DC1L2_MOUSE
ID DC1L2_MOUSE Reviewed; 492 AA.
AC Q6PDL0; Q3UGJ3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cytoplasmic dynein 1 light intermediate chain 2;
DE AltName: Full=Dynein light intermediate chain 2, cytosolic;
GN Name=Dync1li2; Synonyms=Dncli2, Dnclic2;
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=C57BL/6J; TISSUE=Bone marrow, Head, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 IDENTIFICATION BY 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-446, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-397, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 (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 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {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; AK140743; BAE24463.1; -; mRNA.
DR EMBL; AK147899; BAE28215.1; -; mRNA.
DR EMBL; AK152157; BAE30992.1; -; mRNA.
DR EMBL; AK161434; BAE36394.1; -; mRNA.
DR EMBL; BC058645; AAH58645.1; -; mRNA.
DR CCDS; CCDS22579.1; -.
DR RefSeq; NP_001013398.2; NM_001013380.2.
DR AlphaFoldDB; Q6PDL0; -.
DR SMR; Q6PDL0; -.
DR BioGRID; 231551; 15.
DR ComplexPortal; CPX-5699; Cytoplasmic dynein complex, variant 1.
DR STRING; 10090.ENSMUSP00000045480; -.
DR iPTMnet; Q6PDL0; -.
DR PhosphoSitePlus; Q6PDL0; -.
DR SwissPalm; Q6PDL0; -.
DR EPD; Q6PDL0; -.
DR jPOST; Q6PDL0; -.
DR MaxQB; Q6PDL0; -.
DR PaxDb; Q6PDL0; -.
DR PeptideAtlas; Q6PDL0; -.
DR PRIDE; Q6PDL0; -.
DR ProteomicsDB; 279172; -.
DR Antibodypedia; 29288; 116 antibodies from 23 providers.
DR DNASU; 234663; -.
DR Ensembl; ENSMUST00000041769; ENSMUSP00000045480; ENSMUSG00000035770.
DR GeneID; 234663; -.
DR KEGG; mmu:234663; -.
DR UCSC; uc009nao.2; mouse.
DR CTD; 1783; -.
DR MGI; MGI:107738; Dync1li2.
DR VEuPathDB; HostDB:ENSMUSG00000035770; -.
DR eggNOG; KOG3905; Eukaryota.
DR GeneTree; ENSGT00390000008295; -.
DR HOGENOM; CLU_021937_2_1_1; -.
DR InParanoid; Q6PDL0; -.
DR OMA; WKEEEFD; -.
DR OrthoDB; 1299592at2759; -.
DR PhylomeDB; Q6PDL0; -.
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-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; 234663; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Dync1li2; mouse.
DR PRO; PR:Q6PDL0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6PDL0; protein.
DR Bgee; ENSMUSG00000035770; Expressed in embryonic brain and 222 other tissues.
DR ExpressionAtlas; Q6PDL0; baseline and differential.
DR Genevisible; Q6PDL0; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISO:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008467; Dynein1_light_intermed_chain.
DR InterPro; IPR022780; Dynein_light_int_chain.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12688; PTHR12688; 1.
DR Pfam; PF05783; DLIC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Dynein; Methylation; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..492
FT /note="Cytoplasmic dynein 1 light intermediate chain 2"
FT /id="PRO_0000114672"
FT REGION 188..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 397
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 353
FT /note="E -> K (in Ref. 2; AAH58645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 54218 MW; 6418DF74FFD7175E CRC64;
MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRARSK LPSGKNILVF
GEDGSGKTTL MTKLQGAEHG KKGRGLEYLY LSVHDEDRDD HTRCNVWILD GDLYHKGLLK
FAVSAESLRE TLVIFVADMS RPWTIMESLQ KWASVLREHI DKMKIPPEEM RDLERKFMKE
FQDYIEPEEG CQGSPQRRGP LTSGSDEDSV ALPLGDNVLT HNLGIPVLVV CTKCDAMSVL
EKEHDYRDEH LDFIQAHLRR FCLQYGAALI YTSVKEEKNL DLLYKYIVHK TYGFHFTIPA
LVVEKDAVFI PAGWDNEKKI AILHENFTTV KPEDAYEDFI VKPPVRKLVH DKELAAEDEQ
VFLMKQQSLL AKQPATPTRT SESPARGPSG SPRTQGRGGP ASVPSASPGT SVKKPDPNIK
NNAASEGVLA SFFNSLLSKK TGSPGSPSAG GVQSTAKKSG QKTVLSNVQE ELDRMTRKPD
SMVTNSSTEN EA
