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Q8R1Q8 (DC1L1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle 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 processCell cycle
Cell division
Mitosis
Transport
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Dynein
Kinetochore
Microtubule
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processmetabolic process

Inferred from sequence or structural similarity PubMed 11243854. Source: GOC

microtubule-based movement

Inferred from sequence or structural similarity PubMed 11243854. Source: MGI

mitotic nuclear division

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_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

spindle pole

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 523523Cytoplasmic dynein 1 light intermediate chain 1
PRO_0000114667

Regions

Nucleotide binding74 – 818ATP Potential

Amino acid modifications

Modified residue2071Phosphoserine Ref.3 Ref.4 Ref.6 Ref.7
Modified residue2131Phosphothreonine By similarity
Modified residue3981Phosphoserine By similarity
Modified residue4051Phosphoserine Ref.4
Modified residue4081Phosphothreonine By similarity
Modified residue4191Phosphoserine By similarity
Modified residue4211Phosphoserine By similarity
Modified residue4861Phosphoserine By similarity
Modified residue5101Phosphoserine Ref.6
Modified residue5121Phosphothreonine By similarity
Modified residue5131Phosphothreonine Ref.6
Modified residue5151Phosphothreonine Ref.6
Modified residue5161Phosphoserine Ref.6 Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q8R1Q8 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: F080D6865A399498

FASTA52356,614
        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 

« Hide

References

« Hide '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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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-207; SER-510; THR-513; THR-515 AND SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC023347 mRNA. Translation: AAH23347.1.
CCDSCCDS23595.1.
RefSeqNP_666341.1. NM_146229.2.
UniGeneMm.128627.

3D structure databases

ProteinModelPortalQ8R1Q8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231702. 2 interactions.
IntActQ8R1Q8. 1 interaction.
MINTMINT-4118631.

PTM databases

PhosphoSiteQ8R1Q8.

Proteomic databases

MaxQBQ8R1Q8.
PaxDbQ8R1Q8.
PRIDEQ8R1Q8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047404; ENSMUSP00000035366; ENSMUSG00000032435.
GeneID235661.
KEGGmmu:235661.
UCSCuc009rxy.1. mouse.

Organism-specific databases

CTD51143.
MGIMGI:2135610. Dync1li1.

Phylogenomic databases

eggNOGNOG265404.
GeneTreeENSGT00390000008295.
HOGENOMHOG000236263.
HOVERGENHBG005546.
InParanoidQ8R1Q8.
KOK10416.
OMAPNRSVTS.
OrthoDBEOG7V7668.
PhylomeDBQ8R1Q8.
TreeFamTF352602.

Gene expression databases

BgeeQ8R1Q8.
CleanExMM_DYNC1LI1.
GenevestigatorQ8R1Q8.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR008467. Dynein1_light_intermed_chain.
IPR022780. Dynein_light_int_chain.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR12688. PTHR12688. 1 hit.
PfamPF05783. DLIC. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

ChiTaRSDYNC1LI1. mouse.
NextBio382833.
PROQ8R1Q8.
SOURCESearch...

Entry information

Entry nameDC1L1_MOUSE
AccessionPrimary (citable) accession number: Q8R1Q8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot