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Protein

Cytoplasmic dynein 2 light intermediate chain 1

Gene

Dync2li1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May function as a motor for intraflagellar retrograde transport. Functions in cilia biogenesis (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • cilium assembly Source: MGI
  • determination of left/right symmetry Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Motor protein

Keywords - Biological processi

Cilium biogenesis/degradation

Enzyme and pathway databases

ReactomeiR-MMU-2132295. MHC class II antigen presentation.
R-MMU-5620924. Intraflagellar transport.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic dynein 2 light intermediate chain 1
Short name:
mD2LIC
Gene namesi
Name:Dync2li1
Synonyms:D2lic
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1913996. Dync2li1.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: BHF-UCL
  • axoneme Source: BHF-UCL
  • cytoplasm Source: UniProtKB-SubCell
  • dynein complex Source: UniProtKB-KW
  • microtubule Source: UniProtKB-KW
  • motile primary cilium Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Dynein, Microtubule

Pathology & Biotechi

Disruption phenotypei

Death before 11.5 dpc with defects in notochord and floor plate formation and a reduction of definitive endoderm. Mice also display anterior truncations of the forebrain, defects in the ventral body wall, in closure of the neural tube, and either an arrest of embryonic turning and heart looping or a randomization in their direction.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Cytoplasmic dynein 2 light intermediate chain 1PRO_0000318751Add
BLAST

Proteomic databases

MaxQBiQ8K0T2.
PaxDbiQ8K0T2.
PRIDEiQ8K0T2.

PTM databases

iPTMnetiQ8K0T2.
PhosphoSiteiQ8K0T2.

Expressioni

Tissue specificityi

Specifically expressed by ciliated cells in brain, lung, spleen, testis and kidney (at protein level). Enriched in the ependymal layer lining the lateral ventricles (at protein level).4 Publications

Developmental stagei

Specifically expressed by monociliated cells of the ventral node from the late streak to early somite stage.1 Publication

Gene expression databases

BgeeiQ8K0T2.
CleanExiMM_DYNC2LI1.
GenevisibleiQ8K0T2. MM.

Interactioni

Subunit structurei

The cytoplasmic dynein complex 2 is probably composed by a DYNC2H1 homodimer and a number of DYNC2LI1 light intermediate chains.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025101.

Structurei

3D structure databases

ProteinModelPortaliQ8K0T2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3929. Eukaryota.
ENOG410XTE5. LUCA.
GeneTreeiENSGT00390000010498.
HOGENOMiHOG000006828.
HOVERGENiHBG066237.
InParanoidiQ8K0T2.
KOiK10417.
OMAiLELWKKV.
OrthoDBiEOG70CR6X.
PhylomeDBiQ8K0T2.
TreeFamiTF314138.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR022780. Dynein_light_int_chain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF05783. DLIC. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Q8K0T2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSETLWEIA KAEVEKRRSH GSEGDGAEIG EKSVFFIGSK NGGKTTIILR
60 70 80 90 100
CLDRDESAKP TLALEYTYGR KTKGHNTPKD IAHFWELGGG TSLLDLISIP
110 120 130 140 150
ITVDTLRTFS IVLVLDLSKP NDLWSTMENL LQATKSHVDK VIMKLGKTSS
160 170 180 190 200
KASAEMRQRM WSVVQKDHPD RELIDPFPIP LVIIGSKYDI FQDFDPEKRK
210 220 230 240 250
VICKTLRFVA HYYGASLMFT SKSEALLLKI RGVINQLAFG IDKSKSICVD
260 270 280 290 300
QNKPLFITAG LDSLCQIGSP PVPDSDIGKL QAHSPMELWK KVYDKLFPPK
310 320 330 340 350
STGTLKAVQD PARDPQYAES EVDEMRVQKD QELEHYKRSS SKTWKQIELD

S
Length:351
Mass (Da):39,469
Last modified:October 1, 2002 - v1
Checksum:i140D6C96B7188C2F
GO

Sequence cautioni

The sequence BAE35717.1 differs from that shown. Reason: Frameshift at position 326. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151E → Q in BAE35717 (PubMed:16141072).Curated
Sequence conflicti34 – 341V → L in BAE35717 (PubMed:16141072).Curated
Sequence conflicti123 – 1231L → H in BAE35717 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK160259 mRNA. Translation: BAE35717.1. Frameshift.
BC030450 mRNA. Translation: AAH30450.1.
BC039070 mRNA. Translation: AAH39070.1.
CCDSiCCDS29000.1.
RefSeqiNP_758460.1. NM_172256.1.
UniGeneiMm.246119.

Genome annotation databases

EnsembliENSMUST00000025101; ENSMUSP00000025101; ENSMUSG00000024253.
GeneIDi213575.
KEGGimmu:213575.
UCSCiuc008dsy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK160259 mRNA. Translation: BAE35717.1. Frameshift.
BC030450 mRNA. Translation: AAH30450.1.
BC039070 mRNA. Translation: AAH39070.1.
CCDSiCCDS29000.1.
RefSeqiNP_758460.1. NM_172256.1.
UniGeneiMm.246119.

3D structure databases

ProteinModelPortaliQ8K0T2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025101.

PTM databases

iPTMnetiQ8K0T2.
PhosphoSiteiQ8K0T2.

Proteomic databases

MaxQBiQ8K0T2.
PaxDbiQ8K0T2.
PRIDEiQ8K0T2.

Protocols and materials databases

DNASUi213575.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025101; ENSMUSP00000025101; ENSMUSG00000024253.
GeneIDi213575.
KEGGimmu:213575.
UCSCiuc008dsy.1. mouse.

Organism-specific databases

CTDi51626.
MGIiMGI:1913996. Dync2li1.

Phylogenomic databases

eggNOGiKOG3929. Eukaryota.
ENOG410XTE5. LUCA.
GeneTreeiENSGT00390000010498.
HOGENOMiHOG000006828.
HOVERGENiHBG066237.
InParanoidiQ8K0T2.
KOiK10417.
OMAiLELWKKV.
OrthoDBiEOG70CR6X.
PhylomeDBiQ8K0T2.
TreeFamiTF314138.

Enzyme and pathway databases

ReactomeiR-MMU-2132295. MHC class II antigen presentation.
R-MMU-5620924. Intraflagellar transport.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.

Miscellaneous databases

PROiQ8K0T2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K0T2.
CleanExiMM_DYNC2LI1.
GenevisibleiQ8K0T2. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR022780. Dynein_light_int_chain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF05783. DLIC. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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: 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].
    Tissue: Eye and Mammary tumor.
  3. "Molecular structure of cytoplasmic dynein 2 and its distribution in neuronal and ciliated cells."
    Mikami A., Tynan S.H., Hama T., Luby-Phelps K., Saito T., Crandall J.E., Besharse J.C., Vallee R.B.
    J. Cell Sci. 115:4801-4808(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "Identification of a novel light intermediate chain (D2LIC) for mammalian cytoplasmic dynein 2."
    Grissom P.M., Vaisberg E.A., McIntosh J.R.
    Mol. Biol. Cell 13:817-829(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "A novel dynein light intermediate chain colocalizes with the retrograde motor for intraflagellar transport at sites of axoneme assembly in chlamydomonas and mammalian cells."
    Perrone C.A., Tritschler D., Taulman P., Bower R., Yoder B.K., Porter M.E.
    Mol. Biol. Cell 14:2041-2056(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Targeted deletion of the novel cytoplasmic dynein mD2LIC disrupts the embryonic organiser, formation of the body axes and specification of ventral cell fates."
    Rana A.A., Barbera J.P.M., Rodriguez T.A., Lynch D., Hirst E., Smith J.C., Beddington R.S.P.
    Development 131:4999-5007(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiDC2L1_MOUSE
AccessioniPrimary (citable) accession number: Q8K0T2
Secondary accession number(s): Q3TVA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.