ID DC1L1_MOUSE Reviewed; 523 AA. AC Q8R1Q8; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Cytoplasmic dynein 1 light intermediate chain 1; DE AltName: Full=Dynein light chain A; DE Short=DLC-A; DE AltName: Full=Dynein light intermediate chain 1, cytosolic; GN Name=Dync1li1; Synonyms=Dncli1, Dnclic1; 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 [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; 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 [2] RP PROTEIN SEQUENCE OF 134-142, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-405, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., RA Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in naive RT and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-510; THR-513; RP THR-515 AND SER-516, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-510; THR-512; RP THR-513; THR-515 AND SER-516, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC 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). 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 binding dynein to membranous organelles or chromosomes. CC Probably involved in the microtubule-dependent transport of CC pericentrin. Is required for progress through the spindle assembly CC checkpoint. The phosphorylated form appears to be involved in the CC selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores CC (By similarity). Forms a functional Rab11/RAB11FIP3/dynein complex onto CC endosomal membrane that regulates the movement of peripheral sorting CC endosomes (SE) along microtubule tracks toward the microtubule CC organizing center/centrosome, generating the endosomal recycling CC compartment (ERC) (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:Q9Y6G9}. 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 presented by 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 Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind CC mutually exclusive to DYNC1H1. Interacts with PCNT (By similarity). CC Forms a complex with RAB11FIP3 and RAB11A1; the interaction between CC DYNC1LI1 and RAB11FIP3 is direct and induces DYNC1LI1 localization onto CC endosomal membrane; the complex regulates endocytic trafficking (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9Y6G9}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere, CC kinetochore {ECO:0000250|UniProtKB:Q9Y6G9}. Cytoplasm, cytoskeleton, CC spindle pole {ECO:0000250|UniProtKB:Q9Y6G9}. Recycling endosome CC membrane {ECO:0000250|UniProtKB:Q9Y6G9}. CC -!- PTM: Phosphorylated during mitosis but not in interphase. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family. CC {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; BC023347; AAH23347.1; -; mRNA. DR CCDS; CCDS23595.1; -. DR RefSeq; NP_666341.1; NM_146229.2. DR AlphaFoldDB; Q8R1Q8; -. DR SMR; Q8R1Q8; -. DR BioGRID; 231702; 87. DR IntAct; Q8R1Q8; 52. DR MINT; Q8R1Q8; -. DR STRING; 10090.ENSMUSP00000035366; -. DR GlyGen; Q8R1Q8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8R1Q8; -. DR PhosphoSitePlus; Q8R1Q8; -. DR SwissPalm; Q8R1Q8; -. DR EPD; Q8R1Q8; -. DR jPOST; Q8R1Q8; -. DR MaxQB; Q8R1Q8; -. DR PaxDb; 10090-ENSMUSP00000035366; -. DR ProteomicsDB; 279830; -. DR Pumba; Q8R1Q8; -. DR Antibodypedia; 27761; 296 antibodies from 24 providers. DR DNASU; 235661; -. DR Ensembl; ENSMUST00000047404.7; ENSMUSP00000035366.7; ENSMUSG00000032435.10. DR GeneID; 235661; -. DR KEGG; mmu:235661; -. DR UCSC; uc009rxy.1; mouse. DR AGR; MGI:2135610; -. DR CTD; 51143; -. DR MGI; MGI:2135610; Dync1li1. DR VEuPathDB; HostDB:ENSMUSG00000032435; -. DR eggNOG; KOG3905; Eukaryota. DR GeneTree; ENSGT00390000008295; -. DR HOGENOM; CLU_021937_2_1_1; -. DR InParanoid; Q8R1Q8; -. DR OMA; VMLEKDF; -. DR OrthoDB; 179830at2759; -. DR PhylomeDB; Q8R1Q8; -. DR TreeFam; TF352602; -. DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. 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-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-9646399; Aggrephagy. DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation. DR BioGRID-ORCS; 235661; 3 hits in 77 CRISPR screens. DR ChiTaRS; Dync1li1; mouse. DR PRO; PR:Q8R1Q8; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q8R1Q8; Protein. DR Bgee; ENSMUSG00000032435; Expressed in cortical plate and 234 other cell types or tissues. DR ExpressionAtlas; Q8R1Q8; baseline and differential. DR GO; GO:0005813; C:centrosome; ISO:MGI. DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB. DR GO; GO:0030666; C:endocytic vesicle membrane; ISS:UniProtKB. DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0045504; F:dynein heavy chain binding; ISO:MGI. DR GO; GO:0019003; F:GDP binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0003777; F:microtubule motor activity; ISS:MGI. DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISO:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0007018; P:microtubule-based movement; ISS:UniProtKB. DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB. DR GO; GO:0046605; P:regulation of centrosome cycle; ISO:MGI. DR GO; GO:0060627; P:regulation of vesicle-mediated transport; ISS:UniProtKB. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR008467; Dynein1_light_intermed_chain. DR InterPro; IPR022780; Dynein_light_int_chain. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR12688:SF2; CYTOPLASMIC DYNEIN 1 LIGHT INTERMEDIATE CHAIN 1; 1. DR PANTHER; PTHR12688; DYNEIN LIGHT INTERMEDIATE CHAIN; 1. DR Pfam; PF05783; DLIC; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; Q8R1Q8; MM. PE 1: Evidence at protein level; KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Dynein; Endosome; Kinetochore; KW Membrane; Microtubule; Mitosis; Motor protein; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transport. FT CHAIN 1..523 FT /note="Cytoplasmic dynein 1 light intermediate chain 1" FT /id="PRO_0000114667" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 200..219 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 387..434 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 457..523 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 405..422 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 506..523 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 74..81 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT MOD_RES 213 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9" FT MOD_RES 398 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9" FT MOD_RES 405 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087" FT MOD_RES 408 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9" FT MOD_RES 412 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9" FT MOD_RES 419 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9" FT MOD_RES 486 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9" FT MOD_RES 510 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 512 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 513 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 515 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 516 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079" SQ SEQUENCE 523 AA; 56614 MW; F080D6865A399498 CRC64; MAAVGRVGSF GSSPPGLAST YASGPLANEL ASGSGGPAAG DDEDGQNLWS CILSEVSTRS RSKLPTGKNV LLLGEDGAGK TSLIRRIQGI EEYKKGRGLE YLYLNVHDED RDDQTRCNVW ILDGDLYHKG LLKFSLDALS LRDTLVMLVV DMSKPWTALD SLQKWASVVR EHVDKLKIPP EEMKEMEQKL IRDFQEYVEP GEDFPASPQR RTTGAQEDRG DSVVLPLGAD TLTHNLGLPV LVVCTKCDAI SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKVEDNFE DIITKPPVRK FVHEKEIMAE DDQVFLMKLQ SLLAKQPPTA AGRPVDASPR VPGGSPRTPN RSVSSNVASV SPIPAGSKKI DPNMKAGATS EGVLANFFNS LLSKKTGSPG GPGVGGSPGG GAAGASPSLP PSAKKSGQKP VLSDVHAELD RITRKPASVS PTTPTSPTEG EAS //