DYL1_RABIT
ID DYL1_RABIT Reviewed; 89 AA.
AC P63169; Q15701;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dynein light chain 1, cytoplasmic;
DE AltName: Full=8 kDa dynein light chain;
DE Short=DLC8;
DE AltName: Full=Dynein light chain LC8-type 1;
DE AltName: Full=Protein inhibitor of neuronal nitric oxide synthase;
DE Short=PIN;
GN Name=DYNLL1; Synonyms=DLC1, DNCL1, DNCLC1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Brain;
RX PubMed=9651483; DOI=10.1016/s0378-1119(98)00231-5;
RA Jeong Y., Won J., Yim J.;
RT "Cloning and structure of a rabbit protein inhibitor of neuronal nitric
RT oxide synthase (PIN) gene and its pseudogene.";
RL Gene 214:67-75(1998).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=9808041; DOI=10.1038/2940;
RA Tochio H., Ohki S., Zhang Q., Li M., Zhang M.;
RT "Solution structure of a protein inhibitor of neuronal nitric oxide
RT synthase.";
RL Nat. Struct. Biol. 5:965-969(1998).
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: Binds and inhibits the catalytic activity of neuronal nitric
CC oxide synthase. {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. Interacts with TXNDC17. Interacts
CC with WWC1 and ESR1. The interaction with WWC1 is mandatory for the
CC recruitment and transactivation functions of ESR1 or DYNLL1 to the
CC target chromatin. Interacts with BCL2L11 isoform 1 and isoform 2.
CC Interacts with BCL2; the interaction is greatly enhanced in the nucleus
CC and in mitochondria upon induction of apoptosis. Interacts with PAK1;
CC the interaction requires dimeric DYNLL1. Interacts with MYZAP. Part of
CC an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5,
CC PLK1, DYNLL1 and SGO2. Interacts with ATMIN; this interaction inhibits
CC ATMIN transcriptional activity and hence may play a role in a feedback
CC loop whereby DYNLL1 inhibits transactivation of its own promoter by
CC ATMIN. Interacts with NEK9 (not phosphorylated at 'Ser-944'). Interacts
CC with BICD2. Interacts with BCAS1. 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 -!- 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; AF008304; AAC32530.1; -; mRNA.
DR EMBL; AF020710; AAC32531.1; -; Genomic_DNA.
DR RefSeq; NP_001075487.1; NM_001082018.2.
DR RefSeq; XP_017204986.1; XM_017349497.1.
DR AlphaFoldDB; P63169; -.
DR BMRB; P63169; -.
DR SMR; P63169; -.
DR STRING; 9986.ENSOCUP00000024256; -.
DR PRIDE; P63169; -.
DR Ensembl; ENSOCUT00000017805; ENSOCUP00000024256; ENSOCUG00000017806.
DR GeneID; 100008650; -.
DR KEGG; ocu:100008650; -.
DR CTD; 8655; -.
DR eggNOG; KOG3430; Eukaryota.
DR GeneTree; ENSGT00390000000378; -.
DR HOGENOM; CLU_070944_4_0_1; -.
DR InParanoid; P63169; -.
DR OMA; KHSPTWH; -.
DR OrthoDB; 1520814at2759; -.
DR TreeFam; TF300264; -.
DR Proteomes; UP000001811; Chromosome 21.
DR Bgee; ENSOCUG00000017806; Expressed in testis and 16 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IEA:Ensembl.
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; Dynein;
KW Isopeptide bond; Microtubule; Mitochondrion; Motor protein; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..89
FT /note="Dynein light chain 1, cytoplasmic"
FT /id="PRO_0000195128"
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
