DAA11_MOUSE
ID DAA11_MOUSE Reviewed; 473 AA.
AC O88978; Q9CUG2;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
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=Leucine-rich testis-specific protein;
DE AltName: Full=Protein tilB homolog;
DE AltName: Full=Testis-specific leucine-rich repeat protein;
GN Name=Dnaaf11; Synonyms=Lrrc6 {ECO:0000312|MGI:MGI:1859553}, Lrtp, Mc2;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10775177; DOI=10.1095/biolreprod62.5.1278;
RA Xue J.-C., Goldberg E.;
RT "Identification of a novel testis-specific leucine-rich protein in humans
RT and mice.";
RL Biol. Reprod. 62:1278-1284(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=27353389; DOI=10.1111/gtc.12380;
RA Inaba Y., Shinohara K., Botilde Y., Nabeshima R., Takaoka K., Ajima R.,
RA Lamri L., Takeda H., Saga Y., Nakamura T., Hamada H.;
RT "Transport of the outer dynein arm complex to cilia requires a cytoplasmic
RT protein Lrrc6.";
RL Genes Cells 21:728-739(2016).
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 (PubMed:27353389). Acts as a crucial component in the
CC formation and motility of spermatozoal flagella (By similarity).
CC {ECO:0000250|UniProtKB:Q86X45, ECO:0000269|PubMed:27353389}.
CC -!- SUBUNIT: Interacts (via CS domain) with ZMYND10 (via C-terminus).
CC {ECO:0000250|UniProtKB:Q86X45}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10775177,
CC ECO:0000269|PubMed:27353389}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q86X45}. Dynein axonemal particle
CC {ECO:0000305|PubMed:27353389}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q86X45}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in cells with motile cilia
CC (PubMed:27353389). Expressed in epithelial cells of the trachea, testis
CC and ependymal cells of the cerebral ventricles (PubMed:27353389). In
CC testis, abundant expression in late prophase of meiosis I with a
CC dramatic decrease after the first meiotic division (at protein level)
CC (PubMed:10775177). {ECO:0000269|PubMed:10775177,
CC ECO:0000269|PubMed:27353389}.
CC -!- DEVELOPMENTAL STAGE: At the embryonic day 8.0 dpc, expressed at the
CC node, especially in pit cells, which are located at the central region
CC of the node and possess motile cilia. At later stages, expression is
CC detected in the notochord at 9.0 dpc, in the hindbrain, the branchial
CC arches and neural tube at 11.0 dpc, in the hindbrain at 12.0 dpc and in
CC the forebrain at 13.0 dpc. {ECO:0000269|PubMed:27353389}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show primary ciliary dyskinesia
CC defects such as hydrocephalus and laterality defects and die within 5
CC weeks of birth. The morphology of mutant motile cilia is normal, but
CC their motility is completely lost. The 9 + 2 arrangement of
CC microtubules remain normal in mutants, but the outer dynein arms (ODAs)
CC is absent from the cilia. {ECO:0000269|PubMed:27353389}.
CC -!- SIMILARITY: Belongs to the tilB family. {ECO:0000305}.
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DR EMBL; AF092208; AAC61765.1; -; mRNA.
DR EMBL; AK016236; BAB30161.1; -; mRNA.
DR EMBL; AK077124; BAC36627.1; -; mRNA.
DR EMBL; BC046277; AAH46277.1; -; mRNA.
DR CCDS; CCDS49620.1; -.
DR RefSeq; NP_062330.1; NM_019457.2.
DR AlphaFoldDB; O88978; -.
DR SMR; O88978; -.
DR STRING; 10090.ENSMUSP00000023006; -.
DR PhosphoSitePlus; O88978; -.
DR PaxDb; O88978; -.
DR PRIDE; O88978; -.
DR ProteomicsDB; 259451; -.
DR Antibodypedia; 14134; 243 antibodies from 21 providers.
DR DNASU; 54562; -.
DR Ensembl; ENSMUST00000023006; ENSMUSP00000023006; ENSMUSG00000022375.
DR GeneID; 54562; -.
DR KEGG; mmu:54562; -.
DR UCSC; uc011ztm.1; mouse.
DR CTD; 54562; -.
DR MGI; MGI:1859553; Lrrc6.
DR VEuPathDB; HostDB:ENSMUSG00000022375; -.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00940000158506; -.
DR HOGENOM; CLU_034806_0_1_1; -.
DR InParanoid; O88978; -.
DR OMA; QHRAVIV; -.
DR OrthoDB; 800324at2759; -.
DR PhylomeDB; O88978; -.
DR TreeFam; TF324815; -.
DR BioGRID-ORCS; 54562; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Lrrc6; mouse.
DR PRO; PR:O88978; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O88978; protein.
DR Bgee; ENSMUSG00000022375; Expressed in spermatid and 60 other tissues.
DR Genevisible; O88978; MM.
DR GO; GO:0090651; C:apical cytoplasm; IDA:MGI.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0120293; C:dynein axonemal particle; ISS: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; IMP:MGI.
DR GO; GO:0003341; P:cilium movement; IMP:MGI.
DR GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IMP:MGI.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0036159; P:inner dynein arm assembly; ISO:MGI.
DR GO; GO:0008584; P:male gonad development; IEP:BHF-UCL.
DR GO; GO:0044458; P:motile cilium assembly; ISO:MGI.
DR GO; GO:0036158; P:outer dynein arm assembly; IMP:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:0120229; P:protein localization to motile cilium; ISS:UniProtKB.
DR GO; GO:0043393; P:regulation of protein binding; IDA:MGI.
DR GO; GO:0061458; P:reproductive system development; ISO:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR PROSITE; PS51450; LRR; 5.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Flagellum;
KW Leucine-rich repeat; Reference proteome; Repeat.
FT CHAIN 1..473
FT /note="Dynein axonemal assembly factor 11"
FT /id="PRO_0000084498"
FT REPEAT 22..43
FT /note="LRR 1"
FT REPEAT 45..66
FT /note="LRR 2"
FT REPEAT 67..88
FT /note="LRR 3"
FT REPEAT 89..110
FT /note="LRR 4"
FT DOMAIN 123..161
FT /note="LRRCT"
FT DOMAIN 305..402
FT /note="CS"
FT REGION 188..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..205
FT /evidence="ECO:0000255"
FT COMPBIAS 188..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 225
FT /note="N -> I (in Ref. 2; BAB30161)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="H -> N (in Ref. 2; BAB30161)"
FT /evidence="ECO:0000305"
FT CONFLICT 259..262
FT /note="LFTP -> FFFL (in Ref. 2; BAB30161)"
FT /evidence="ECO:0000305"
FT CONFLICT 271..272
FT /note="HM -> FL (in Ref. 2; BAB30161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 55049 MW; A7181C5B4560E135 CRC64;
MGRITEDLIR RNAEHNDCVI FSLEELSLHQ QEIERLEHID KWCRDLKILY LQNNLIGKIE
NVSKLKKLEY LNLALNNIER IENLEGCEWL TKLDLTVNFI GELSSVKTLT HNIHLKELFL
MGNPCADFDG YRQFVVVTLQ QLKWLDGKEI ERSERIQALQ NYTSVEQQIR EQEKAYCLRR
AKEKEEAQRK LEEENESEDK KKSSTGFDGH WYTDIHTACP SATENQDYPQ VPETQEEQHN
TKESDDIEDD LAFWNKPSLF TPESRLETLR HMEKQRKAQD KLSEKKKKAK PPRTLITEDG
KVLNVNEAKL DFSLKDDEKH NQIILDLAVY RYMDTSLIEV DVQPTYVRVM VKGKPFQLAL
STEVQPDRSS AKRSQTTGHL LICMPKVGEM ITGGQRTPTS VKTTSTSSRE QTNPRKKQIE
RLEVDPSKHS CPDVSTIVQE KRHRPKRMES QPRDEPSEED PDFEDNPEVP PLI
