DYL1_BOVIN
ID DYL1_BOVIN Reviewed; 89 AA.
AC P61285; Q6B859;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Dynein light chain 1, cytoplasmic;
DE AltName: Full=Dynein light chain LC8-type 1;
GN Name=DYNLL1; Synonyms=DNCL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12658628; DOI=10.1002/mrd.10292;
RA Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T.,
RA Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G.,
RA Izaike Y., Todoroki J., Hashizume K.;
RT "Characterization of gene expression profiles in early bovine pregnancy
RT using a custom cDNA microarray.";
RL Mol. Reprod. Dev. 65:9-18(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hwang K.C., Park S.Y., Cui X.S., Kim N.H.;
RT "Differentially expressed genes in bovine GV oocyte.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 10-21 AND 37-43, IDENTIFICATION IN THE CYTOPLASMIC
RP DYNEIN 1 COMPLEX, AND SUBUNIT.
RX PubMed=8702622; DOI=10.1074/jbc.271.32.19358;
RA King S.M., Barbarese E., Dillman J.F. III, Patel-King R.S., Carson J.H.,
RA Pfister K.K.;
RT "Brain cytoplasmic and flagellar outer arm dyneins share a highly conserved
RT Mr 8,000 light chain.";
RL J. Biol. Chem. 271:19358-19366(1996).
RN [6]
RP SUBUNIT, AND IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
RX PubMed=11967380; DOI=10.1110/ps.2520102;
RA King S.J., Bonilla M., Rodgers M.E., Schroer T.A.;
RT "Subunit organization in cytoplasmic dynein subcomplexes.";
RL Protein Sci. 11:1239-1250(2002).
RN [7]
RP INTERACTION WITH BOVINE IMMUNODEFICIENCY VIRUS GAG PROTEIN (MICROBIAL
RP INFECTION).
RX PubMed=20148896; DOI=10.1111/j.1462-5822.2010.01453.x;
RA Su Y., Qiao W., Guo T., Tan J., Li Z., Chen Y., Li X., Li Y., Zhou J.,
RA Chen Q.;
RT "Microtubule-dependent retrograde transport of bovine immunodeficiency
RT virus.";
RL Cell. Microbiol. 12:1098-1107(2010).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 1 complex that are thought to be involved in
CC linking dynein to cargos and to adapter proteins that regulate dynein
CC function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules. May
CC play a role in changing or maintaining the spatial distribution of
CC cytoskeletal structures (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Promotes transactivation functions of ESR1 and plays a role
CC in the nuclear localization of ESR1. {ECO:0000250|UniProtKB:P63167}.
CC -!- FUNCTION: Regulates apoptotic activities of BCL2L11 by sequestering it
CC to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex
CC dissociates from cytoplasmic dynein and translocates to mitochondria
CC and sequesters BCL2 thus neutralizing its antiapoptotic activity (By
CC similarity). {ECO:0000250|UniProtKB:P63167}.
CC -!- SUBUNIT: Homodimer. Monomer; the monomeric form is incapable of binding
CC to target proteins. The cytoplasmic dynein 1 complex consists of two
CC catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC presented by intermediate chains (ICs), light intermediate chains
CC (LICs) and light chains (LCs); the composition seems to vary in respect
CC to the IC, LIC and LC composition. The heavy chain homodimer serves as
CC a scaffold for the probable homodimeric assembly of the respective non-
CC catalytic subunits. The ICs and LICs bind directly to the HC dimer and
CC the LCs assemble on the IC dimer (PubMed:8702622, PubMed:11967380).
CC Interacts with TXNDC17. Interacts with WWC1 and ESR1. The interaction
CC with WWC1 is mandatory for the recruitment and transactivation
CC functions of ESR1 or DYNLL1 to the target chromatin. Interacts with
CC BCL2L11. Interacts with BCL2; the interaction is greatly enhanced in
CC the nucleus and in mitochondria upon induction of apoptosis. Interacts
CC with PAK1; the interaction requires dimeric DYNLL1 (By similarity).
CC Interacts with MYZAP. Part of an astrin (SPAG5)-kinastrin (SKAP)
CC complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. Interacts with
CC ATMIN; this interaction inhibits ATMIN transcriptional activity and
CC hence may play a role in a feedback loop whereby DYNLL1 inhibits
CC transactivation of its own promoter by ATMIN. Interacts with NEK9 (not
CC phosphorylated at 'Ser-944'). Interacts with BICD2 (By similarity).
CC Interacts with BCAS1 (By similarity). Interacts with Bassoon/BSN (By
CC similarity). Interacts with HDAC6 (By similarity). Interacts with TPPP
CC (By similarity). Interacts with AMBRA1 (via TQT motifs); tethering
CC AMBRA1 to the cytoskeleton (By similarity). Interacts with FAM83D/CHICA
CC (via C-terminus) (By similarity). Interacts with HMMR, SPAG5/Astrin and
CC KNSTRN/Kinastrin (By similarity). {ECO:0000250|UniProtKB:P63167,
CC ECO:0000250|UniProtKB:P63168, ECO:0000250|UniProtKB:P63170,
CC ECO:0000269|PubMed:11967380, ECO:0000269|PubMed:8702622}.
CC -!- SUBUNIT: (Microbial infection) Interacts with bovine immunodeficiency
CC virus Gag protein; this interaction is critical for intracellular
CC microtubule-dependent viral genome transport.
CC {ECO:0000269|PubMed:20148896}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:P63167}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:P63167}. Nucleus
CC {ECO:0000250|UniProtKB:P63167}. Mitochondrion
CC {ECO:0000250|UniProtKB:P63167}. Note=Upon induction of apoptosis
CC translocates together with BCL2L11 to mitochondria.
CC {ECO:0000250|UniProtKB:P63167}.
CC -!- PTM: Phosphorylation at Ser-88 appears to control the dimer-monomer
CC transition. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
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DR EMBL; AB099086; BAC56576.1; -; mRNA.
DR EMBL; AY675078; AAT84371.1; -; mRNA.
DR EMBL; BT021030; AAX09047.1; -; mRNA.
DR EMBL; BC102872; AAI02873.1; -; mRNA.
DR RefSeq; NP_001003901.1; NM_001003901.1.
DR RefSeq; XP_010796262.1; XM_010797960.2.
DR RefSeq; XP_010799037.1; XM_010800735.1.
DR RefSeq; XP_010804565.1; XM_010806263.2.
DR RefSeq; XP_010815015.1; XM_010816713.1.
DR RefSeq; XP_015323821.1; XM_015468335.1.
DR AlphaFoldDB; P61285; -.
DR BMRB; P61285; -.
DR SMR; P61285; -.
DR STRING; 9913.ENSBTAP00000034172; -.
DR PaxDb; P61285; -.
DR PeptideAtlas; P61285; -.
DR PRIDE; P61285; -.
DR Ensembl; ENSBTAT00000034274; ENSBTAP00000034172; ENSBTAG00000024605.
DR Ensembl; ENSBTAT00000045443; ENSBTAP00000056381; ENSBTAG00000032034.
DR Ensembl; ENSBTAT00000078917; ENSBTAP00000058355; ENSBTAG00000024605.
DR Ensembl; ENSBTAT00000081563; ENSBTAP00000074218; ENSBTAG00000024605.
DR GeneID; 101902172; -.
DR GeneID; 404151; -.
DR GeneID; 784058; -.
DR KEGG; bta:101902172; -.
DR KEGG; bta:404151; -.
DR KEGG; bta:784058; -.
DR CTD; 8655; -.
DR VEuPathDB; HostDB:ENSBTAG00000024605; -.
DR VEuPathDB; HostDB:ENSBTAG00000032034; -.
DR eggNOG; KOG3430; Eukaryota.
DR GeneTree; ENSGT00390000000378; -.
DR HOGENOM; CLU_070944_4_0_1; -.
DR InParanoid; P61285; -.
DR OMA; EKMQIHA; -.
DR OrthoDB; 1520814at2759; -.
DR TreeFam; TF300264; -.
DR Reactome; R-BTA-111446; Activation of BIM and translocation to mitochondria.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 17.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000024605; Expressed in oocyte and 104 other tissues.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035721; P:intraciliary retrograde transport; IBA:GO_Central.
DR GO; GO:0044458; P:motile cilium assembly; IBA:GO_Central.
DR Gene3D; 3.30.740.10; -; 1.
DR InterPro; IPR037177; DLC_sf.
DR InterPro; IPR019763; Dynein_light_1/2_CS.
DR InterPro; IPR001372; Dynein_light_chain_typ-1/2.
DR PANTHER; PTHR11886; PTHR11886; 1.
DR Pfam; PF01221; Dynein_light; 1.
DR SMART; SM01375; Dynein_light; 1.
DR SUPFAM; SSF54648; SSF54648; 1.
DR PROSITE; PS01239; DYNEIN_LIGHT_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Apoptosis; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Dynein; Host-virus interaction; Isopeptide bond;
KW Microtubule; Mitochondrion; Motor protein; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Transport;
KW Ubl conjugation.
FT CHAIN 1..89
FT /note="Dynein light chain 1, cytoplasmic"
FT /id="PRO_0000195124"
FT REGION 67..89
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63167"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63167"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63167"
SQ SEQUENCE 89 AA; 10366 MW; F5E7647D092BEB3A CRC64;
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG
