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Dynein light chain 1, cytoplasmic (Dynein light chain LC8-type 1)

 DYL1_BOVIN              Reviewed;          89 AA.
P61285; Q6B859;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 1.
27-SEP-2017, entry version 120.
RecName: Full=Dynein light chain 1, cytoplasmic;
AltName: Full=Dynein light chain LC8-type 1;
Name=DYNLL1; Synonyms=DNCL1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Hwang K.C., Park S.Y., Cui X.S., Kim N.H.;
"Differentially expressed genes in bovine GV oocyte.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 10-21 AND 37-43, IDENTIFICATION IN THE CYTOPLASMIC
DYNEIN 1 COMPLEX, AND SUBUNIT.
PubMed=8702622; DOI=10.1074/jbc.271.32.19358;
King S.M., Barbarese E., Dillman J.F. III, Patel-King R.S.,
Carson J.H., Pfister K.K.;
"Brain cytoplasmic and flagellar outer arm dyneins share a highly
conserved Mr 8,000 light chain.";
J. Biol. Chem. 271:19358-19366(1996).
[6]
SUBUNIT, AND IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
PubMed=11967380; DOI=10.1110/ps.2520102;
King S.J., Bonilla M., Rodgers M.E., Schroer T.A.;
"Subunit organization in cytoplasmic dynein subcomplexes.";
Protein Sci. 11:1239-1250(2002).
[7]
INTERACTION WITH BOVINE IMMUNODEFICIENCY VIRUS GAG PROTEIN.
PubMed=20148896; DOI=10.1111/j.1462-5822.2010.01453.x;
Su Y., Qiao W., Guo T., Tan J., Li Z., Chen Y., Li X., Li Y., Zhou J.,
Chen Q.;
"Microtubule-dependent retrograde transport of bovine immunodeficiency
virus.";
Cell. Microbiol. 12:1098-1107(2010).
-!- 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
(By similarity). {ECO:0000250}.
-!- 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. 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 (PubMed:8702622, PubMed:11967380). 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 bovine immunodeficiency virus Gag
protein; this interaction is critical for intracellular
microtubule-dependent viral genome transport (PubMed:20148896).
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). {ECO:0000250|UniProtKB:P63167,
ECO:0000250|UniProtKB:P63168, ECO:0000269|PubMed:11967380,
ECO:0000269|PubMed:20148896, ECO:0000269|PubMed:8702622}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-88 appears to control the dimer-
monomer transition. {ECO:0000250}.
-!- SIMILARITY: Belongs to the dynein light chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB099086; BAC56576.1; -; mRNA.
EMBL; AY675078; AAT84371.1; -; mRNA.
EMBL; BT021030; AAX09047.1; -; mRNA.
EMBL; BC102872; AAI02873.1; -; mRNA.
RefSeq; NP_001003901.1; NM_001003901.1.
RefSeq; XP_010796262.1; XM_010797960.2.
RefSeq; XP_010804565.1; XM_010806263.2.
RefSeq; XP_010815015.1; XM_010816713.1.
RefSeq; XP_015323821.1; XM_015468335.1.
UniGene; Bt.2307; -.
UniGene; Bt.51760; -.
ProteinModelPortal; P61285; -.
SMR; P61285; -.
STRING; 9913.ENSBTAP00000056381; -.
PaxDb; P61285; -.
PeptideAtlas; P61285; -.
PRIDE; P61285; -.
Ensembl; ENSBTAT00000034274; ENSBTAP00000034172; ENSBTAG00000024605.
Ensembl; ENSBTAT00000045443; ENSBTAP00000056381; ENSBTAG00000032034.
Ensembl; ENSBTAT00000064169; ENSBTAP00000053982; ENSBTAG00000034170.
GeneID; 404151; -.
GeneID; 783613; -.
GeneID; 784058; -.
KEGG; bta:404151; -.
KEGG; bta:783613; -.
KEGG; bta:784058; -.
CTD; 8655; -.
eggNOG; KOG3430; Eukaryota.
eggNOG; ENOG4111NK2; LUCA.
GeneTree; ENSGT00390000000378; -.
HOVERGEN; HBG002133; -.
InParanoid; P61285; -.
KO; K10418; -.
OMA; QAIMSDR; -.
OrthoDB; EOG091G15JY; -.
TreeFam; TF300264; -.
Reactome; R-BTA-111446; Activation of BIM and translocation to mitochondria.
Reactome; R-BTA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-BTA-1632852; Macroautophagy.
Reactome; R-BTA-2132295; MHC class II antigen presentation.
Reactome; R-BTA-2467813; Separation of Sister Chromatids.
Reactome; R-BTA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-BTA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-BTA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-BTA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-BTA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-BTA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-BTA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-BTA-5620924; Intraflagellar transport.
Reactome; R-BTA-5663220; RHO GTPases Activate Formins.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-6807878; COPI-mediated anterograde transport.
Reactome; R-BTA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-BTA-68877; Mitotic Prometaphase.
Reactome; R-BTA-8854518; AURKA Activation by TPX2.
Proteomes; UP000009136; Chromosome 17.
Proteomes; UP000009136; Chromosome 20.
Proteomes; UP000009136; Chromosome 6.
Bgee; ENSBTAG00000024605; -.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IBA:GO_Central.
GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
GO; GO:0042326; P:negative regulation of phosphorylation; IEA:Ensembl.
GO; GO:2000582; P:positive regulation of ATP-dependent microtubule motor activity, plus-end-directed; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0021762; P:substantia nigra development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0010970; P:transport along microtubule; IBA:GO_Central.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR019763; Dynein_light_1/2_CS.
InterPro; IPR001372; Dynein_light_chain_typ-1/2.
PANTHER; PTHR11886; PTHR11886; 1.
Pfam; PF01221; Dynein_light; 1.
SMART; SM01375; Dynein_light; 1.
PROSITE; PS01239; DYNEIN_LIGHT_1; 1.
1: Evidence at protein level;
Acetylation; Activator; Apoptosis; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Dynein;
Host-virus interaction; Isopeptide bond; Microtubule; Mitochondrion;
Motor protein; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Transport; Ubl conjugation.
CHAIN 1 89 Dynein light chain 1, cytoplasmic.
/FTId=PRO_0000195124.
REGION 67 89 Interaction with ESR1. {ECO:0000250}.
MOD_RES 36 36 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63167}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000250|UniProtKB:P63167}.
CROSSLNK 43 43 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P63167}.
SEQUENCE 89 AA; 10366 MW; F5E7647D092BEB3A CRC64;
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG


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