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DAA11_XENLA
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   25-MAY-2022, entry version 15.
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}.
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DR   EMBL; CM004476; OCT77178.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L8G016; -.
DR   SMR; A0A1L8G016; -.
DR   STRING; 8355.A0A1L8G016; -.
DR   OMA; QHRAVIV; -.
DR   Proteomes; UP000186698; Genome assembly.
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; -; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR   SMART; SM00446; LRRcap; 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
 
 
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