DYL1_RAT
ID DYL1_RAT Reviewed; 89 AA.
AC P63170; Q15701;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Dynein light chain 1, cytoplasmic;
DE AltName: Full=8 kDa dynein light chain;
DE Short=DLC8;
DE AltName: Full=Dynein light chain LC8-type 1;
DE AltName: Full=Protein inhibitor of neuronal nitric oxide synthase;
DE Short=PIN;
GN Name=Dynll1; Synonyms=Dncl1, Dnclc1, Pin;
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].
RX PubMed=8864115; DOI=10.1126/science.274.5288.774;
RA Jaffrey S.R., Snyder S.H.;
RT "PIN: an associated protein inhibitor of neuronal nitric oxide synthase.";
RL Science 274:774-777(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9299562; DOI=10.1006/bbrc.1997.7361;
RA Greenwood M.T., Guo Y., Kumar U., Beausejours S., Hussain S.N.A.;
RT "Distribution of protein inhibitor of neuronal nitric oxide synthase in rat
RT brain.";
RL Biochem. Biophys. Res. Commun. 238:617-621(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [4]
RP PROTEIN SEQUENCE OF 50-60, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [5]
RP IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8702622; DOI=10.1074/jbc.271.32.19358;
RA King S.M., Barbarese E., Dillman J.F. III, Patel-King R.S., Carson J.H.,
RA Pfister K.K.;
RT "Brain cytoplasmic and flagellar outer arm dyneins share a highly conserved
RT Mr 8,000 light chain.";
RL J. Biol. Chem. 271:19358-19366(1996).
RN [6]
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 [7]
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 [8]
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 [9]
RP INTERACTION WITH BCL2L11.
RX PubMed=21478148; DOI=10.1074/jbc.m110.197707;
RA Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P.,
RA Henshall D.C., Morris K.T., Simon R.P., Meller R.;
RT "Identification of a novel Bcl-2-interacting mediator of cell death (Bim)
RT E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in
RT rapid ischemic tolerance-induced neuroprotection.";
RL J. Biol. Chem. 286:19331-19339(2011).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=11178896; DOI=10.1006/jmbi.2000.4374;
RA Fan J.-S., Zhang Q., Tochio H., Li M., Zhang M.;
RT "Structural basis of diverse sequence-dependent target recognition by the 8
RT kDa dynein light chain.";
RL J. Mol. Biol. 306:97-108(2001).
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.
CC -!- FUNCTION: Binds and inhibits the catalytic activity of neuronal nitric
CC oxide synthase.
CC -!- FUNCTION: Promotes transactivation functions of ESR1 and plays a role
CC in the nuclear localization of ESR1. {ECO:0000250|UniProtKB:P63167}.
CC -!- FUNCTION: Regulates apoptotic activities of BCL2L11 by sequestering it
CC to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex
CC dissociates from cytoplasmic dynein and translocates to mitochondria
CC and sequesters BCL2 thus neutralizing its antiapoptotic activity (By
CC similarity). {ECO:0000250|UniProtKB:P63167}.
CC -!- SUBUNIT: Homodimer. Monomer; the monomeric form is incapable of binding
CC to target proteins (By similarity). 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. The ICs and LICs
CC bind directly to the HC dimer and the LCs assemble on the IC dimer
CC (PubMed:8702622, PubMed:11746667). Interacts with TXNDC17. Interacts
CC with WWC1 and ESR1. The interaction with WWC1 is mandatory for the
CC recruitment and transactivation functions of ESR1 or DYNLL1 to the
CC target chromatin (By similarity). Interacts with BCL2L11
CC (PubMed:21478148). Interacts with BCL2; the interaction is greatly
CC enhanced in the nucleus and in mitochondria upon induction of
CC apoptosis. Interacts with PAK1; the interaction requires dimeric DYNLL1
CC (By similarity). Interacts with MYZAP. Part of an astrin (SPAG5)-
CC kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and
CC SGO2. Interacts with ATMIN; this interaction inhibits ATMIN
CC transcriptional activity and hence may play a role in a feedback loop
CC whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN.
CC Interacts with NEK9 (not phosphorylated at 'Ser-944'). Interacts with
CC BICD2 (By similarity). Interacts with BCAS1 (PubMed:16133941).
CC Interacts with Bassoon/BSN (By similarity). Interacts with HDAC6 (By
CC similarity). Interacts with TPPP (By similarity). Interacts with AMBRA1
CC (via TQT motifs); tethering AMBRA1 to the cytoskeleton (By similarity).
CC Interacts with FAM83D/CHICA (via C-terminus) (By similarity). Interacts
CC with HMMR, SPAG5/Astrin and KNSTRN/Kinastrin (By similarity).
CC {ECO:0000250|UniProtKB:P63167, ECO:0000250|UniProtKB:P63168,
CC ECO:0000269|PubMed:11746667, ECO:0000269|PubMed:16133941,
CC ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:8702622}.
CC -!- SUBUNIT: (Microbial infection) Interacts with rabies virus
CC phosphoprotein. {ECO:0000269|PubMed:11602781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:P63167}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:P63167}. Nucleus
CC {ECO:0000250|UniProtKB:P63167}. Mitochondrion
CC {ECO:0000250|UniProtKB:P63167}. Note=Upon induction of apoptosis
CC translocates together with BCL2L11 to mitochondria.
CC {ECO:0000250|UniProtKB:P63167}.
CC -!- TISSUE SPECIFICITY: Weaker expression in the cerebellum and spinal cord
CC compared with other brain regions.
CC -!- PTM: Phosphorylation at Ser-88 appears to control the dimer-monomer
CC transition. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
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DR EMBL; U66461; AAB38257.1; -; mRNA.
DR EMBL; BC063183; AAH63183.1; -; mRNA.
DR PIR; JC5633; JC5633.
DR RefSeq; NP_445771.1; NM_053319.3.
DR PDB; 1F3C; NMR; -; A/B=1-89.
DR PDB; 1F95; NMR; -; A/B=1-89.
DR PDB; 1F96; NMR; -; A/B=1-89.
DR PDBsum; 1F3C; -.
DR PDBsum; 1F95; -.
DR PDBsum; 1F96; -.
DR AlphaFoldDB; P63170; -.
DR SMR; P63170; -.
DR BioGRID; 248680; 4.
DR CORUM; P63170; -.
DR IntAct; P63170; 36.
DR MINT; P63170; -.
DR STRING; 10116.ENSRNOP00000061342; -.
DR iPTMnet; P63170; -.
DR PhosphoSitePlus; P63170; -.
DR jPOST; P63170; -.
DR PaxDb; P63170; -.
DR PRIDE; P63170; -.
DR Ensembl; ENSRNOT00000014910; ENSRNOP00000061342; ENSRNOG00000011222.
DR GeneID; 58945; -.
DR KEGG; rno:58945; -.
DR UCSC; RGD:619866; rat.
DR CTD; 8655; -.
DR RGD; 619866; Dynll1.
DR eggNOG; KOG3430; Eukaryota.
DR GeneTree; ENSGT00390000000378; -.
DR HOGENOM; CLU_070944_4_0_1; -.
DR InParanoid; P63170; -.
DR OMA; KHSPTWH; -.
DR OrthoDB; 1520814at2759; -.
DR PhylomeDB; P63170; -.
DR TreeFam; TF300264; -.
DR Reactome; R-RNO-111446; Activation of BIM 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-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-5620924; Intraflagellar transport.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
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-8854518; AURKA Activation by TPX2.
DR Reactome; R-RNO-9646399; Aggrephagy.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR EvolutionaryTrace; P63170; -.
DR PRO; PR:P63170; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000011222; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; P63170; RN.
DR GO; GO:1904115; C:axon cytoplasm; IDA:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005929; C:cilium; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030286; C:dynein complex; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0045505; F:dynein intermediate chain binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; IDA:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO: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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035721; P:intraciliary retrograde transport; ISO:RGD.
DR GO; GO:0044458; P:motile cilium assembly; ISO:RGD.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:MGI.
DR GO; GO:0042326; P:negative regulation of phosphorylation; ISO:RGD.
DR GO; GO:0042133; P:neurotransmitter metabolic process; TAS:ProtInc.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; TAS:ProtInc.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:RGD.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; IEP:RGD.
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; Acetylation; Activator; Apoptosis; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Dynein; Isopeptide bond; Microtubule;
KW Mitochondrion; Motor protein; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..89
FT /note="Dynein light chain 1, cytoplasmic"
FT /id="PRO_0000195129"
FT REGION 67..89
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63167"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63167"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63167"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1F3C"
FT HELIX 15..31
FT /evidence="ECO:0007829|PDB:1F3C"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:1F3C"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:1F3C"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1F3C"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1F3C"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1F3C"
SQ SEQUENCE 89 AA; 10366 MW; F5E7647D092BEB3A CRC64;
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG
