ID A0A1D5RMC1_MOUSE Unreviewed; 406 AA.
AC A0A1D5RMC1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
DE Flags: Fragment;
GN Name=Dync1li2 {ECO:0000313|Ensembl:ENSMUSP00000148716.2,
GN ECO:0000313|MGI:MGI:107738};
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 {ECO:0000313|Ensembl:ENSMUSP00000148716.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:19131326}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [2] {ECO:0000313|Ensembl:ENSMUSP00000148716.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000148716.2,
RC ECO:0000313|Proteomes:UP000000589};
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 [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [4] {ECO:0007829|PubMed:24129315}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24129315;
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).
RN [5] {ECO:0000313|Ensembl:ENSMUSP00000148716.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000148716.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00037133, ECO:0000256|RuleBase:RU366047}.
CC -!- SUBUNIT: Homodimer. 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).
CC {ECO:0000256|RuleBase:RU366047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU366047}.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000256|ARBA:ARBA00006831, ECO:0000256|RuleBase:RU366047}.
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DR jPOST; A0A1D5RMC1; -.
DR ProteomicsDB; 363320; -.
DR Antibodypedia; 29288; 126 antibodies from 24 providers.
DR Ensembl; ENSMUST00000212230.2; ENSMUSP00000148716.2; ENSMUSG00000035770.9.
DR AGR; MGI:107738; -.
DR MGI; MGI:107738; Dync1li2.
DR VEuPathDB; HostDB:ENSMUSG00000035770; -.
DR GeneTree; ENSGT00390000008295; -.
DR ChiTaRS; Dync1li2; mouse.
DR Proteomes; UP000000589; Chromosome 8.
DR Bgee; ENSMUSG00000035770; Expressed in embryonic brain and 225 other cell types or tissues.
DR ExpressionAtlas; A0A1D5RMC1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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:SF1; CYTOPLASMIC DYNEIN 1 LIGHT INTERMEDIATE CHAIN 2; 1.
DR PANTHER; PTHR12688; DYNEIN LIGHT INTERMEDIATE CHAIN; 1.
DR Pfam; PF05783; DLIC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366047};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU366047};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|RuleBase:RU366047}; Dynein {ECO:0000256|RuleBase:RU366047};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU366047};
KW Motor protein {ECO:0000256|RuleBase:RU366047};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366047};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|EPD:A0A1D5RMC1,
KW ECO:0007829|MaxQB:A0A1D5RMC1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT REGION 116..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000148716.2"
SQ SEQUENCE 406 AA; 45352 MW; 3E9510D8718B31D7 CRC64;
XLQGAEHGKK GRGLEYLYLS VHDEDRDDHT RCNVWILDGD LYHKGLLKFA VSAESLRETL
VIFVADMSRP WTIMESLQKW ASVLREHIDK MKIPPEEMRD LERKFMKEFQ DYIEPEEGCQ
GSPQRRGPLT SGSDEDSVAL PLGDNVLTHN LGIPVLVVCT KCDAMSVLEK EHDYRDEHLD
FIQAHLRRFC LQYGAALIYT SVKEEKNLDL LYKYIVHKTY GFHFTIPALV VEKDAVFIPA
GWDNEKKIAI LHENFTTVKP EDAYEDFIVK PPVRKLVHDK ELAAEDEQVF LMKQQESPAR
GPSGSPRTQG RGGPASVPSA SPGTSVKKPD PNIKNNAASE GVLASFFNSL LSKKTGSPGS
PSAGGVQSTA KKSGQKTVLS NVQEELDRMT RKPDSMVTNS STENEA
//
