Q8R1Q8 (DC1L1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytoplasmic dynein 1 light intermediate chain 1

Alternative name(s):
Dynein light chain A
Short name=DLC-A
Dynein light intermediate chain 1, cytosolic

Gene names

Name:	Dync1li1
Synonyms:	Dncli1, Dnclic1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress throuh the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores By similarity.
Subunit structure	Homodimer By similarity. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with PCNT By similarity.
Subcellular location	Cytoplasm By similarity. Chromosome › centromere › kinetochore By similarity. Cytoplasm › cytoskeleton › spindle pole By similarity.
Post-translational modification	Phosphorylated during mitosis but not in interphase By similarity.
Sequence similarities	Belongs to the dynein light intermediate chain family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Transport
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Dynein Kinetochore Microtubule
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW microtubule-based movement Inferred from sequence or structural similarity PubMed 11243854. Source: MGI mitosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of mitotic cell cycle spindle assembly checkpoint Inferred from sequence or structural similarity. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centrosome Inferred from electronic annotation. Source: Compara condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic dynein complex Inferred from sequence or structural similarity. Source: UniProtKB kinetochore Inferred from sequence or structural similarity. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: Compara spindle pole Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule motor activity Inferred from sequence or structural similarity PubMed 11243854. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 523	523	Cytoplasmic dynein 1 light intermediate chain 1		PRO_0000114667
Regions
	Nucleotide binding	74 – 81	8	ATP Potential
Amino acid modifications
	Modified residue	207	1	Phosphoserine Ref.3 Ref.4 Ref.5 Ref.7
	Modified residue	213	1	Phosphothreonine By similarity
	Modified residue	398	1	Phosphoserine By similarity
	Modified residue	405	1	Phosphoserine Ref.4
	Modified residue	408	1	Phosphothreonine By similarity
	Modified residue	412	1	Phosphoserine By similarity
	Modified residue	414	1	Phosphoserine By similarity
	Modified residue	419	1	Phosphoserine By similarity
	Modified residue	421	1	Phosphoserine By similarity
	Modified residue	450	1	Phosphoserine By similarity
	Modified residue	486	1	Phosphoserine By similarity
	Modified residue	510	1	Phosphoserine Ref.5 Ref.6 Ref.8
	Modified residue	512	1	Phosphothreonine By similarity
	Modified residue	513	1	Phosphothreonine Ref.3 Ref.6
	Modified residue	515	1	Phosphothreonine Ref.5 Ref.6
	Modified residue	516	1	Phosphoserine Ref.3 Ref.6 Ref.8
	Modified residue	518	1	Phosphothreonine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8R1Q8 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: F080D6865A399498	FASTA	523	56,614
	10 20 30 40 50 60 MAAVGRVGSF GSSPPGLAST YASGPLANEL ASGSGGPAAG DDEDGQNLWS CILSEVSTRS 70 80 90 100 110 120 RSKLPTGKNV LLLGEDGAGK TSLIRRIQGI EEYKKGRGLE YLYLNVHDED RDDQTRCNVW 130 140 150 160 170 180 ILDGDLYHKG LLKFSLDALS LRDTLVMLVV DMSKPWTALD SLQKWASVVR EHVDKLKIPP 190 200 210 220 230 240 EEMKEMEQKL IRDFQEYVEP GEDFPASPQR RTTGAQEDRG DSVVLPLGAD TLTHNLGLPV 250 260 270 280 290 300 LVVCTKCDAI SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI 310 320 330 340 350 360 VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKVEDNFE DIITKPPVRK 370 380 390 400 410 420 FVHEKEIMAE DDQVFLMKLQ SLLAKQPPTA AGRPVDASPR VPGGSPRTPN RSVSSNVASV 430 440 450 460 470 480 SPIPAGSKKI DPNMKAGATS EGVLANFFNS LLSKKTGSPG GPGVGGSPGG GAAGASPSLP 490 500 510 520 PSAKKSGQKP VLSDVHAELD RITRKPASVS PTTPTSPTEG EAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney.
[2]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 134-142, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[3]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; THR-513 AND SER-516, MASS SPECTROMETRY. Tissue: Embryonic brain.
[4]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-405, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-510; THR-515 AND THR-518, MASS SPECTROMETRY. Tissue: Brain cortex.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510; THR-513; THR-515 AND SER-516, MASS SPECTROMETRY. Tissue: Liver.
[7]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, MASS SPECTROMETRY. Tissue: Macrophage.
[8]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510 AND SER-516, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC023347 mRNA. Translation: AAH23347.1.
IPI	IPI00153421.
RefSeq	NP_666341.1. NM_146229.2.
UniGene	Mm.128627.
3D structure databases
ProteinModelPortal	Q8R1Q8.
ModBase	Search...
PTM databases
PhosphoSite	Q8R1Q8.
Proteomic databases
PaxDb	Q8R1Q8.
PRIDE	Q8R1Q8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000047404; ENSMUSP00000035366; ENSMUSG00000032435.
GeneID	235661.
KEGG	mmu:235661.
Organism-specific databases
CTD	51143.
MGI	MGI:2135610. Dync1li1.
Phylogenomic databases
eggNOG	NOG265404.
GeneTree	ENSGT00390000008295.
HOGENOM	HOG000236263.
HOVERGEN	HBG005546.
InParanoid	Q8R1Q8.
KO	K10416.
OMA	RISRKPE.
OrthoDB	EOG4W3SN1.
Gene expression databases
ArrayExpress	Q8R1Q8.
Bgee	Q8R1Q8.
CleanEx	MM_DYNC1LI1.
Genevestigator	Q8R1Q8.
GermOnline	ENSMUSG00000032435. Mus musculus.
Family and domain databases
InterPro	IPR008467. Dynein1_light_intermed_chain. IPR022780. Dynein_light_int_chain. [Graphical view]
PANTHER	PTHR12688. PTHR12688. 1 hit.
Pfam	PF05783. DLIC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DYNC1LI1. mouse.
NextBio	382833.
SOURCE	Search...

Entry information

Entry name

DC1L1_MOUSE

Accession

Primary (citable) accession number: Q8R1Q8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program