ID   DYL1_YEAST              Reviewed;          92 AA.
AC   Q02647; D6VT54;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Dynein light chain 1, cytoplasmic;
GN   Name=DYN2; Synonyms=SLC1; OrderedLocusNames=YDR424C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8628245; DOI=10.1007/bf02174342;
RA   Dick T., Surana U., Chia W.;
RT   "Molecular and genetic characterization of SLC1, a putative Saccharomyces
RT   cerevisiae homolog of the metazoan cytoplasmic dynein light chain 1.";
RL   Mol. Gen. Genet. 251:38-43(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, IDENTIFICATION IN
RP   THE NUP82 NPC SUBCOMPLEX, INTERACTION WITH NUP159, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=17546040; DOI=10.1038/ncb1604;
RA   Stelter P., Kunze R., Flemming D., Hoepfner D., Diepholz M., Philippsen P.,
RA   Boettcher B., Hurt E.;
RT   "Molecular basis for the functional interaction of dynein light chain with
RT   the nuclear-pore complex.";
RL   Nat. Cell Biol. 9:788-796(2007).
RN   [6]
RP   FUNCTION, SUBUNIT, INTERACTION WITH NUP159, AND SUBCELLULAR LOCATION.
RX   PubMed=23223634; DOI=10.1074/jbc.m112.432831;
RA   Nyarko A., Song Y., Novacek J., Zidek L., Barbar E.;
RT   "Multiple recognition motifs in nucleoporin Nup159 provide a stable and
RT   rigid Nup159-Dyn2 assembly.";
RL   J. Biol. Chem. 288:2614-2622(2013).
RN   [7]
RP   FUNCTION, SUBUNIT, IDENTIFICATION IN THE NUP82 NPC SUBCOMPLEX, INTERACTION
RP   WITH NUP159, AND SUBCELLULAR LOCATION.
RX   PubMed=25646085; DOI=10.1083/jcb.201411003;
RA   Gaik M., Flemming D., von Appen A., Kastritis P., Muecke N., Fischer J.,
RA   Stelter P., Ori A., Bui K.H., Bassler J., Barbar E., Beck M., Hurt E.;
RT   "Structural basis for assembly and function of the Nup82 complex in the
RT   nuclear pore scaffold.";
RL   J. Cell Biol. 208:283-297(2015).
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 where it may contribute to the stable association
CC       of the Nup82 subcomplex with the NPC (PubMed:17546040, PubMed:23223634,
CC       PubMed:25646085). {ECO:0000250, ECO:0000269|PubMed:17546040,
CC       ECO:0000269|PubMed:23223634, ECO:0000269|PubMed:25646085}.
CC   -!- SUBUNIT: Homodimer (PubMed:17546040, PubMed:23223634, PubMed:25646085).
CC       Cytoplasmic dynein consists of two catalytic heavy chains (HCs) and a
CC       number of non-catalytic subunits which present intermediate chains
CC       (ICs), light intermediate chains (LICs) and light chains (LCs).
CC       Component of the nuclear pore complex (NPC) (PubMed:17546040). NPC
CC       constitutes the exclusive means of nucleocytoplasmic transport. NPCs
CC       allow the passive diffusion of ions and small molecules and the active,
CC       nuclear transport receptor-mediated bidirectional transport of
CC       macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and
CC       ribosomal subunits across the nuclear envelope. Due to its 8-fold
CC       rotational symmetry, all subunits are present with 8 copies or
CC       multiples thereof (PubMed:17546040). Part of the NUP82 subcomplex
CC       (PubMed:17546040, PubMed:25646085, PubMed:23223634). In the complex,
CC       interacts directly with Nup159 (PubMed:17546040, PubMed:25646085,
CC       PubMed:23223634). {ECO:0000269|PubMed:17546040,
CC       ECO:0000269|PubMed:23223634, ECO:0000269|PubMed:25646085}.
CC   -!- INTERACTION:
CC       Q02647; P40960: PAC11; NbExp=4; IntAct=EBI-6240, EBI-30551;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus, nuclear pore
CC       complex {ECO:0000269|PubMed:17546040, ECO:0000269|PubMed:23223634,
CC       ECO:0000269|PubMed:25646085}.
CC   -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U36468; AAB03677.1; -; mRNA.
DR   EMBL; U33007; AAB64894.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12264.1; -; Genomic_DNA.
DR   PIR; S66142; S66142.
DR   RefSeq; NP_010712.1; NM_001180732.1.
DR   PDB; 4DS1; X-ray; 1.85 A; A/C=1-92.
DR   PDB; 4HT6; X-ray; 1.90 A; A/C/E=1-92.
DR   PDB; 7N9F; EM; 37.00 A; o/p/q/r/s/t=1-92.
DR   PDBsum; 4DS1; -.
DR   PDBsum; 4HT6; -.
DR   PDBsum; 7N9F; -.
DR   AlphaFoldDB; Q02647; -.
DR   SMR; Q02647; -.
DR   BioGRID; 32483; 148.
DR   ComplexPortal; CPX-1178; Cytoplasmic dynein complex.
DR   ComplexPortal; CPX-824; Nuclear pore complex.
DR   DIP; DIP-6480N; -.
DR   IntAct; Q02647; 4.
DR   MINT; Q02647; -.
DR   STRING; 4932.YDR424C; -.
DR   MaxQB; Q02647; -.
DR   PaxDb; Q02647; -.
DR   PRIDE; Q02647; -.
DR   EnsemblFungi; YDR424C_mRNA; YDR424C; YDR424C.
DR   GeneID; 852034; -.
DR   KEGG; sce:YDR424C; -.
DR   SGD; S000002832; DYN2.
DR   VEuPathDB; FungiDB:YDR424C; -.
DR   eggNOG; KOG3430; Eukaryota.
DR   GeneTree; ENSGT00390000000378; -.
DR   HOGENOM; CLU_070944_4_0_1; -.
DR   InParanoid; Q02647; -.
DR   OMA; RHGATWH; -.
DR   BioCyc; YEAST:G3O-29965-MON; -.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-9646399; Aggrephagy.
DR   PRO; PR:Q02647; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q02647; protein.
DR   GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; IPI:SGD.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:SGD.
DR   GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR   GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR   GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR   GO; GO:1990429; C:peroxisomal importomer complex; IDA:SGD.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:SGD.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IC:ComplexPortal.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0030473; P:nuclear migration along microtubule; IMP:SGD.
DR   GO; GO:0051292; P:nuclear pore complex assembly; IMP:SGD.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   3D-structure; Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW   mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW   Reference proteome; Translocation; Transport.
FT   CHAIN           1..92
FT                   /note="Dynein light chain 1, cytoplasmic"
FT                   /id="PRO_0000195149"
FT   STRAND          10..16
FT                   /evidence="ECO:0007829|PDB:4DS1"
FT   HELIX           18..34
FT                   /evidence="ECO:0007829|PDB:4DS1"
FT   HELIX           38..53
FT                   /evidence="ECO:0007829|PDB:4DS1"
FT   STRAND          57..71
FT                   /evidence="ECO:0007829|PDB:4DS1"
FT   STRAND          75..81
FT                   /evidence="ECO:0007829|PDB:4DS1"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:4DS1"
SQ   SEQUENCE   92 AA;  10441 MW;  C25A690F35C3CEEC CRC64;
     MSDENKSTPI VKASDITDKL KEDILTISKD ALDKYQLERD IAGTVKKQLD VKYGNTWHVI
     VGKNFGSYVT HEKGHFVYFY IGPLAFLVFK TA