ID   DNAL1_RAT               Reviewed;         190 AA.
AC   A0A096MJZ0;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   26-NOV-2014, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Dynein axonemal light chain 1 {ECO:0000250|UniProtKB:Q4LDG9};
DE            Short=LC1 {ECO:0000250|UniProtKB:Q9XHH2};
GN   Name=Dnal1 {ECO:0000312|RGD:1591349};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   INTERACTION WITH TUBULIN, SUBUNIT, AND INTERACTION WITH DNAH5.
RX   PubMed=21496787; DOI=10.1016/j.ajhg.2011.03.018;
RA   Mazor M., Alkrinawi S., Chalifa-Caspi V., Manor E., Sheffield V.C.,
RA   Aviram M., Parvari R.;
RT   "Primary ciliary dyskinesia caused by homozygous mutation in DNAL1,
RT   encoding dynein light chain 1.";
RL   Am. J. Hum. Genet. 88:599-607(2011).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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) (By similarity).
CC       Interacts with DNAH5, a outer arm dynein heavy chain (PubMed:21496787).
CC       Interacts with tubulin located within the A-tubule of the outer
CC       doublets in a ATP-independent manner (PubMed:21496787).
CC       {ECO:0000250|UniProtKB:Q4LDG9, ECO:0000269|PubMed:21496787}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:Q4LDG9}.
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}.
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DR   EMBL; AC094055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001102947.2; NM_001109477.2.
DR   AlphaFoldDB; A0A096MJZ0; -.
DR   SMR; A0A096MJZ0; -.
DR   STRING; 10116.ENSRNOP00000068314; -.
DR   iPTMnet; A0A096MJZ0; -.
DR   PaxDb; A0A096MJZ0; -.
DR   Ensembl; ENSRNOT00000076882; ENSRNOP00000068314; ENSRNOG00000042333.
DR   GeneID; 685664; -.
DR   KEGG; rno:685664; -.
DR   CTD; 83544; -.
DR   RGD; 1591349; Dnal1.
DR   eggNOG; KOG0531; Eukaryota.
DR   GeneTree; ENSGT00390000016904; -.
DR   HOGENOM; CLU_092189_0_0_1; -.
DR   OMA; LWISYNN; -.
DR   OrthoDB; 1395642at2759; -.
DR   PRO; PR:A0A096MJZ0; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000042333; Expressed in frontal cortex and 19 other tissues.
DR   ExpressionAtlas; A0A096MJZ0; baseline and differential.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0043014; F:alpha-tubulin binding; ISO:RGD.
DR   GO; GO:0045504; F:dynein heavy chain binding; ISO:RGD.
DR   GO; GO:0036158; P:outer dynein arm assembly; ISO:RGD.
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; Cell projection; Cytoplasm; Cytoskeleton; Dynein;
KW   Leucine-rich repeat; Microtubule; Motor protein; Phosphoprotein;
KW   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_0000441778"
FT   REPEAT          47..69
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          70..93
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          95..114
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          115..138
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
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:22673903"
SQ   SEQUENCE   190 AA;  21503 MW;  679B7E227994495F CRC64;
     MAKATTIKEA LSRWEEKTGQ KPSDAREIKL YAQIPPIEKM DASLSTLANC EKLSLSTNCI
     EKIANLNGLK NLRILSLGRN NIKNLNGLEA VGDTLEELWI SYNFIEKLKG IHVMRKLKIL
     YISNNLVKDW AEFVKLAELP CLEDLVFVGN PLEEKHSAEG NWIEEATKRV PKLKKLDGTP
     VIKEDEEEES