DYL1_MOUSE
ID DYL1_MOUSE Reviewed; 89 AA.
AC P63168; Q15701; Q3UGE7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 168.
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;
DE Short=mPIN;
GN Name=Dynll1; Synonyms=Dlc1, Dncl1, Dnclc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Mount D.B.;
RT "Intra-renal localization of mPIN (Protein Inhibitor of Nitric oxide
RT synthase).";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
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 [6]
RP INTERACTION WITH BICD2.
RX PubMed=22956769; DOI=10.1091/mbc.e12-03-0210;
RA Splinter D., Razafsky D.S., Schlager M.A., Serra-Marques A., Grigoriev I.,
RA Demmers J., Keijzer N., Jiang K., Poser I., Hyman A.A., Hoogenraad C.C.,
RA King S.J., Akhmanova A.;
RT "BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to
RT cellular structures.";
RL Mol. Biol. Cell 23:4226-4241(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 -!- FUNCTION: Binds and inhibits the catalytic activity of neuronal nitric
CC oxide synthase. {ECO:0000250}.
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. The cytoplasmic dynein 1 complex consists of two
CC catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC presented by intermediate chains (ICs), light intermediate chains
CC (LICs) and light chains (LCs); the composition seems to vary in respect
CC to the IC, LIC and LC composition. The heavy chain homodimer serves as
CC a scaffold for the probable homodimeric assembly of the respective non-
CC catalytic subunits. The ICs and LICs bind directly to the HC dimer and
CC the LCs assemble on the IC dimer. 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. 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
CC DYNLL1. Interacts with MYZAP. Part of an astrin (SPAG5)-kinastrin
CC (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2.
CC Interacts with ATMIN; this interaction inhibits ATMIN transcriptional
CC activity and hence may play a role in a feedback loop whereby DYNLL1
CC inhibits transactivation of its own promoter by ATMIN. Interacts with
CC NEK9 (not phosphorylated at 'Ser-944') (By similarity). Interacts with
CC BCL2L11 (PubMed:21478148). Interacts with BICD2 (PubMed:22956769).
CC Interacts with BCAS1 (By similarity). Interacts with Bassoon/BSN (By
CC similarity). Interacts with HDAC6 (By similarity). Interacts with TPPP
CC (By similarity). Interacts with AMBRA1 (via TQT motifs); tethering
CC AMBRA1 to the cytoskeleton (By similarity). Interacts with FAM83D/CHICA
CC (via C-terminus) (By similarity). Interacts with HMMR, SPAG5/Astrin and
CC KNSTRN/Kinastrin (By similarity). {ECO:0000250|UniProtKB:P63167,
CC ECO:0000250|UniProtKB:P63170, ECO:0000269|PubMed:21478148,
CC ECO:0000269|PubMed:22956769}.
CC -!- INTERACTION:
CC P63168; Q64368: Dazl; NbExp=12; IntAct=EBI-349121, EBI-2024439;
CC P63168; O88485: Dync1i1; NbExp=2; IntAct=EBI-349121, EBI-492834;
CC P63168; P26367: PAX6; Xeno; NbExp=3; IntAct=EBI-349121, EBI-747278;
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 -!- 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; AF020185; AAD01643.1; -; mRNA.
DR EMBL; AK002522; BAB22160.1; -; mRNA.
DR EMBL; AK010614; BAB27063.1; -; mRNA.
DR EMBL; AK010685; BAB27117.1; -; mRNA.
DR EMBL; AK013721; BAB28970.1; -; mRNA.
DR EMBL; AK082923; BAC38691.1; -; mRNA.
DR EMBL; AK147977; BAE28262.1; -; mRNA.
DR EMBL; BC008106; AAH08106.1; -; mRNA.
DR EMBL; BC034258; AAH34258.1; -; mRNA.
DR CCDS; CCDS39227.1; -.
DR RefSeq; NP_062656.3; NM_019682.4.
DR AlphaFoldDB; P63168; -.
DR BMRB; P63168; -.
DR SMR; P63168; -.
DR BioGRID; 207994; 118.
DR ComplexPortal; CPX-5699; Cytoplasmic dynein complex, variant 1.
DR ELM; P63168; -.
DR IntAct; P63168; 74.
DR MINT; P63168; -.
DR STRING; 10090.ENSMUSP00000009157; -.
DR iPTMnet; P63168; -.
DR PhosphoSitePlus; P63168; -.
DR EPD; P63168; -.
DR jPOST; P63168; -.
DR MaxQB; P63168; -.
DR PaxDb; P63168; -.
DR PeptideAtlas; P63168; -.
DR PRIDE; P63168; -.
DR ProteomicsDB; 277617; -.
DR TopDownProteomics; P63168; -.
DR Antibodypedia; 31481; 306 antibodies from 30 providers.
DR DNASU; 56455; -.
DR Ensembl; ENSMUST00000009157; ENSMUSP00000009157; ENSMUSG00000009013.
DR Ensembl; ENSMUST00000112090; ENSMUSP00000107720; ENSMUSG00000009013.
DR GeneID; 56455; -.
DR KEGG; mmu:56455; -.
DR UCSC; uc008zdp.2; mouse.
DR CTD; 8655; -.
DR MGI; MGI:1861457; Dynll1.
DR VEuPathDB; HostDB:ENSMUSG00000009013; -.
DR eggNOG; KOG3430; Eukaryota.
DR GeneTree; ENSGT00390000000378; -.
DR HOGENOM; CLU_070944_4_0_1; -.
DR InParanoid; P63168; -.
DR OMA; KHSPTWH; -.
DR OrthoDB; 1520814at2759; -.
DR PhylomeDB; P63168; -.
DR TreeFam; TF300264; -.
DR Reactome; R-MMU-111446; Activation of BIM and translocation to mitochondria.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 56455; 12 hits in 39 CRISPR screens.
DR ChiTaRS; Dynll1; mouse.
DR PRO; PR:P63168; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P63168; protein.
DR Bgee; ENSMUSG00000009013; Expressed in floor plate of midbrain and 249 other tissues.
DR Genevisible; P63168; MM.
DR GO; GO:1904115; C:axon cytoplasm; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005929; C:cilium; IEA:GOC.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IPI:MGI.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030286; C:dynein complex; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0045505; F:dynein intermediate chain binding; IPI:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035721; P:intraciliary retrograde transport; IMP:MGI.
DR GO; GO:0044458; P:motile cilium assembly; IMP:MGI.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0042326; P:negative regulation of phosphorylation; ISO:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
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 Acetylation; Activator; Apoptosis; Cytoplasm; Cytoskeleton; Dynein;
KW Isopeptide bond; Microtubule; Mitochondrion; Motor protein; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..89
FT /note="Dynein light chain 1, cytoplasmic"
FT /id="PRO_0000195127"
FT REGION 67..89
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
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"
SQ SEQUENCE 89 AA; 10366 MW; F5E7647D092BEB3A CRC64;
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG
