ID   DYL1_EMENI              Reviewed;          94 AA.
AC   O94111; C8VTG5; Q547D6; Q5BGB0;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Dynein light chain, cytoplasmic;
DE   AltName: Full=8 kDa cytoplasmic dynein light chain;
GN   Name=nudG; ORFNames=AN0420;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Beckwith S.M., Roghi C.H., Liu B., Morris N.R.;
RT   "Requirement of 8K dynein light chain in cellular localization of dynein
RT   heavy chain and nuclear migration.";
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12519184; DOI=10.1046/j.1365-2958.2003.03285.x;
RA   Liu B., Xiang X., Lee Y.R.;
RT   "The requirement of the LC8 dynein light chain for nuclear migration and
RT   septum positioning is temperature dependent in Aspergillus nidulans.";
RL   Mol. Microbiol. 47:291-301(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC       the cytoplasmic dynein complex that are thought to be involved in
CC       linking dynein to cargos and to adapter proteins that regulate dynein
CC       function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC       retrograde motility of vesicles and organelles along microtubules. May
CC       play a role in changing or maintaining the spatial distribution of
CC       cytoskeletal structures (By similarity). Also a component of the
CC       nuclear pore complex (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q02647}.
CC   -!- SUBUNIT: Homodimer. Cytoplasmic dynein consists of two catalytic heavy
CC       chains (HCs) and a number of non-catalytic subunits which present
CC       intermediate chains (ICs), light intermediate chains (LICs) and light
CC       chains (LCs). Component of the nuclear pore complex (NPC). The nuclear
CC       pore complex constitutes the exclusive means of nucleocytoplasmic
CC       transport. NPCs allow the passive diffusion of ions and small molecules
CC       and the active, nuclear transport receptor-mediated bidirectional
CC       transport of macromolecules such as proteins, RNAs, ribonucleoparticles
CC       (RNPs), and ribosomal subunits across the nuclear envelope. Due to its
CC       8-fold rotational symmetry, all subunits are present with 8 copies or
CC       multiples thereof. {ECO:0000250|UniProtKB:Q02647}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:Q02647}.
CC   -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA66519.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U81827; AAD00525.1; -; mRNA.
DR   EMBL; AF499001; AAO41062.1; -; Genomic_DNA.
DR   EMBL; AACD01000007; EAA66519.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001308; CBF89522.1; -; Genomic_DNA.
DR   RefSeq; XP_658024.1; XM_652932.1.
DR   AlphaFoldDB; O94111; -.
DR   SMR; O94111; -.
DR   STRING; 162425.CADANIAP00002278; -.
DR   EnsemblFungi; CBF89522; CBF89522; ANIA_00420.
DR   EnsemblFungi; EAA66519; EAA66519; AN0420.2.
DR   GeneID; 2876196; -.
DR   KEGG; ani:AN0420.2; -.
DR   VEuPathDB; FungiDB:AN0420; -.
DR   eggNOG; KOG3430; Eukaryota.
DR   HOGENOM; CLU_2183916_0_0_1; -.
DR   InParanoid; O94111; -.
DR   OMA; RHGATWH; -.
DR   OrthoDB; 1520814at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; IDA:AspGD.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IEA:EnsemblFungi.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:1990429; C:peroxisomal importomer complex; IEA:EnsemblFungi.
DR   GO; GO:0005777; C:peroxisome; IEA:EnsemblFungi.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR   GO; GO:0008574; F:plus-end-directed microtubule motor activity; IEA:EnsemblFungi.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:EnsemblFungi.
DR   GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IEA:EnsemblFungi.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0030473; P:nuclear migration along microtubule; IMP:AspGD.
DR   GO; GO:0051292; P:nuclear pore complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
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   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW   mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW   Reference proteome; Translocation; Transport.
FT   CHAIN           1..94
FT                   /note="Dynein light chain, cytoplasmic"
FT                   /id="PRO_0000195146"
SQ   SEQUENCE   94 AA;  11031 MW;  37EAEFE4998A63B2 CRC64;
     MASEKKDKLE PQIKSVDMSE DMQQEAVEVA IEAMEKYHIE KDIAQYIKRE FDSRKGATWH
     CVVGRNFGSF VTHETKHFIY FYLGHCAILL FKTQ