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Q6PDL0 (DC1L2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. 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
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 2
Alternative name(s):
Dynein light intermediate chain 2, cytosolic
Gene names
Name:Dync1li2
Synonyms:Dncli2, Dnclic2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length492 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 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 By similarity.

Subcellular location

Cytoplasm › cytoskeleton By similarity.

Sequence similarities

Belongs to the dynein light intermediate chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Cytoplasmic dynein 1 light intermediate chain 2
PRO_0000114672

Regions

Nucleotide binding61 – 688ATP Potential

Amino acid modifications

Modified residue1941Phosphoserine Ref.3
Modified residue3831Phosphoserine By similarity
Modified residue3911Phosphoserine By similarity
Modified residue4411Phosphothreonine By similarity
Modified residue4431Phosphoserine By similarity
Modified residue4461Phosphoserine By similarity

Experimental info

Sequence conflict3531E → K in AAH58645. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6PDL0 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 6418DF74FFD7175E

FASTA49254,218
        10         20         30         40         50         60 
MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRARSK LPSGKNILVF 

        70         80         90        100        110        120 
GEDGSGKTTL MTKLQGAEHG KKGRGLEYLY LSVHDEDRDD HTRCNVWILD GDLYHKGLLK 

       130        140        150        160        170        180 
FAVSAESLRE TLVIFVADMS RPWTIMESLQ KWASVLREHI DKMKIPPEEM RDLERKFMKE 

       190        200        210        220        230        240 
FQDYIEPEEG CQGSPQRRGP LTSGSDEDSV ALPLGDNVLT HNLGIPVLVV CTKCDAMSVL 

       250        260        270        280        290        300 
EKEHDYRDEH LDFIQAHLRR FCLQYGAALI YTSVKEEKNL DLLYKYIVHK TYGFHFTIPA 

       310        320        330        340        350        360 
LVVEKDAVFI PAGWDNEKKI AILHENFTTV KPEDAYEDFI VKPPVRKLVH DKELAAEDEQ 

       370        380        390        400        410        420 
VFLMKQQSLL AKQPATPTRT SESPARGPSG SPRTQGRGGP ASVPSASPGT SVKKPDPNIK 

       430        440        450        460        470        480 
NNAASEGVLA SFFNSLLSKK TGSPGSPSAG GVQSTAKKSG QKTVLSNVQE ELDRMTRKPD 

       490 
SMVTNSSTEN EA

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow, Head and Testis.
[2]"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: C57BL/6.
Tissue: Brain.
[3]"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-194, MASS SPECTROMETRY.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK140743 mRNA. Translation: BAE24463.1.
AK147899 mRNA. Translation: BAE28215.1.
AK152157 mRNA. Translation: BAE30992.1.
AK161434 mRNA. Translation: BAE36394.1.
BC058645 mRNA. Translation: AAH58645.1.
IPIIPI00420806.
RefSeqNP_001013398.2. NM_001013380.2.
UniGeneMm.289583.

3D structure databases

ProteinModelPortalQ6PDL0.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000045480.

PTM databases

PhosphoSiteQ6PDL0.

Proteomic databases

PaxDbQ6PDL0.
PRIDEQ6PDL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041769; ENSMUSP00000045480; ENSMUSG00000035770.
GeneID234663.
KEGGmmu:234663.

Organism-specific databases

CTD1783.
MGIMGI:107738. Dync1li2.

Phylogenomic databases

eggNOGNOG265404.
GeneTreeENSGT00390000008295.
HOGENOMHOG000236263.
HOVERGENHBG005546.
InParanoidQ3UGJ3.
KOK10416.
OMALNIHDED.
OrthoDBEOG4PNXGQ.

Gene expression databases

BgeeQ6PDL0.
CleanExMM_DYNC1LI2.
GenevestigatorQ6PDL0.
GermOnlineENSMUSG00000035770. Mus musculus.

Family and domain databases

InterProIPR008467. Dynein1_light_intermed_chain.
IPR022780. Dynein_light_int_chain.
[Graphical view]
PANTHERPTHR12688. PTHR12688. 1 hit.
PfamPF05783. DLIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDYNC1LI2. mouse.
NextBio382249.
SOURCESearch...

Entry information

Entry nameDC1L2_MOUSE
AccessionPrimary (citable) accession number: Q6PDL0
Secondary accession number(s): Q3UGJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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