DNAL1_MOUSE
ID DNAL1_MOUSE Reviewed; 190 AA.
AC Q05A62; A0JLX1; Q9DAH9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Dynein axonemal light chain 1;
GN Name=Dnal1; Synonyms=Dnalc1;
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 [LARGE SCALE MRNA] (ISOFORM 3).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain;
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 [3]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=15845866; DOI=10.1165/rcmb.2004-0335oc;
RA Horvath J., Fliegauf M., Olbrich H., Kispert A., King S.M., Mitchison H.,
RA Zariwala M.A., Knowles M.R., Sudbrak R., Fekete G., Neesen J.,
RA Reinhardt R., Omran H.;
RT "Identification and analysis of axonemal dynein light chain 1 in primary
RT ciliary dyskinesia patients.";
RL Am. J. Respir. Cell Mol. Biol. 33:41-47(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and 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).
CC -!- FUNCTION: Part of the multisubunit axonemal ATPase complexes that
CC generate the force for cilia motility and govern beat frequency (By
CC similarity). Component of the outer arm dynein (ODA). May be involved
CC in a mechanosensory feedback mechanism controlling ODA activity based
CC on external conformational cues by tethering the outer arm dynein heavy
CC chain (DNAH5) to the microtubule within the axoneme (By similarity).
CC Important for ciliary function in the airways and for the function of
CC the cilia that produce the nodal flow essential for the determination
CC of the left-right asymmetry (By similarity).
CC {ECO:0000250|UniProtKB:Q4LDG9, ECO:0000250|UniProtKB:Q9XHH2}.
CC -!- SUBUNIT: Interacts with ZMYND10 (via C-terminus). Interacts with DNAH5,
CC a outer arm dynein heavy chain. Interacts with tubulin located within
CC the A-tubule of the outer doublets in a ATP-independent manner.
CC {ECO:0000250|UniProtKB:Q4LDG9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q4LDG9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q05A62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05A62-2; Sequence=VSP_023984, VSP_023983;
CC Name=3;
CC IsoId=Q05A62-3; Sequence=VSP_023985;
CC -!- TISSUE SPECIFICITY: Expressed in the respiratory epithelium of the
CC upper airways and the ependymal cells lining the brain ventricles.
CC {ECO:0000269|PubMed:15845866}.
CC -!- MISCELLANEOUS: Outer (ODAs) and inner (IDAs) dynein arms contain the
CC molecular motors that generate the force to move cilia by ATP-dependent
CC reactions. There are two mechanosensory systems that monitor and
CC respond to the mechanical state (curvature) of the axoneme. One system
CC involves the central pair microtubule complex and radial spokes and the
CC second system involves the outer dynein arms.
CC {ECO:0000250|UniProtKB:Q9XHH2}.
CC -!- SIMILARITY: Belongs to the dynein light chain LC1-type family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI25395.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK005826; BAB24259.1; -; mRNA.
DR EMBL; BC125392; AAI25393.1; -; mRNA.
DR EMBL; BC125394; AAI25395.2; ALT_INIT; mRNA.
DR EMBL; BG916281; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS26039.2; -. [Q05A62-1]
DR CCDS; CCDS83987.1; -. [Q05A62-3]
DR RefSeq; NP_001333457.1; NM_001346528.1. [Q05A62-3]
DR RefSeq; NP_083097.2; NM_028821.3. [Q05A62-1]
DR AlphaFoldDB; Q05A62; -.
DR SMR; Q05A62; -.
DR BioGRID; 222746; 1.
DR STRING; 10090.ENSMUSP00000121038; -.
DR iPTMnet; Q05A62; -.
DR PhosphoSitePlus; Q05A62; -.
DR MaxQB; Q05A62; -.
DR PaxDb; Q05A62; -.
DR PRIDE; Q05A62; -.
DR ProteomicsDB; 277472; -. [Q05A62-1]
DR ProteomicsDB; 277473; -. [Q05A62-2]
DR ProteomicsDB; 277474; -. [Q05A62-3]
DR Antibodypedia; 25408; 231 antibodies from 32 providers.
DR DNASU; 105000; -.
DR Ensembl; ENSMUST00000046340; ENSMUSP00000037076; ENSMUSG00000042523. [Q05A62-3]
DR Ensembl; ENSMUST00000123491; ENSMUSP00000121038; ENSMUSG00000042523. [Q05A62-1]
DR GeneID; 105000; -.
DR KEGG; mmu:105000; -.
DR UCSC; uc007oek.2; mouse. [Q05A62-1]
DR UCSC; uc011yot.1; mouse. [Q05A62-2]
DR CTD; 83544; -.
DR MGI; MGI:1921462; Dnal1.
DR VEuPathDB; HostDB:ENSMUSG00000042523; -.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00390000016904; -.
DR HOGENOM; CLU_092189_0_0_1; -.
DR InParanoid; Q05A62; -.
DR OMA; LWISYNN; -.
DR OrthoDB; 1395642at2759; -.
DR PhylomeDB; Q05A62; -.
DR TreeFam; TF323974; -.
DR BioGRID-ORCS; 105000; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Dnal1; mouse.
DR PRO; PR:Q05A62; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q05A62; protein.
DR Bgee; ENSMUSG00000042523; Expressed in otolith organ and 214 other tissues.
DR ExpressionAtlas; Q05A62; baseline and differential.
DR Genevisible; Q05A62; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0036157; C:outer dynein arm; ISA:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0045504; F:dynein heavy chain binding; ISO:MGI.
DR GO; GO:0036158; P:outer dynein arm assembly; 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; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Cytoplasm;
KW Cytoskeleton; Dynein; Leucine-rich repeat; Microtubule; Motor protein;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q4LDG9"
FT CHAIN 2..190
FT /note="Dynein axonemal light chain 1"
FT /id="PRO_0000281131"
FT REPEAT 49..70
FT /note="LRR 1"
FT REPEAT 71..92
FT /note="LRR 2"
FT REPEAT 94..115
FT /note="LRR 3"
FT REPEAT 116..137
FT /note="LRR 4"
FT DOMAIN 150..190
FT /note="LRRCT"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q4LDG9"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023985"
FT VAR_SEQ 2..14
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023984"
FT VAR_SEQ 15
FT /note="E -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023983"
FT CONFLICT 147
FT /note="F -> L (in Ref. 1; BAB24259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 21465 MW; 7052EB49CDCE4A0B CRC64;
MAKATTIKEA LSRWEEKTGQ KPSDAKEIKL YAQIPPIEKM DASLSTLGNC EKLSLSTNCI
EKIANLNGLK NLRILSLGRN NIKNLNGLEA VGETLEELWI SYNFIEKLKG IHVMKKLKIL
YMSNNLVKDW AEFLKLAELP CLEDLVFVGN PLEEKHSAEG NWIDEATKRV PKLKKLDGTP
VIKEDEEEES
