DYL2_MOUSE
ID DYL2_MOUSE Reviewed; 89 AA.
AC Q9D0M5; A7M7R8; Q3TFB4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Dynein light chain 2, cytoplasmic;
DE AltName: Full=8 kDa dynein light chain b;
DE Short=DLC8;
DE Short=DLC8b;
DE AltName: Full=Dynein light chain LC8-type 2;
GN Name=Dynll2; Synonyms=Dlc2;
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], INTERACTION WITH BMF, IDENTIFICATION IN THE
RP CYTOPLASMIC DYNEIN 1 COMPLEX, AND IDENTIFICATION IN THE MYOSIN V COMPLEX.
RC STRAIN=C57BL/6J;
RX PubMed=11546872; DOI=10.1126/science.1062257;
RA Puthalakath H., Villunger A., O'Reilly L.A., Beaumont J.G., Coultas L.,
RA Cheney R.E., Huang D.C.S., Strasser A.;
RT "Bmf: a proapoptotic BH3-only protein regulated by interaction with the
RT myosin V actin motor complex, activated by anoikis.";
RL Science 293:1829-1832(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Kidney, and Spinal cord;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 [5]
RP INTERACTION WITH DYNC1I1.
RX PubMed=11148209; DOI=10.1074/jbc.m010320200;
RA Lo K.W., Naisbitt S., Fan J.S., Sheng M., Zhang M.;
RT "The 8-kDa dynein light chain binds to its targets via a conserved
RT (K/R)XTQT motif.";
RL J. Biol. Chem. 276:14059-14066(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, and Liver;
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 [7]
RP STRUCTURE BY NMR, SUBCELLULAR LOCATION, AND BINDING SITE.
RX PubMed=14561217; DOI=10.1042/bj20031251;
RA Day C.L., Puthalakath H., Skea G., Strasser A., Barsukov I., Lian L.Y.,
RA Huang D.C., Hinds M.G.;
RT "Localization of dynein light chains 1 and 2 and their pro-apoptotic
RT ligands.";
RL Biochem. J. 377:597-605(2004).
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 (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. Dynein ICs and LICs
CC bind directly to the HC dimer and the LCs assemble on the IC dimer
CC (PubMed:11546872). Interacts with DYNC1I1 (PubMed:11148209). Interacts
CC with BMF (PubMed:11546872). Component of the myosin V motor complex
CC (PubMed:11546872). Interacts with BCAS1 (By similarity). Interacts with
CC Basson/BSN (By similarity). Interacts with AMBRA1 (via TQT motifs);
CC tethering AMBRA1 to the cytoskeleton (By similarity).
CC {ECO:0000250|UniProtKB:Q78P75, ECO:0000250|UniProtKB:Q96FJ2,
CC ECO:0000269|PubMed:11148209, ECO:0000269|PubMed:11546872}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14561217}.
CC -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
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DR EMBL; AY029255; AAK38749.1; -; mRNA.
DR EMBL; AK011284; BAB27516.1; -; mRNA.
DR EMBL; AK028319; BAC25877.1; -; mRNA.
DR EMBL; AK049645; BAC33856.1; -; mRNA.
DR EMBL; AK078434; BAC37271.1; -; mRNA.
DR EMBL; AK160114; BAE35638.1; -; mRNA.
DR EMBL; AK169212; BAE40984.1; -; mRNA.
DR EMBL; AL606805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011289; AAH11289.1; -; mRNA.
DR EMBL; BC040822; AAH40822.1; -; mRNA.
DR CCDS; CCDS36272.1; -.
DR RefSeq; NP_001161943.1; NM_001168471.1.
DR RefSeq; NP_001161944.1; NM_001168472.1.
DR RefSeq; NP_080832.1; NM_026556.4.
DR PDB; 1RE6; NMR; -; A/B=1-89.
DR PDBsum; 1RE6; -.
DR AlphaFoldDB; Q9D0M5; -.
DR SMR; Q9D0M5; -.
DR BioGRID; 212654; 11.
DR IntAct; Q9D0M5; 4.
DR MINT; Q9D0M5; -.
DR STRING; 10090.ENSMUSP00000020775; -.
DR iPTMnet; Q9D0M5; -.
DR PhosphoSitePlus; Q9D0M5; -.
DR SwissPalm; Q9D0M5; -.
DR REPRODUCTION-2DPAGE; Q9D0M5; -.
DR EPD; Q9D0M5; -.
DR jPOST; Q9D0M5; -.
DR MaxQB; Q9D0M5; -.
DR PaxDb; Q9D0M5; -.
DR PeptideAtlas; Q9D0M5; -.
DR PRIDE; Q9D0M5; -.
DR ProteomicsDB; 277648; -.
DR TopDownProteomics; Q9D0M5; -.
DR Antibodypedia; 71353; 156 antibodies from 27 providers.
DR DNASU; 68097; -.
DR Ensembl; ENSMUST00000020775; ENSMUSP00000020775; ENSMUSG00000020483.
DR Ensembl; ENSMUST00000107923; ENSMUSP00000103556; ENSMUSG00000020483.
DR Ensembl; ENSMUST00000178105; ENSMUSP00000136241; ENSMUSG00000020483.
DR GeneID; 68097; -.
DR KEGG; mmu:68097; -.
DR UCSC; uc007kva.2; mouse.
DR CTD; 140735; -.
DR MGI; MGI:1915347; Dynll2.
DR VEuPathDB; HostDB:ENSMUSG00000020483; -.
DR eggNOG; KOG3430; Eukaryota.
DR GeneTree; ENSGT00390000000378; -.
DR HOGENOM; CLU_070944_4_0_1; -.
DR InParanoid; Q9D0M5; -.
DR OMA; RHGATWH; -.
DR OrthoDB; 1520814at2759; -.
DR PhylomeDB; Q9D0M5; -.
DR TreeFam; TF300264; -.
DR Reactome; R-MMU-139910; Activation of BMF 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-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
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-9646399; Aggrephagy.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 68097; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Dynll2; mouse.
DR EvolutionaryTrace; Q9D0M5; -.
DR PRO; PR:Q9D0M5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D0M5; protein.
DR Bgee; ENSMUSG00000020483; Expressed in motor neuron and 267 other tissues.
DR ExpressionAtlas; Q9D0M5; baseline and differential.
DR Genevisible; Q9D0M5; MM.
DR GO; GO:0097731; C:9+0 non-motile cilium; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IPI:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031475; C:myosin V complex; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO: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: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; Dynein; Microtubule; Motor protein;
KW Reference proteome; Transport.
FT CHAIN 1..89
FT /note="Dynein light chain 2, cytoplasmic"
FT /id="PRO_0000195133"
FT SITE 41
FT /note="Interaction with myosin V motor complex"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1RE6"
FT HELIX 15..31
FT /evidence="ECO:0007829|PDB:1RE6"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:1RE6"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1RE6"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1RE6"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1RE6"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1RE6"
SQ SEQUENCE 89 AA; 10350 MW; 45364D32C0077F8E CRC64;
MSDRKAVIKN ADMSEDMQQD AVDCATQAME KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG
