ODAD1_RAT
ID ODAD1_RAT Reviewed; 694 AA.
AC B1H228;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Outer dynein arm-docking complex subunit 1;
DE AltName: Full=Coiled-coil domain-containing protein 114;
GN Name=Odad1; Synonyms=Ccdc114;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536; SER-542; SER-543 AND
RP SER-545, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the outer dynein arm-docking complex that
CC mediates outer dynein arms (ODA) binding onto the doublet microtubule.
CC Involved in mediating assembly of both ODAs and their axonemal docking
CC complex onto ciliary microtubules (By similarity).
CC {ECO:0000250|UniProtKB:F1N2N9, ECO:0000250|UniProtKB:Q96M63}.
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 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:F1N2N9,
CC ECO:0000250|UniProtKB:Q96M63}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q96M63}.
CC -!- SIMILARITY: Belongs to the ODA1/DCC2 family. {ECO:0000305}.
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DR EMBL; BC160835; AAI60835.1; -; mRNA.
DR RefSeq; NP_001119749.1; NM_001126277.2.
DR RefSeq; XP_008757609.1; XM_008759387.2.
DR RefSeq; XP_008757610.1; XM_008759388.2.
DR AlphaFoldDB; B1H228; -.
DR SMR; B1H228; -.
DR STRING; 10116.ENSRNOP00000028662; -.
DR iPTMnet; B1H228; -.
DR PhosphoSitePlus; B1H228; -.
DR PaxDb; B1H228; -.
DR PRIDE; B1H228; -.
DR GeneID; 308594; -.
DR KEGG; rno:308594; -.
DR UCSC; RGD:1308141; rat.
DR CTD; 93233; -.
DR RGD; 1308141; Ccdc114.
DR VEuPathDB; HostDB:ENSRNOG00000021109; -.
DR eggNOG; ENOG502QSIU; Eukaryota.
DR HOGENOM; CLU_027546_3_1_1; -.
DR InParanoid; B1H228; -.
DR OMA; HCDGSMI; -.
DR OrthoDB; 648380at2759; -.
DR PhylomeDB; B1H228; -.
DR TreeFam; TF323742; -.
DR PRO; PR:B1H228; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021109; Expressed in testis and 10 other tissues.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0036157; C:outer dynein arm; ISS:UniProtKB.
DR GO; GO:0120228; C:outer dynein arm docking complex; ISS:UniProtKB.
DR GO; GO:0003341; P:cilium movement; ISS:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..694
FT /note="Outer dynein arm-docking complex subunit 1"
FT /id="PRO_0000360998"
FT REGION 271..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..192
FT /evidence="ECO:0000255"
FT COILED 222..259
FT /evidence="ECO:0000255"
FT COILED 339..418
FT /evidence="ECO:0000255"
FT COMPBIAS 578..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 694 AA; 78170 MW; EA0A74DB239B90C4 CRC64;
MRLGLSSRSA RSEEGSEIFL EGPVDGELSR LHRQRKVMEL ERRAYSREVH QRIRKQVEEI
RQLEMLRAKL QMQINVAQTQ VKRLGDKKRL ADMDHLLKCR AQVQIEIEAL QEQNRALEKQ
IQDWETHILT QSKDISTPDV ILDQKMKIQR RIRILEDQLD RVTCHFDIHL VRNAALREEL
ELLRIERGRY LNMDRKLKKE IHLLQEMVGA LSTSSTSAYT AREEAKTKMG MLQERAEKEL
AQSDTEAQIL LRQISHLEQL HRFLKLKNHD RQPDPGVVQK EEQRAWETSE GLRKTSQEKL
VLRYEDTLNK LAQLTGESDP DLLVEKYLEL EERNFAEFNF INEQNSELYH LQEEIKEMQE
ALVSEHASQD KQSLEREQQC KVLQQDVEKV CSESERLEAR FQVLRVQLEK IKTDIQVLFD
KAQCDNSVIK DLLGVKTYMR DRDIGLFLST IEKRLVQLLT VQAFLEVQNN VPLADAALLA
LGQSIQEPPK KTTPLKPPDT MEDSSGVVIK DDYPMSKEEL LSQVMKLVQL QDEEGSPKKR
DSSPSLTLSS PRISLAAASV HARKASVVPE SILSHKTGRG RGTGSISHVT FGDSASAPGP
VTLASTSASG LPVSGRGSQG GRGAFKHTSS SSYLGSTGYL ETSRGRESGT GGGHSQSMGS
EMSRGFSSGS GQTSSAAPAS RPSSATSKDS RGYN
