DYL1_DROME
ID DYL1_DROME Reviewed; 89 AA.
AC Q24117; A4V3Y5; Q9V3Y6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Dynein light chain 1, cytoplasmic;
DE AltName: Full=8 kDa dynein light chain;
DE AltName: Full=Cut up protein;
GN Name=ctp; Synonyms=Cdlc1, ddlc1; ORFNames=CG6998;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=8628263; DOI=10.1128/mcb.16.5.1966;
RA Dick T., Ray K., Salz H.K., Chia W.;
RT "Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and
RT apoptotic cell death in Drosophila melanogaster.";
RL Mol. Cell. Biol. 16:1966-1977(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Head, and Ovary;
RA Li M.-G., Serr M., Hays T.S.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP INTERACTION WITH SPN-F.
RX PubMed=16540510; DOI=10.1242/dev.02319;
RA Abdu U., Bar D., Schuepbach T.;
RT "spn-F encodes a novel protein that affects oocyte patterning and bristle
RT morphology in Drosophila.";
RL Development 133:1477-1484(2006).
RN [6]
RP IDENTIFICATION IN COMPLEX WITH SPN-F AND IKKEPSILON.
RX PubMed=26092846; DOI=10.1242/dev.121863;
RA Otani T., Oshima K., Kimpara A., Takeda M., Abdu U., Hayashi S.;
RT "A transport and retention mechanism for the sustained distal localization
RT of Spn-F-IKKepsilon during Drosophila bristle elongation.";
RL Development 142:2338-2351(2015).
RN [7]
RP IDENTIFICATION IN COMPLEX WITH SPN-F AND IKKEPSILON.
RX PubMed=26540204; DOI=10.1371/journal.pgen.1005642;
RA Lin T., Pan P.Y., Lai Y.T., Chiang K.W., Hsieh H.L., Wu Y.P., Ke J.M.,
RA Lee M.C., Liao S.S., Shih H.T., Tang C.Y., Yang S.B., Cheng H.C., Wu J.T.,
RA Jan Y.N., Lee H.H.;
RT "Spindle-F is the central mediator of Ik2 kinase-dependent dendrite pruning
RT in Drosophila sensory neurons.";
RL PLoS Genet. 11:E1005642-E1005642(2015).
CC -!- FUNCTION: Acts as a non-catalytic accessory component of a dynein
CC complex. {ECO:0000269|PubMed:8628263}.
CC -!- SUBUNIT: Interacts with spn-F (PubMed:16540510). Forms ternary
CC complexes with spn-F and IKKepsilon (PubMed:26092846, PubMed:26540204).
CC {ECO:0000269|PubMed:16540510, ECO:0000269|PubMed:26092846,
CC ECO:0000269|PubMed:26540204}.
CC -!- INTERACTION:
CC Q24117; Q058Z8: Dmel\CG30324; NbExp=4; IntAct=EBI-156442, EBI-148486;
CC Q24117; Q9VFB9: Dmel\CG6654; NbExp=4; IntAct=EBI-156442, EBI-143939;
CC Q24117; Q7JX41: geminin; NbExp=5; IntAct=EBI-156442, EBI-88763;
CC Q24117; Q8SYK5: insv; NbExp=3; IntAct=EBI-156442, EBI-192407;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:8628263}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8628263}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit defects in bristle and wing
CC development. {ECO:0000269|PubMed:8628263}.
CC -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
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DR EMBL; U32855; AAB04148.1; -; mRNA.
DR EMBL; U48846; AAD00072.1; -; mRNA.
DR EMBL; U48848; AAD00074.1; -; mRNA.
DR EMBL; AE014298; AAF45975.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09126.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09127.1; -; Genomic_DNA.
DR RefSeq; NP_001245530.1; NM_001258601.3.
DR RefSeq; NP_525075.1; NM_080336.5.
DR RefSeq; NP_726942.1; NM_167014.3.
DR RefSeq; NP_726943.1; NM_167015.3.
DR PDB; 1RHW; NMR; -; A=1-89.
DR PDB; 2P2T; X-ray; 3.00 A; A=1-89.
DR PDB; 2PG1; X-ray; 2.80 A; A/B/C/D=1-89.
DR PDB; 3BRI; X-ray; 1.70 A; A=1-89.
DR PDB; 3BRL; X-ray; 1.90 A; A=1-87.
DR PDB; 3DVH; X-ray; 2.00 A; A/B/C=1-89.
DR PDB; 3DVP; X-ray; 2.50 A; A/B=1-89.
DR PDB; 3DVT; X-ray; 2.30 A; A/B/C/D/E/F=1-89.
DR PDB; 3E2B; X-ray; 2.00 A; A=1-89.
DR PDB; 3FM7; X-ray; 3.50 A; E/F=1-89.
DR PDB; 3GLW; X-ray; 3.15 A; A=1-89.
DR PDB; 4QH7; X-ray; 1.83 A; A/B/E/F=1-89.
DR PDB; 4QH8; X-ray; 1.90 A; A/B/E/F/G/H=1-89.
DR PDB; 5E0L; X-ray; 1.31 A; A=3-89.
DR PDB; 5E0M; X-ray; 1.65 A; A=1-89.
DR PDB; 7K3J; X-ray; 2.50 A; A/C/E/G/I/K=1-89.
DR PDB; 7K3K; X-ray; 1.42 A; A=1-89.
DR PDB; 7K3L; X-ray; 1.79 A; A=1-89.
DR PDBsum; 1RHW; -.
DR PDBsum; 2P2T; -.
DR PDBsum; 2PG1; -.
DR PDBsum; 3BRI; -.
DR PDBsum; 3BRL; -.
DR PDBsum; 3DVH; -.
DR PDBsum; 3DVP; -.
DR PDBsum; 3DVT; -.
DR PDBsum; 3E2B; -.
DR PDBsum; 3FM7; -.
DR PDBsum; 3GLW; -.
DR PDBsum; 4QH7; -.
DR PDBsum; 4QH8; -.
DR PDBsum; 5E0L; -.
DR PDBsum; 5E0M; -.
DR PDBsum; 7K3J; -.
DR PDBsum; 7K3K; -.
DR PDBsum; 7K3L; -.
DR AlphaFoldDB; Q24117; -.
DR BMRB; Q24117; -.
DR SMR; Q24117; -.
DR BioGRID; 57920; 71.
DR DIP; DIP-17520N; -.
DR IntAct; Q24117; 15.
DR STRING; 7227.FBpp0070672; -.
DR iPTMnet; Q24117; -.
DR PaxDb; Q24117; -.
DR PRIDE; Q24117; -.
DR DNASU; 31405; -.
DR EnsemblMetazoa; FBtr0070704; FBpp0070672; FBgn0011760.
DR EnsemblMetazoa; FBtr0070706; FBpp0070674; FBgn0011760.
DR EnsemblMetazoa; FBtr0070707; FBpp0070675; FBgn0011760.
DR EnsemblMetazoa; FBtr0307065; FBpp0297908; FBgn0011760.
DR GeneID; 31405; -.
DR KEGG; dme:Dmel_CG6998; -.
DR CTD; 31405; -.
DR FlyBase; FBgn0011760; ctp.
DR VEuPathDB; VectorBase:FBgn0011760; -.
DR eggNOG; KOG3430; Eukaryota.
DR GeneTree; ENSGT00390000000378; -.
DR HOGENOM; CLU_070944_4_0_1; -.
DR InParanoid; Q24117; -.
DR OMA; FAGTRRN; -.
DR OrthoDB; 1520814at2759; -.
DR PhylomeDB; Q24117; -.
DR Reactome; R-DME-1632852; Macroautophagy.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-5620924; Intraflagellar transport.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-9646399; Aggrephagy.
DR SignaLink; Q24117; -.
DR BioGRID-ORCS; 31405; 0 hits in 3 CRISPR screens.
DR ChiTaRS; ctp; fly.
DR EvolutionaryTrace; Q24117; -.
DR GenomeRNAi; 31405; -.
DR PRO; PR:Q24117; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0011760; Expressed in cleaving embryo and 56 other tissues.
DR ExpressionAtlas; Q24117; baseline and differential.
DR Genevisible; Q24117; DM.
DR GO; GO:0005814; C:centriole; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:FlyBase.
DR GO; GO:0030286; C:dynein complex; IDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0045505; F:dynein intermediate chain binding; IPI:FlyBase.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:FlyBase.
DR GO; GO:0006914; P:autophagy; IMP:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:UniProtKB.
DR GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:FlyBase.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:1904801; P:positive regulation of neuron remodeling; IMP:FlyBase.
DR GO; GO:0035071; P:salivary gland cell autophagic cell death; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0007290; P:spermatid nucleus elongation; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:UniProtKB.
DR Gene3D; 3.30.740.10; -; 1.
DR IDEAL; IID50051; -.
DR InterPro; IPR037177; DLC_sf.
DR InterPro; IPR019763; Dynein_light_1/2_CS.
DR InterPro; IPR001372; Dynein_light_chain_typ-1/2.
DR PANTHER; PTHR11886; PTHR11886; 1.
DR Pfam; PF01221; Dynein_light; 1.
DR SMART; SM01375; Dynein_light; 1.
DR SUPFAM; SSF54648; SSF54648; 1.
DR PROSITE; PS01239; DYNEIN_LIGHT_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW Reference proteome; Transport.
FT CHAIN 1..89
FT /note="Dynein light chain 1, cytoplasmic"
FT /id="PRO_0000195131"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:5E0L"
FT HELIX 15..31
FT /evidence="ECO:0007829|PDB:5E0L"
FT HELIX 35..50
FT /evidence="ECO:0007829|PDB:5E0L"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:5E0L"
FT STRAND 63..78
FT /evidence="ECO:0007829|PDB:5E0L"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:5E0L"
SQ SEQUENCE 89 AA; 10374 MW; 44871BC030423A8F CRC64;
MSDRKAVIKN ADMSEEMQQD AVDCATQALE KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR
NFGSYVTHET RHFIYFYLGQ VAILLFKSG
