ODAD1_BOVIN
ID ODAD1_BOVIN Reviewed; 687 AA.
AC F1N2N9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 3.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Outer dynein arm-docking complex subunit 1;
GN Name=ODAD1; Synonyms=CCDC114 {ECO:0000303|PubMed:34715025};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000312|Proteomes:UP000009136};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:7RRO}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBUNIT, FUNCTION,
RP INTERACTION WITH PIERCE1 AND PIERCE2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=34715025; DOI=10.1016/j.cell.2021.10.007;
RA Gui M., Farley H., Anujan P., Anderson J.R., Maxwell D.W., Whitchurch J.B.,
RA Botsch J.J., Qiu T., Meleppattu S., Singh S.K., Zhang Q., Thompson J.,
RA Lucas J.S., Bingle C.D., Norris D.P., Roy S., Brown A.;
RT "De novo identification of mammalian ciliary motility proteins using cryo-
RT EM.";
RL Cell 184:5791-5806.e19(2021).
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.
CC {ECO:0000269|PubMed:34715025}.
CC -!- SUBUNIT: Component of the outer dynein arm-docking complex along with
CC ODAD2, ODAD3, ODAD4 and CLXN. Interacts with ODAD3. Interacts with
CC ODAD4; this interaction may facilitate the recruitment and/or
CC attachment of outer dynein arm docking complex proteins, including
CC ODAD1, ODAD3, and ODAD4 to ciliary axonemes. Interacts with DNAH9.
CC Interacts with MNS1 (PubMed:34715025). Interacts with PIERCE1 and
CC PIERCE2; the interactions link the outer dynein arms docking complex
CC (ODA-DC) to the internal microtubule inner proteins (MIP) in cilium
CC axoneme (PubMed:34715025). {ECO:0000269|PubMed:34715025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:34715025}.
CC -!- TISSUE SPECIFICITY: Expressed in trachea multiciliated cells.
CC {ECO:0000269|PubMed:34715025}.
CC -!- SIMILARITY: Belongs to the ODA1/DCC2 family. {ECO:0000305}.
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DR PDB; 7RRO; EM; 3.40 A; H1/H2/H3=1-687.
DR PDBsum; 7RRO; -.
DR SMR; F1N2N9; -.
DR STRING; 9913.ENSBTAP00000040922; -.
DR PaxDb; F1N2N9; -.
DR PRIDE; F1N2N9; -.
DR Ensembl; ENSBTAT00000043347; ENSBTAP00000040922; ENSBTAG00000030667.
DR VEuPathDB; HostDB:ENSBTAG00000030667; -.
DR VGNC; VGNC:26836; ODAD1.
DR eggNOG; ENOG502QSIU; Eukaryota.
DR GeneTree; ENSGT00950000183364; -.
DR HOGENOM; CLU_027546_3_1_1; -.
DR InParanoid; F1N2N9; -.
DR OMA; HCDGSMI; -.
DR TreeFam; TF323742; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000030667; Expressed in olfactory segment of nasal mucosa and 101 other tissues.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0120228; C:outer dynein arm docking complex; IDA:UniProtKB.
DR GO; GO:0003341; P:cilium movement; IDA:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..687
FT /note="Outer dynein arm-docking complex subunit 1"
FT /id="PRO_0000455518"
FT REGION 126..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..193
FT /evidence="ECO:0000255"
FT COILED 222..267
FT /evidence="ECO:0000255"
FT COILED 341..421
FT /evidence="ECO:0000255"
FT COMPBIAS 540..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 77563 MW; 3BC3187BC344C28F CRC64;
MPFGLSAGST RSEDGSEAFL EGMVDWELSR LQRQCKVMED ERRAYSKEVH QRINKQLEEI
QRLEGVRHKL RVQISIAQSQ VRRLRDSERL ESMGHLLKCQ VRVQAEVKEL QAQNQALDRE
IQEWESRNSA HSKNARSPGC VQHDKVKSQR RIKSLENQLD KVICRFDIQL AQNATLREEL
DLLRIERNRY LNVDRKLQKE IQLLKDSVRN LMVSSTSAYT VREEAKAKLG MLRERAEKEV
AQNETEVQIL QRQIAHLEQL HHFLKLKNGD RQPDSAIVEK REQRAREVAE GLRKTSQEKL
VLRYEDALNK LSQMTGESDP DLLVEKYLEL EERNFAEFNF INEQNSELEH LQEEIKEMQE
ALVSGRRSEE DRRAQQEQQR AELQQRVDDV HSEADDLEAR YHNFREQLEK LKTNIQHLFT
RAQCDSTLIN DLLGIKTHMR DRDISLFLSL IEKRLVQLLT VQAFLETQVV VMFNAALMVL
GQSSEDFPKK VAPPQPPDNL EDPPGFEAKD DYPLSKEELL SSVMKAEQHL KELVESIKVE
STPSMTSSTQ KVSSSSRLVT QRPSQVPGSI MSHRTSGILV SSGGRATSSN VGHVTFGDSS
ATTGGLMSSR GSIPGRVTFR SPNSSSYLGS TGYVGSSRDH DSFEASKGPG SESSGGLGSS
PGPASSPGPA SSTGQASSTS KDSQSNY
