TPR 8"
FT /evidence="ECO:0000255"
FT REGION 511..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 123
FT /note="E -> K (in Ref. 1; BAB30363)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="E -> D (in Ref. 1; BAB30363)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="E -> K (in Ref. 1; BAB30363)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="K -> E (in Ref. 1; BAB30363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 624 AA; 71530 MW; 0E8D9B701545FA19 CRC64;
MSDGDILRST FPSYMAEGER LYLCGEFTKA IQSFTNALHL QSGDKNCLVA RSKCYLKMGD
LEKSLNDAEA SLRNDPTFCK GILQKAETLY TMGDFEFALV FYHRGYKLRP DREFKVGIQK
AQEAINNSVG SPSSIKLENK GDLSFLSKQA ESKKAQQKHL PIKQLSYSTK HEIKRKGSLK
SEKTVRQLLG ELYVDKEYLE KLLLDEDLIK GTIKSGLTVE DLIMTGINYL DTRSNFWRQQ
KPIYARERDR KLMQEKWLRD RKRSPSQTAH YILKSLEDID MLLTSGSADG SLQKAEKVLK
KVLEWNQEEV PNKDELVGNL YSCIGNAQIE LGQMVAALQS HRKDLEIAKE HDLPDAKSRA
LDNIGRVFAR VGKFQQAIDT WEEKIPLAKT TLEKTWLFHE IGRCYLELDQ AWQAQSYGEK
SQQYAEEEGD LEWQLNASVL VAQAQVKLRD FESAVNNFEK ALERAKLVHN NEAQQAIISA
LDDANKGIIE ELKKTNYREI LREKAERQDI MSQMDLQGAS EKEPLRGREE QERVVKQWER
DQESEREATD DEQDRKSSGG LSKKLLGDGH SSNLGIRRES REIYRRLSDY SSHLPSEDGS
QKQEKKQAEA AKGEVQKLEK TKEE
