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Database: UniProt
Entry: Q05A62
LinkDB: Q05A62
Original site: Q05A62 
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   24-JAN-2024, entry version 116.
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   SwissPalm; Q05A62; -.
DR   MaxQB; Q05A62; -.
DR   PaxDb; 10090-ENSMUSP00000121038; -.
DR   ProteomicsDB; 277472; -. [Q05A62-1]
DR   ProteomicsDB; 277473; -. [Q05A62-2]
DR   ProteomicsDB; 277474; -. [Q05A62-3]
DR   Pumba; Q05A62; -.
DR   Antibodypedia; 25408; 257 antibodies from 32 providers.
DR   DNASU; 105000; -.
DR   Ensembl; ENSMUST00000046340.9; ENSMUSP00000037076.3; ENSMUSG00000042523.13. [Q05A62-3]
DR   Ensembl; ENSMUST00000123491.8; ENSMUSP00000121038.2; ENSMUSG00000042523.13. [Q05A62-1]
DR   GeneID; 105000; -.
DR   KEGG; mmu:105000; -.
DR   UCSC; uc007oek.2; mouse. [Q05A62-1]
DR   UCSC; uc011yot.1; mouse. [Q05A62-2]
DR   AGR; MGI:1921462; -.
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; 166694at2759; -.
DR   PhylomeDB; Q05A62; -.
DR   TreeFam; TF323974; -.
DR   BioGRID-ORCS; 105000; 0 hits in 77 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 217 other cell types or 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; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR025875; Leu-rich_rpt_4.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR15454:SF33; DYNEIN AXONEMAL LIGHT CHAIN 1; 1.
DR   PANTHER; PTHR15454; NISCHARIN RELATED; 1.
DR   Pfam; PF12799; LRR_4; 2.
DR   SMART; SM00365; LRR_SD22; 4.
DR   SUPFAM; SSF52058; L domain-like; 1.
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
//
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