DYL2_RAT
ID DYL2_RAT Reviewed; 89 AA.
AC Q78P75;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Dynein light chain 2, cytoplasmic;
DE AltName: Full=Dynein light chain LC8-type 2;
GN Name=Dynll2; Synonyms=Dlc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP GPHN.
RX PubMed=12097491; DOI=10.1523/jneurosci.22-13-05393.2002;
RA Fuhrmann J.C., Kins S., Rostaing P., El Far O., Kirsch J., Sheng M.,
RA Triller A., Betz H., Kneussel M.;
RT "Gephyrin interacts with dynein light chains 1 and 2, components of motor
RT protein complexes.";
RL J. Neurosci. 22:5393-5402(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 32-43 AND 72-87, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Diao W., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
RX PubMed=11746667; DOI=10.1002/cm.1036;
RA Wilson M.J., Salata M.W., Susalka S.J., Pfister K.K.;
RT "Light chains of mammalian cytoplasmic dynein: identification and
RT characterization of a family of LC8 light chains.";
RL Cell Motil. Cytoskeleton 49:229-240(2001).
RN [5]
RP INTERACTION WITH RABIES VIRUS PHOSPHOPROTEIN (MICROBIAL INFECTION).
RX PubMed=11602781; DOI=10.1099/0022-1317-82-11-2691;
RA Poisson N., Real E., Gaudin Y., Vaney M.C., King S., Jacob Y., Tordo N.,
RA Blondel D.;
RT "Molecular basis for the interaction between rabies virus phosphoprotein P
RT and the dynein light chain LC8: dissociation of dynein-binding properties
RT and transcriptional functionality of P.";
RL J. Gen. Virol. 82:2691-2696(2001).
RN [6]
RP INTERACTION WITH BCAS1.
RC TISSUE=Brain;
RX PubMed=16133941; DOI=10.1007/s10571-005-4955-5;
RA Ninomiya K., Ishimoto T., Taguchi T.;
RT "Subcellular localization of PMES-2 proteins regulated by their two
RT cytoskeleton-associated domains.";
RL Cell. Mol. Neurobiol. 25:899-911(2005).
RN [7]
RP STRUCTURE BY NMR, AND SUBUNIT.
RX PubMed=12904292; DOI=10.1074/jbc.m307118200;
RA Wang W., Lo K.-W., Kan H.-M., Fan J.-S., Zhang M.;
RT "Structure of the monomeric 8-kDa dynein light chain and mechanism of the
RT domain-swapped dimer assembly.";
RL J. Biol. Chem. 278:41491-41499(2003).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 1 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). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (PubMed:12904292). The cytoplasmic dynein 1 complex
CC consists of two catalytic heavy chains (HCs) and a number of non-
CC catalytic subunits which present intermediate chains (ICs), light
CC intermediate chains (LICs) and light chains (LCs); the composition
CC seems to vary in respect to the IC, LIC and LC composition. The heavy
CC chain homodimer serves as a scaffold for the probable homodimeric
CC assembly of the respective non-catalytic subunits. Dynein ICs and LICs
CC bind directly to the HC dimer and the LCs assemble on the IC dimer
CC (PubMed:11746667). Interacts with DYNC1I1 (By similarity). Interacts
CC with GPHN (PubMed:12097491). Component of the myosin V motor complex
CC (By similarity). Interacts with BMF (By similarity). Interacts with
CC BCAS1 (PubMed:16133941). Interacts with Basson/BSN (By similarity).
CC Interacts with Basson/BSN (By similarity). Interacts with AMBRA1 (via
CC TQT motifs); tethering AMBRA1 to the cytoskeleton (By similarity).
CC {ECO:0000250|UniProtKB:Q96FJ2, ECO:0000250|UniProtKB:Q9D0M5,
CC ECO:0000269|PubMed:11746667, ECO:0000269|PubMed:12097491,
CC ECO:0000269|PubMed:12904292, ECO:0000269|PubMed:16133941}.
CC -!- SUBUNIT: (Microbial infection) Interacts with rabies virus
CC phosphoprotein. {ECO:0000269|PubMed:11602781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12097491}.
CC -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
CC -!- CAUTION: As DLC8 is commonly used to refer to both DLC1 and DLC2
CC proteins, it is preferable to adopt the following nomenclature (see
CC PubMed:11602781) where DLC8a and DLC8b corresponds respectively to DLC1
CC and DLC2. {ECO:0000305}.
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DR EMBL; AY034383; AAK57536.1; -; mRNA.
DR EMBL; BC061874; AAH61874.1; -; mRNA.
DR RefSeq; NP_542428.1; NM_080697.2.
DR RefSeq; XP_006247139.1; XM_006247077.3.
DR PDB; 1PWJ; NMR; -; A=1-89.
DR PDB; 1PWK; NMR; -; A=1-89.
DR PDBsum; 1PWJ; -.
DR PDBsum; 1PWK; -.
DR AlphaFoldDB; Q78P75; -.
DR SMR; Q78P75; -.
DR BioGRID; 250846; 3.
DR IntAct; Q78P75; 2.
DR MINT; Q78P75; -.
DR STRING; 10116.ENSRNOP00000012279; -.
DR iPTMnet; Q78P75; -.
DR PhosphoSitePlus; Q78P75; -.
DR SwissPalm; Q78P75; -.
DR jPOST; Q78P75; -.
DR PaxDb; Q78P75; -.
DR PRIDE; Q78P75; -.
DR Ensembl; ENSRNOT00000012279; ENSRNOP00000012279; ENSRNOG00000008921.
DR GeneID; 140734; -.
DR KEGG; rno:140734; -.
DR CTD; 140735; -.
DR RGD; 619860; Dynll2.
DR eggNOG; KOG3430; Eukaryota.
DR GeneTree; ENSGT00940000172072; -.
DR HOGENOM; CLU_070944_4_0_1; -.
DR InParanoid; Q78P75; -.
DR OMA; RHGATWH; -.
DR OrthoDB; 1520814at2759; -.
DR PhylomeDB; Q78P75; -.
DR TreeFam; TF300264; -.
DR Reactome; R-RNO-139910; Activation of BMF and translocation to mitochondria.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-5620924; Intraflagellar transport.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9646399; Aggrephagy.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR EvolutionaryTrace; Q78P75; -.
DR PRO; PR:Q78P75; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000008921; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q78P75; RN.
DR GO; GO:0097731; C:9+0 non-motile cilium; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031475; C:myosin V complex; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:RGD.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
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; Direct protein sequencing; Dynein;
KW Microtubule; Motor protein; Reference proteome; Transport.
FT CHAIN 1..89
FT /note="Dynein light chain 2, cytoplasmic"
FT /id="PRO_0000195134"
FT SITE 41
FT /note="Interaction with myosin V motor complex"
FT /evidence="ECO:0000250"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1PWJ"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:1PWJ"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:1PWJ"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:1PWJ"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1PWK"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1PWJ"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:1PWJ"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1PWJ"
SQ SEQUENCE 89 AA; 10350 MW; 45364D32C0077F8E CRC64;
MSDRKAVIKN ADMSEDMQQD AVDCATQAME KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG
