ODAD3_MOUSE
ID ODAD3_MOUSE Reviewed; 593 AA.
AC Q8BSN3; G3X951; Q6PGE8; Q9CWC6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Outer dynein arm-docking complex subunit 3;
DE AltName: Full=Coiled-coil domain-containing protein 151;
GN Name=ODAD3; Synonyms=Ccdc151;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Fetal forelimb;
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] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=25192045; DOI=10.1016/j.ajhg.2014.08.005;
RG UK10K Consortium;
RA Hjeij R., Onoufriadis A., Watson C.M., Slagle C.E., Klena N.T.,
RA Dougherty G.W., Kurkowiak M., Loges N.T., Diggle C.P., Morante N.F.,
RA Gabriel G.C., Lemke K.L., Li Y., Pennekamp P., Menchen T., Konert F.,
RA Marthin J.K., Mans D.A., Letteboer S.J., Werner C., Burgoyne T.,
RA Westermann C., Rutman A., Carr I.M., O'Callaghan C., Moya E., Chung E.M.,
RA Sheridan E., Nielsen K.G., Roepman R., Bartscherer K., Burdine R.D.,
RA Lo C.W., Omran H., Mitchison H.M.;
RT "CCDC151 mutations cause primary ciliary dyskinesia by disruption of the
RT outer dynein arm docking complex formation.";
RL Am. J. Hum. Genet. 95:257-274(2014).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24067530; DOI=10.1093/hmg/ddt445;
RA Jerber J., Baas D., Soulavie F., Chhin B., Cortier E., Vesque C.,
RA Thomas J., Durand B.;
RT "The coiled-coil domain containing protein CCDC151 is required for the
RT function of IFT-dependent motile cilia in animals.";
RL Hum. Mol. Genet. 23:563-577(2014).
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. Involved in mediating assembly of both ODAs and their
CC axonemal docking complex onto ciliary microtubules (By similarity). May
CC be required for motile cilia function (PubMed:24067530).
CC {ECO:0000250|UniProtKB:A5D8V7, ECO:0000269|PubMed:24067530}.
CC -!- SUBUNIT: Component of the outer dynein arm-docking complex along with
CC ODAD1, ODAD2, ODAD4 and CLXN (By similarity). Interacts with ODAD1 (By
CC similarity). Interacts with PIERCE1 and PIERCE2; the interactions link
CC the outer dynein arms docking complex (ODA-DC) to the internal
CC microtubule inner proteins (MIP) in cilium axoneme (By similarity).
CC {ECO:0000250|UniProtKB:A5D8V7, ECO:0000250|UniProtKB:A7MBH5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:24067530}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:24067530}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:24067530}. Note=Enriched at centrioles in IMCD3
CC dividing cells. {ECO:0000269|PubMed:24067530}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BSN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BSN3-2; Sequence=VSP_031786, VSP_031787;
CC Name=3;
CC IsoId=Q8BSN3-3; Sequence=VSP_031788;
CC -!- DEVELOPMENTAL STAGE: At 7.5 dpc specifically expressed in the ventral
CC node. {ECO:0000269|PubMed:25192045}.
CC -!- DISRUPTION PHENOTYPE: Mice have a spectrum of laterality defects,
CC including complex congenital heart defects associated with heterotaxy,
CC and airway epithelia show largely immotile cilia with loss of the outer
CC dynein arms. {ECO:0000269|PubMed:25192045}.
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DR EMBL; AK021166; BAB32312.1; -; mRNA.
DR EMBL; AK031175; BAC27290.1; -; mRNA.
DR EMBL; AC163623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057069; AAH57069.2; -; mRNA.
DR CCDS; CCDS22917.1; -. [Q8BSN3-1]
DR CCDS; CCDS52740.1; -. [Q8BSN3-3]
DR RefSeq; NP_001157259.1; NM_001163787.1. [Q8BSN3-3]
DR RefSeq; NP_084215.2; NM_029939.3. [Q8BSN3-1]
DR RefSeq; XP_006510748.1; XM_006510685.2. [Q8BSN3-3]
DR AlphaFoldDB; Q8BSN3; -.
DR SMR; Q8BSN3; -.
DR BioGRID; 218795; 2.
DR STRING; 10090.ENSMUSP00000110993; -.
DR iPTMnet; Q8BSN3; -.
DR PhosphoSitePlus; Q8BSN3; -.
DR MaxQB; Q8BSN3; -.
DR PaxDb; Q8BSN3; -.
DR PRIDE; Q8BSN3; -.
DR ProteomicsDB; 265289; -. [Q8BSN3-1]
DR ProteomicsDB; 265290; -. [Q8BSN3-2]
DR ProteomicsDB; 265291; -. [Q8BSN3-3]
DR ProteomicsDB; 337162; -.
DR Antibodypedia; 25849; 80 antibodies from 17 providers.
DR DNASU; 77609; -.
DR Ensembl; ENSMUST00000044926; ENSMUSP00000041117; ENSMUSG00000039632. [Q8BSN3-1]
DR Ensembl; ENSMUST00000115336; ENSMUSP00000110993; ENSMUSG00000039632. [Q8BSN3-3]
DR GeneID; 77609; -.
DR KEGG; mmu:77609; -.
DR UCSC; uc009onh.1; mouse. [Q8BSN3-2]
DR UCSC; uc012gpk.1; mouse. [Q8BSN3-3]
DR CTD; 115948; -.
DR MGI; MGI:1924859; Odad3.
DR VEuPathDB; HostDB:ENSMUSG00000039632; -.
DR eggNOG; ENOG502QR7A; Eukaryota.
DR GeneTree; ENSGT00940000153116; -.
DR HOGENOM; CLU_033878_0_0_1; -.
DR InParanoid; Q8BSN3; -.
DR OMA; QPMPVCY; -.
DR OrthoDB; 969618at2759; -.
DR PhylomeDB; Q8BSN3; -.
DR TreeFam; TF324955; -.
DR BioGRID-ORCS; 77609; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8BSN3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BSN3; protein.
DR Bgee; ENSMUSG00000039632; Expressed in seminiferous tubule of testis and 88 other tissues.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0035253; C:ciliary rootlet; IBA:GO_Central.
DR GO; GO:0097542; C:ciliary tip; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0120228; C:outer dynein arm docking complex; ISS:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0036158; P:outer dynein arm assembly; IMP:UniProtKB.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR InterPro; IPR033192; ODAD3.
DR PANTHER; PTHR46518; PTHR46518; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..593
FT /note="Outer dynein arm-docking complex subunit 3"
FT /id="PRO_0000321527"
FT REGION 10..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 84..317
FT /evidence="ECO:0000255"
FT COILED 378..449
FT /evidence="ECO:0000255"
FT VAR_SEQ 144..166
FT /note="QALEHLEHQLREKMNQLNALRHQ -> VSPAITIPPFPPHWTFSFPELSL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031786"
FT VAR_SEQ 167..593
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031787"
FT VAR_SEQ 317
FT /note="K -> KQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031788"
FT CONFLICT 47
FT /note="H -> R (in Ref. 1; BAB32312/BAC27290 and 3;
FT AAH57069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 69713 MW; 665214C1C8555302 CRC64;
MTSPLCWAAA TTTVTSPEQA PAPSSKAKGS KVHRSKSMGR AQAWPAHHPK SATSFHAMKS
SVHAQVLELQ RKIQLLEGDR KAFYESSQWN MKKNQDTINQ LQEETKALHV QLKDLLQGDS
KVIQAIIQEW KSEKPFLKNR TCEQALEHLE HQLREKMNQL NALRHQVILR QKRLEDLRLQ
HSLRQLEMAE VQDSNMEAAK TMRNLENRLE KARMKAEEAE HITNVYLQLK SYLQEESLNL
ESRLDSMEAE VMNTKHEVQE LKVVNQEAIN ARDIAKNQLQ YLEESAIRDR KKREHYITDC
KKRAEEKKLQ TERMERKTHR DHVLLQSEDT IQDHQRHREE ELRQRWSMYQ MEVMFGKVKD
ATGVAESHAV VRRFLAQDET FTQLENLKKD NELALAKLKE EKQRLQRELE NLKYSGDATL
VSQRRLHEEM QKTFKKEEQR HNDVHERLEH TSRILQLVKD CLEHLANKLS HVKLDDTVLA
GKKLDRDSED YAYNLLVVVQ EKLLKLQDQL ESQDVPELLR HIADREFLAT LEGKLPLYNT
RILLPVASVK DKFFDEEESE DDDRDVVTRA AFKLRSQKLI EARSKKRNRL RRS
