UniProt functional annotation for P63170



	UniProt functional annotation for P63170

UniProt codes: P63170, Q15701.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

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 changing or maintaining the spatial distribution of cytoskeletal structures.

Function: Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.

Function: Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1. {ECO:0000250}.

Function: 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). {ECO:0000250}.

Subunit: Homodimer. Monomer; the monomeric form is incapable of binding to target proteins (By similarity). 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 (PubMed:8702622, PubMed:11746667). 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 (By similarity). Interacts with BCL2L11 (PubMed:21478148). 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 MYZAP. Part of an astrin (SPAG5)- kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. 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'). Interacts with BICD2 (By similarity). Interacts with BCAS1 (PubMed:16133941). Interacts with Bassoon/BSN (By similarity). Interacts with HDAC6 (By similarity). Interacts with TPPP (By similarity). {ECO:0000250|UniProtKB:P63167, ECO:0000250|UniProtKB:P63168, ECO:0000269|PubMed:11746667, ECO:0000269|PubMed:16133941, ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:8702622}.

Subunit: (Microbial infection) Interacts with rabies virus phosphoprotein. {ECO:0000269|PubMed:11602781}.

Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8702622}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Associated with microtubules.

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

Ptm: Phosphorylation at Ser-88 appears to control the dimer-monomer transition. {ECO:0000250}.

Similarity: Belongs to the dynein light chain family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



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 changing or maintaining the spatial distribution of cytoskeletal structures.



Function:		Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.



Function:		Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1. {ECO:0000250}.



Function:		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). {ECO:0000250}.


Subunit:		Homodimer. Monomer; the monomeric form is incapable of binding to target proteins (By similarity). 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 (PubMed:8702622, PubMed:11746667). 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 (By similarity). Interacts with BCL2L11 (PubMed:21478148). 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 MYZAP. Part of an astrin (SPAG5)- kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. 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'). Interacts with BICD2 (By similarity). Interacts with BCAS1 (PubMed:16133941). Interacts with Bassoon/BSN (By similarity). Interacts with HDAC6 (By similarity). Interacts with TPPP (By similarity). {ECO:0000250\|UniProtKB:P63167, ECO:0000250\|UniProtKB:P63168, ECO:0000269\|PubMed:11746667, ECO:0000269\|PubMed:16133941, ECO:0000269\|PubMed:21478148, ECO:0000269\|PubMed:8702622}.
Subunit:		(Microbial infection) Interacts with rabies virus phosphoprotein. {ECO:0000269\|PubMed:11602781}.
Subcellular location:		Cytoplasm, cytoskeleton {ECO:0000269\|PubMed:8702622}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Associated with microtubules.
Tissue specificity:		Weaker expression in the cerebellum and spinal cord compared with other brain regions.
Ptm:		Phosphorylation at Ser-88 appears to control the dimer-monomer transition. {ECO:0000250}.
Similarity:		Belongs to the dynein light chain family. {ECO:0000305}.