ID DAA11_XENLA Reviewed; 469 AA. AC A0A1L8G016; DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2017, sequence version 1. DT 08-NOV-2023, entry version 19. DE RecName: Full=Dynein axonemal assembly factor 11 {ECO:0000305}; DE Short=DNAAF11 {ECO:0000305}; DE AltName: Full=Leucine-rich repeat-containing protein 6; DE AltName: Full=Protein tilB homolog; GN Name=dnaaf11; Synonyms=lrrc6; GN ORFNames=XELAEV_18032374mg {ECO:0000312|EMBL:OCT77178.1}; 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 {ECO:0000312|EMBL:OCT77178.1}; RN [1] {ECO:0000312|Proteomes:UP000186698} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J {ECO:0000312|Proteomes:UP000186698}; RX PubMed=27762356; DOI=10.1038/nature19840; RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S., RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I., RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O., RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M., RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I., RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J., RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y., RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J., RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V., RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W., RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M., RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J., RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.; RT "Genome evolution in the allotetraploid frog Xenopus laevis."; RL Nature 538:336-343(2016). RN [2] RP SUBCELLULAR LOCATION. RX PubMed=30561330; DOI=10.7554/elife.38497; RA Huizar R.L., Lee C., Boulgakov A.A., Horani A., Tu F., Marcotte E.M., RA Brody S.L., Wallingford J.B.; RT "A liquid-like organelle at the root of motile ciliopathy."; RL Elife 7:0-0(2018). RN [3] RP SUBCELLULAR LOCATION. RX PubMed=33263282; DOI=10.7554/elife.58662; RA Lee C., Cox R.M., Papoulas O., Horani A., Drew K., Devitt C.C., Brody S.L., RA Marcotte E.M., Wallingford J.B.; RT "Functional partitioning of a liquid-like organelle during assembly of RT axonemal dyneins."; RL Elife 9:0-0(2020). CC -!- FUNCTION: Involved in dynein arm assembly, is important for expression CC and transporting outer dynein arm (ODA) proteins from the cytoplasm to CC the cilia. {ECO:0000250|UniProtKB:Q86X45}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86X45}. Cell CC projection, cilium {ECO:0000250|UniProtKB:Q86X45}. Dynein axonemal CC particle {ECO:0000269|PubMed:33263282}. Cell projection, cilium, CC flagellum {ECO:0000250|UniProtKB:Q86X45}. Note=Localized to cytoplasmic CC puncta in ciliated cells. In the semicircular canal, localized to CC kinocilia (By similarity). {ECO:0000250|UniProtKB:B3DH20}. CC -!- SIMILARITY: Belongs to the tilB family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM004476; OCT77178.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1L8G016; -. DR SMR; A0A1L8G016; -. DR STRING; 8355.A0A1L8G016; -. DR PaxDb; 8355-A0A1L8G016; -. DR Xenbase; XB-GENE-6487993; dnaaf11.L. DR OMA; QHRAVIV; -. DR Proteomes; UP000186698; Genome assembly. DR Proteomes; UP000694892; Chromosome 6L. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0120293; C:dynein axonemal particle; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:GOC. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell. DR GO; GO:0070286; P:axonemal dynein complex assembly; ISS:UniProtKB. DR GO; GO:0090660; P:cerebrospinal fluid circulation; ISS:UniProtKB. DR GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; ISS:UniProtKB. DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; ISS:UniProtKB. DR GO; GO:0051649; P:establishment of localization in cell; ISS:UniProtKB. DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB. DR GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB. DR GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB. DR GO; GO:0120229; P:protein localization to motile cilium; ISS:UniProtKB. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR003603; U2A'_phosphoprotein32A_C. DR PANTHER; PTHR18849:SF0; CILIA- AND FLAGELLA-ASSOCIATED PROTEIN 410-RELATED; 1. DR PANTHER; PTHR18849; LEUCINE RICH REPEAT PROTEIN; 1. DR Pfam; PF14580; LRR_9; 1. DR SMART; SM00365; LRR_SD22; 2. DR SMART; SM00446; LRRcap; 1. DR SUPFAM; SSF52058; L domain-like; 1. DR PROSITE; PS51450; LRR; 5. PE 3: Inferred from homology; KW Cell projection; Cilium; Coiled coil; Cytoplasm; Flagellum; KW Leucine-rich repeat; Reference proteome; Repeat. FT CHAIN 1..469 FT /note="Dynein axonemal assembly factor 11" FT /id="PRO_0000452439" FT REPEAT 20..43 FT /note="LRR 1" FT /evidence="ECO:0000255" FT REPEAT 44..65 FT /note="LRR 2" FT /evidence="ECO:0000255" FT REPEAT 66..89 FT /note="LRR 3" FT /evidence="ECO:0000255" FT REPEAT 90..110 FT /note="LRR 4" FT /evidence="ECO:0000255" FT DOMAIN 114..135 FT /note="LRRCT" FT /evidence="ECO:0000255" FT REGION 179..290 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 436..469 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 179..211 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..251 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 263..290 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 469 AA; 54340 MW; 3565B6B4B25C783A CRC64; MPTISEDLIR RRAEHNNCEI FSLEEISLHQ QDLERIEHID KWCRELKILY LQNNLIGKIE NVSKLKKLEY LNLALNNIEK IENLEGCESL QKLDLTVNFV GELSSINSLQ ENLHLRELYL VGNPCAEYEG YRQYVVATLP QLKWLDGKEI ERSERIQALQ DYPQVQGRMK EQQEAYLRKR AAEREEARSK LQGKQKESRK TQEKKPGFDR RWYTDINNTI PDPVEKPDPT EQNGDETALR KAEEEEEKEF WSQPSQYTPE SRLETHRYLE EKRKSKESSS EGELKKKPPR TLITAEGRVL NVNESKLDFS LVDDEENNQF VLDLAIYRHL DTSLVDVDVQ PSYIKVLVKE KPFQLVLPAE VKPDSSSAKR SQTTGHLVVT MPKAIGVIQT KRAKSPVVEE QTRKNPPKCS KTFEKLEVDP KACSVPDFAN IVQEKKTQAQ GPLQFHKNKV KDTEDSEDFI DNTDVPPLM //