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Protein

Dynein light chain 1, cytoplasmic

Gene

Dynll1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 changing or maintaining the spatial distribution of cytoskeletal structures.
Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.
Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.By similarity
Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (By similarity).By similarity

GO - Molecular functioni

  • enzyme binding Source: RGD
  • enzyme inhibitor activity Source: ProtInc
  • motor activity Source: UniProtKB-KW
  • nitric-oxide synthase regulator activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • microtubule-based process Source: InterPro
  • negative regulation of catalytic activity Source: GOC
  • neurotransmitter metabolic process Source: ProtInc
  • nitric oxide biosynthetic process Source: ProtInc
  • regulation of catalytic activity Source: GOC
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Motor protein

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Dynein light chain 1, cytoplasmic
Alternative name(s):
8 kDa dynein light chain
Short name:
DLC8
Dynein light chain LC8-type 1
Protein inhibitor of neuronal nitric oxide synthase
Short name:
PIN
Gene namesi
Name:Dynll1
Synonyms:Dncl1, Dnclc1, Pin
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi619866. Dynll1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic dynein complex Source: UniProtKB
  • kinetochore Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • mitochondrion Source: UniProtKB-SubCell
  • mitotic spindle Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8989Dynein light chain 1, cytoplasmicPRO_0000195129Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6-acetyllysineBy similarity
Modified residuei88 – 881PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Ser-88 appears to control the dimer-monomer transition.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP63170.
PRIDEiP63170.

PTM databases

iPTMnetiP63170.
PhosphoSiteiP63170.

Expressioni

Tissue specificityi

Weaker expression in the cerebellum and spinal cord compared with other brain regions.

Gene expression databases

GenevisibleiP63170. RN.

Interactioni

Subunit structurei

Homodimer. Monomer; the monomeric form is incapable of binding to target proteins. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits which present 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. Interacts with TXNDC17. Interacts with WWC1 and ESR1. The interaction with WWC1 is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin. Interacts with BCL2L11. Interacts with BCL2; the interaction is greatly enhanced in the nucleus and in mitochondria upon induction of apoptosis. Interacts with PAK1; the interaction requires dimeric DYNLL1 (By similarity). Interacts with rabies virus phosphoprotein. Interacts with MYZAP (By similarity). Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGOL2 (By similarity). Interacts with ATMIN; this interaction inhibits ATMIN transcriptional activity and hence may play a role in a feedback loop whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN. Interacts with NEK9 (not phosphorylated at 'Ser-944') (By similarity).By similarity

GO - Molecular functioni

  • enzyme binding Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi248680. 3 interactions.
IntActiP63170. 36 interactions.
MINTiMINT-241889.
STRINGi10116.ENSRNOP00000061342.

Structurei

Secondary structure

1
89
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Helixi15 – 3117Combined sources
Helixi35 – 4915Combined sources
Beta strandi54 – 618Combined sources
Beta strandi63 – 653Combined sources
Beta strandi73 – 764Combined sources
Beta strandi82 – 876Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F3CNMR-A/B1-89[»]
1F95NMR-A/B1-89[»]
1F96NMR-A/B1-89[»]
ProteinModelPortaliP63170.
SMRiP63170. Positions 5-89.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63170.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 8923Interaction with ESR1By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the dynein light chain family.Curated

Phylogenomic databases

eggNOGiKOG3430. Eukaryota.
ENOG4111NK2. LUCA.
GeneTreeiENSGT00390000000378.
HOVERGENiHBG002133.
InParanoidiP63170.
KOiK10418.
OMAiYGPTWHV.
OrthoDBiEOG7BZVVQ.
PhylomeDBiP63170.
TreeFamiTF300264.

Family and domain databases

Gene3Di3.30.740.10. 1 hit.
InterProiIPR019763. Dynein_light_1/2_CS.
IPR001372. Dynein_light_chain_typ-1/2.
[Graphical view]
PfamiPF01221. Dynein_light. 1 hit.
[Graphical view]
SMARTiSM01375. Dynein_light. 1 hit.
[Graphical view]
PROSITEiPS01239. DYNEIN_LIGHT_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63170-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY
60 70 80
NPTWHCIVGR NFGSYVTHET KHFIYFYLGQ VAILLFKSG
Length:89
Mass (Da):10,366
Last modified:September 27, 2004 - v1
Checksum:iF5E7647D092BEB3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66461 mRNA. Translation: AAB38257.1.
BC063183 mRNA. Translation: AAH63183.1.
PIRiJC5633.
RefSeqiNP_445771.1. NM_053319.3.
UniGeneiRn.35769.

Genome annotation databases

EnsembliENSRNOT00000014910; ENSRNOP00000061342; ENSRNOG00000011222.
GeneIDi58945.
KEGGirno:58945.
UCSCiRGD:619866. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66461 mRNA. Translation: AAB38257.1.
BC063183 mRNA. Translation: AAH63183.1.
PIRiJC5633.
RefSeqiNP_445771.1. NM_053319.3.
UniGeneiRn.35769.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F3CNMR-A/B1-89[»]
1F95NMR-A/B1-89[»]
1F96NMR-A/B1-89[»]
ProteinModelPortaliP63170.
SMRiP63170. Positions 5-89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248680. 3 interactions.
IntActiP63170. 36 interactions.
MINTiMINT-241889.
STRINGi10116.ENSRNOP00000061342.

PTM databases

iPTMnetiP63170.
PhosphoSiteiP63170.

Proteomic databases

PaxDbiP63170.
PRIDEiP63170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014910; ENSRNOP00000061342; ENSRNOG00000011222.
GeneIDi58945.
KEGGirno:58945.
UCSCiRGD:619866. rat.

Organism-specific databases

CTDi8655.
RGDi619866. Dynll1.

Phylogenomic databases

eggNOGiKOG3430. Eukaryota.
ENOG4111NK2. LUCA.
GeneTreeiENSGT00390000000378.
HOVERGENiHBG002133.
InParanoidiP63170.
KOiK10418.
OMAiYGPTWHV.
OrthoDBiEOG7BZVVQ.
PhylomeDBiP63170.
TreeFamiTF300264.

Miscellaneous databases

EvolutionaryTraceiP63170.
NextBioi611548.
PROiP63170.

Gene expression databases

GenevisibleiP63170. RN.

Family and domain databases

Gene3Di3.30.740.10. 1 hit.
InterProiIPR019763. Dynein_light_1/2_CS.
IPR001372. Dynein_light_chain_typ-1/2.
[Graphical view]
PfamiPF01221. Dynein_light. 1 hit.
[Graphical view]
SMARTiSM01375. Dynein_light. 1 hit.
[Graphical view]
PROSITEiPS01239. DYNEIN_LIGHT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PIN: an associated protein inhibitor of neuronal nitric oxide synthase."
    Jaffrey S.R., Snyder S.H.
    Science 274:774-777(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Distribution of protein inhibitor of neuronal nitric oxide synthase in rat brain."
    Greenwood M.T., Guo Y., Kumar U., Beausejours S., Hussain S.N.A.
    Biochem. Biophys. Res. Commun. 238:617-621(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: Pituitary.
  4. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 50-60, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  5. "Brain cytoplasmic and flagellar outer arm dyneins share a highly conserved Mr 8,000 light chain."
    King S.M., Barbarese E., Dillman J.F. III, Patel-King R.S., Carson J.H., Pfister K.K.
    J. Biol. Chem. 271:19358-19366(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX, SUBCELLULAR LOCATION.
  6. "Light chains of mammalian cytoplasmic dynein: identification and characterization of a family of LC8 light chains."
    Wilson M.J., Salata M.W., Susalka S.J., Pfister K.K.
    Cell Motil. Cytoskeleton 49:229-240(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
  7. "Molecular basis for the interaction between rabies virus phosphoprotein P and the dynein light chain LC8: dissociation of dynein-binding properties and transcriptional functionality of P."
    Poisson N., Real E., Gaudin Y., Vaney M.C., King S., Jacob Y., Tordo N., Blondel D.
    J. Gen. Virol. 82:2691-2696(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABIES VIRUS PHOSPHOPROTEIN.
  8. "Identification of a novel Bcl-2-interacting mediator of cell death (Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in rapid ischemic tolerance-induced neuroprotection."
    Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P., Henshall D.C., Morris K.T., Simon R.P., Meller R.
    J. Biol. Chem. 286:19331-19339(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL2L11.
  9. "Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain."
    Fan J.-S., Zhang Q., Tochio H., Li M., Zhang M.
    J. Mol. Biol. 306:97-108(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiDYL1_RAT
AccessioniPrimary (citable) accession number: P63170
Secondary accession number(s): Q15701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: May 11, 2016
This is version 117 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.