DYL1_CAEEL
ID DYL1_CAEEL Reviewed; 89 AA.
AC Q22799;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Dynein light chain 1, cytoplasmic;
GN Name=dlc-1 {ECO:0000312|WormBase:T26A5.9};
GN ORFNames=T26A5.9 {ECO:0000312|WormBase:T26A5.9};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, INTERACTION WITH METT-10, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF PHE-62; THR-67; HIS-68 AND PHE-73.
RX PubMed=19752194; DOI=10.1128/mcb.00815-09;
RA Dorsett M., Schedl T.;
RT "A role for dynein in the inhibition of germ cell proliferative fate.";
RL Mol. Cell. Biol. 29:6128-6139(2009).
RN [3]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH BICD-1 AND EGAL-1, INTERACTION
RP WITH EGAL-1 AND UNC-83, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20005871; DOI=10.1016/j.ydbio.2009.12.004;
RA Fridolfsson H.N., Ly N., Meyerzon M., Starr D.A.;
RT "UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope
RT during nuclear migration.";
RL Dev. Biol. 338:237-250(2010).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24030151; DOI=10.1038/cddis.2013.319;
RA Morthorst T.H., Olsen A.;
RT "Cell-nonautonomous inhibition of radiation-induced apoptosis by dynein
RT light chain 1 in Caenorhabditis elegans.";
RL Cell Death Dis. 4:E799-E799(2013).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26483555; DOI=10.1083/jcb.201409035;
RA Bohr T., Nelson C.R., Klee E., Bhalla N.;
RT "Spindle assembly checkpoint proteins regulate and monitor meiotic synapsis
RT in C. elegans.";
RL J. Cell Biol. 211:233-242(2015).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH FGF-2,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27864381; DOI=10.1242/dev.140921;
RA Wang X., Olson J.R., Rasoloson D., Ellenbecker M., Bailey J., Voronina E.;
RT "Dynein light chain DLC-1 promotes localization and function of the PUF
RT protein FBF-2 in germline progenitor cells.";
RL Development 143:4643-4653(2016).
CC -!- FUNCTION: Acts as a non-catalytic accessory component of a dynein
CC complex (By similarity). Part of a complex with bicd-1 and egal-1,
CC which is recruited to the nuclear envelope by unc-83, where in turn, it
CC recruits dynein to the nuclear surface and regulates nuclear migrations
CC in hypodermal precursor cells (PubMed:20005871). Probably within a
CC dynein motor complex, plays a role in the cell fate specification of
CC the germline and oogenesis (PubMed:19752194, PubMed:27864381). In
CC particular, it inhibits germ cell proliferation (PubMed:19752194).
CC Regulates the function and localization of the RNA-binding protein fbf-
CC 2 in the germline (PubMed:27864381). Plays a role in mitotic and
CC meiotic processes (PubMed:19752194, PubMed:26483555). Involved in the
CC pairing of homologous chromosomes (PubMed:26483555). Independently of
CC its dynein-mediated functions, plays a role in germ cell apoptosis
CC (PubMed:24030151). {ECO:0000250|UniProtKB:Q24117,
CC ECO:0000269|PubMed:19752194, ECO:0000269|PubMed:20005871,
CC ECO:0000269|PubMed:24030151, ECO:0000269|PubMed:26483555,
CC ECO:0000269|PubMed:27864381}.
CC -!- SUBUNIT: Interacts with mett-10; the interaction is direct, and is
CC required for the nuclear localization of mett-10 (PubMed:19752194).
CC Component of a dynein-regulating complex composed of at least bicd-1,
CC dlc-1 and egal-1 (PubMed:20005871). Interacts with egal-1 and unc-83
CC (PubMed:20005871). Interacts with fbf-2 (PubMed:27864381).
CC {ECO:0000269|PubMed:19752194, ECO:0000269|PubMed:20005871,
CC ECO:0000269|PubMed:27864381}.
CC -!- INTERACTION:
CC Q22799; Q17902: egal-1; NbExp=5; IntAct=EBI-328324, EBI-328330;
CC Q22799; C6KRN1: sao-1; NbExp=4; IntAct=EBI-328324, EBI-323135;
CC Q22799; G5ECT7: spat-1; NbExp=3; IntAct=EBI-328324, EBI-328382;
CC Q22799; Q23064-3: unc-83; NbExp=2; IntAct=EBI-328324, EBI-2902257;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P63170}. Nucleus envelope
CC {ECO:0000269|PubMed:27864381, ECO:0000305|PubMed:20005871}. Cytoplasmic
CC granule {ECO:0000269|PubMed:27864381}. Note=Probably recruited to the
CC nuclear envelope by unc-83 (PubMed:20005871). Localizes to perinuclear
CC patches in the transition zone (PubMed:27864381). Localizes to P-
CC granules in the mitotic region and transition zone (PubMed:27864381).
CC {ECO:0000269|PubMed:27864381, ECO:0000305|PubMed:20005871}.
CC -!- TISSUE SPECIFICITY: Broadly expressed in tissues including the
CC intestine, body wall muscles, germs cells, oocytes, the rectal valve
CC and cells in the head. {ECO:0000269|PubMed:24030151}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages from the
CC one-cell embryo. {ECO:0000269|PubMed:24030151}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in viable
CC animals, with progeny that have nuclear migration defects in the hyp7
CC hypodermal precursor cells at the L1 stage of larval development
CC (PubMed:20005871). RNAi-mediated knockdown results in increased germ
CC cell apoptosis, but does not affect somatic cell death
CC (PubMed:24030151). RNAi-mediated knockdown results in reduced mett-10
CC accumulation in nuclei (PubMed:19752194). RNAi-mediated knockdown
CC prevents fbf-2 localization to P-granules (PubMed:27864381).
CC Furthermore, RNAi-mediated knockdown in a fbf-2 loss of function
CC background results in sterility and masculinization of the germline
CC where only sperm, and not oocytes, are produced (PubMed:27864381).
CC RNAi-mediated knockdown in a dhc-1 loss of function (or195) mutant
CC background results in failed homologous chromosome pairing during
CC meiosis (PubMed:26483555). RNAi-mediated knockdown in a glp-1 gain of
CC function sensitized mutant background results in disrupted meiotic and
CC mitotic processes (PubMed:19752194). This in turn results in polyploid
CC nuclei, that are larger in size and contain more DNA as compared to
CC wild-type (PubMed:19752194). In addition, many oocytes from these
CC animals also contain unpaired chromosomes (PubMed:19752194).
CC {ECO:0000269|PubMed:19752194, ECO:0000269|PubMed:20005871,
CC ECO:0000269|PubMed:24030151, ECO:0000269|PubMed:26483555,
CC ECO:0000269|PubMed:27864381}.
CC -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
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DR EMBL; FO080366; CCD63216.1; -; Genomic_DNA.
DR PIR; T34388; T34388.
DR RefSeq; NP_498422.1; NM_066021.4.
DR AlphaFoldDB; Q22799; -.
DR SMR; Q22799; -.
DR BioGRID; 41140; 66.
DR ComplexPortal; CPX-1388; bicd-1-dlc-1-egal-1 microtubule-associated dynein motor complex.
DR DIP; DIP-25449N; -.
DR IntAct; Q22799; 28.
DR STRING; 6239.T26A5.9.2; -.
DR EPD; Q22799; -.
DR PaxDb; Q22799; -.
DR PeptideAtlas; Q22799; -.
DR EnsemblMetazoa; T26A5.9.1; T26A5.9.1; WBGene00001005.
DR UCSC; T26A5.9.1; c. elegans.
DR WormBase; T26A5.9; CE00788; WBGene00001005; dlc-1.
DR eggNOG; KOG3430; Eukaryota.
DR GeneTree; ENSGT00390000000378; -.
DR HOGENOM; CLU_070944_4_0_1; -.
DR InParanoid; Q22799; -.
DR OMA; RHGATWH; -.
DR OrthoDB; 1520814at2759; -.
DR PhylomeDB; Q22799; -.
DR Reactome; R-CEL-1632852; Macroautophagy.
DR Reactome; R-CEL-5620924; Intraflagellar transport.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-9646399; Aggrephagy.
DR SignaLink; Q22799; -.
DR PRO; PR:Q22799; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001005; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IC:ComplexPortal.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030473; P:nuclear migration along microtubule; IC:ComplexPortal.
DR Gene3D; 3.30.740.10; -; 1.
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 Apoptosis; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Dynein;
KW Meiosis; Microtubule; Mitosis; Motor protein; Nucleus; Reference proteome;
KW Transport.
FT CHAIN 1..89
FT /note="Dynein light chain 1, cytoplasmic"
FT /id="PRO_0000195130"
FT SITE 62
FT /note="Required for mett-10 binding"
FT /evidence="ECO:0000269|PubMed:19752194"
FT SITE 67
FT /note="Required for mett-10 binding"
FT /evidence="ECO:0000269|PubMed:19752194"
FT SITE 73
FT /note="Required for mett-10 binding"
FT /evidence="ECO:0000269|PubMed:19752194"
FT MUTAGEN 62
FT /note="F->S: Reduces mett-10 binding."
FT /evidence="ECO:0000269|PubMed:19752194"
FT MUTAGEN 67
FT /note="T->A: Reduces mett-10 binding."
FT /evidence="ECO:0000269|PubMed:19752194"
FT MUTAGEN 68
FT /note="H->A: Does not affect mett-10 binding."
FT /evidence="ECO:0000269|PubMed:19752194"
FT MUTAGEN 73
FT /note="F->S: Reduces mett-10 binding."
FT /evidence="ECO:0000269|PubMed:19752194"
SQ SEQUENCE 89 AA; 10344 MW; 72831C3103C2294E CRC64;
MVDRKAVIKN ADMSDDMQQD AIDCATQALE KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG
