DNAL1_CHLRE
ID DNAL1_CHLRE Reviewed; 198 AA.
AC Q9XHH2; A8I9F6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Dynein axonemal light chain 1;
DE Short=DNAL1 {ECO:0000305};
DE AltName: Full=Flagellar outer arm dynein light chain 1;
DE AltName: Full=ODA-LC protein LC1 {ECO:0000305};
GN Name=LC1 {ECO:0000303|PubMed:17932292}; ORFNames=CHLREDRAFT_186669;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 84-103; 127-129; 132-135
RP AND 178-192, AND FUNCTION.
RX PubMed=10353837; DOI=10.1021/bi990466y;
RA Benashski S.E., Patel-King R.S., King S.M.;
RT "Light chain 1 from the Chlamydomonas outer dynein arm is a leucine-rich
RT repeat protein associated with the motor domain of the gamma heavy chain.";
RL Biochemistry 38:7253-7264(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503, and cw92;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-182; ASP-185; ARG-189
RP AND ARG-196, INTERACTION WITH TUBULIN, AND INTERACTION WITH ODA2.
RX PubMed=19620633; DOI=10.1083/jcb.200905083;
RA Patel-King R.S., King S.M.;
RT "An outer arm dynein light chain acts in a conformational switch for
RT flagellar motility.";
RL J. Cell Biol. 186:283-295(2009).
RN [4]
RP FUNCTION, INTERACTION WITH TUBULIN, AND INTERACTION WITH ODA2.
RX PubMed=22157010; DOI=10.1074/jbc.m111.286211;
RA King S.M., Patel-King R.S.;
RT "Functional architecture of the outer arm dynein conformational switch.";
RL J. Biol. Chem. 287:3108-3122(2012).
RN [5]
RP STRUCTURE BY NMR, AND SUBUNIT.
RX PubMed=10876244; DOI=10.1038/76804;
RA Wu H., Maciejewski M.W., Marintchev A., Benashski S.E., Mullen G.P.,
RA King S.M.;
RT "Solution structure of a dynein motor domain associated light chain.";
RL Nat. Struct. Biol. 7:575-579(2000).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=12515539; DOI=10.1021/bi026762j;
RA Wu H., Blackledge M., Maciejewski M.W., Mullen G.P., King S.M.;
RT "Relaxation-based structure refinement and backbone molecular dynamics of
RT the dynein motor domain-associated light chain.";
RL Biochemistry 42:57-71(2003).
CC -!- FUNCTION: Part of the multisubunit axonemal ATPase complexes that
CC generate the force for flagellar motility and govern beat frequency
CC (PubMed:19620633). Component of the outer arm dynein (ODA)
CC (PubMed:19620633). May be involved in a mechanosensory feedback
CC mechanism controlling ODA activity based on external conformational
CC cues by tethering the outer arm dynein heavy chain (ODA2) to the A-
CC tubule of the outer doublet microtubules within the axoneme
CC (PubMed:22157010, PubMed:10353837, PubMed:19620633).
CC {ECO:0000269|PubMed:10353837, ECO:0000269|PubMed:19620633,
CC ECO:0000269|PubMed:22157010}.
CC -!- SUBUNIT: Interacts with OCAD2, a outer arm dynein heavy chain
CC (PubMed:19620633, PubMed:22157010). Interacts with tubulin (previously
CC called p45) located within the A-tubule of the outer doublets in a ATP-
CC independent manner (PubMed:19620633, PubMed:10876244, PubMed:22157010).
CC {ECO:0000269|PubMed:10876244, ECO:0000269|PubMed:19620633,
CC ECO:0000269|PubMed:22157010}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000269|PubMed:19620633}.
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:0000303|PubMed:19620633}.
CC -!- SIMILARITY: Belongs to the dynein light chain LC1-type family.
CC {ECO:0000305}.
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DR EMBL; AF112476; AAD41040.1; -; mRNA.
DR EMBL; DS496114; EDP06769.1; -; Genomic_DNA.
DR RefSeq; XP_001701794.1; XM_001701742.1.
DR PDB; 1DS9; NMR; -; A=1-198.
DR PDB; 1M9L; NMR; -; A=1-198.
DR PDB; 5YXM; X-ray; 1.54 A; A=1-198.
DR PDB; 6L4P; X-ray; 1.70 A; A=1-198.
DR PDBsum; 1DS9; -.
DR PDBsum; 1M9L; -.
DR PDBsum; 5YXM; -.
DR PDBsum; 6L4P; -.
DR AlphaFoldDB; Q9XHH2; -.
DR BMRB; Q9XHH2; -.
DR SMR; Q9XHH2; -.
DR STRING; 3055.EDP06769; -.
DR EnsemblPlants; PNW86588; PNW86588; CHLRE_02g092850v5.
DR GeneID; 5727508; -.
DR Gramene; PNW86588; PNW86588; CHLRE_02g092850v5.
DR KEGG; cre:CHLRE_02g092850v5; -.
DR eggNOG; KOG0531; Eukaryota.
DR HOGENOM; CLU_092189_0_0_1; -.
DR OMA; LWISYNN; -.
DR OrthoDB; 1395642at2759; -.
DR EvolutionaryTrace; Q9XHH2; -.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0036157; C:outer dynein arm; IDA:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF12799; LRR_4; 1.
DR PROSITE; PS51450; LRR; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Dynein; Flagellum; Leucine-rich repeat;
KW Microtubule; Motor protein; Repeat.
FT CHAIN 1..198
FT /note="Dynein axonemal light chain 1"
FT /id="PRO_0000282346"
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 157..195
FT /note="LRRCT"
FT SITE 182
FT /note="Controls the orientation of the C-terminal helical
FT region"
FT /evidence="ECO:0000303|PubMed:22157010"
FT SITE 185
FT /note="Controls the orientation of the C-terminal helical
FT region"
FT /evidence="ECO:0000303|PubMed:22157010"
FT MUTAGEN 182
FT /note="M->A: Reduces swimming velocity."
FT /evidence="ECO:0000269|PubMed:19620633"
FT MUTAGEN 182
FT /note="M->G: Reduces swimming velocity."
FT /evidence="ECO:0000269|PubMed:19620633"
FT MUTAGEN 182
FT /note="M->P: Reduces swimming velocity."
FT /evidence="ECO:0000269|PubMed:19620633"
FT MUTAGEN 185
FT /note="D->G: Reduces swimming velocity."
FT /evidence="ECO:0000269|PubMed:19620633"
FT MUTAGEN 185
FT /note="D->P: Reduces swimming velocity and beat frequency."
FT /evidence="ECO:0000269|PubMed:19620633"
FT MUTAGEN 189
FT /note="R->A: Reduces swimming velocity."
FT /evidence="ECO:0000269|PubMed:19620633"
FT MUTAGEN 189
FT /note="R->E: Reduces swimming velocity."
FT /evidence="ECO:0000269|PubMed:19620633"
FT MUTAGEN 196
FT /note="R->A: Reduces swimming velocity."
FT /evidence="ECO:0000269|PubMed:19620633"
FT MUTAGEN 196
FT /note="R->D: Reduces swimming velocity."
FT /evidence="ECO:0000269|PubMed:19620633"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:5YXM"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5YXM"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:5YXM"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:5YXM"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1DS9"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5YXM"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1DS9"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:1DS9"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5YXM"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1M9L"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5YXM"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:5YXM"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5YXM"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1M9L"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5YXM"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5YXM"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:5YXM"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:5YXM"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5YXM"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:5YXM"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:5YXM"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1DS9"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1DS9"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:5YXM"
SQ SEQUENCE 198 AA; 22151 MW; FFAEF4B52D76374D CRC64;
MAKATTIKDA IRIFEERKSV VATEAEKVEL HGMIPPIEKM DATLSTLKAC KHLALSTNNI
EKISSLSGME NLRILSLGRN LIKKIENLDA VADTLEELWI SYNQIASLSG IEKLVNLRVL
YMSNNKITNW GEIDKLAALD KLEDLLLAGN PLYNDYKENN ATSEYRIEVV KRLPNLKKLD
GMPVDVDERE QANVARGG
