DC1L1_RAT
ID DC1L1_RAT Reviewed; 523 AA.
AC Q9QXU8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytoplasmic dynein 1 light intermediate chain 1;
DE AltName: Full=Dynein light chain A;
DE Short=DLC-A;
DE AltName: Full=Dynein light intermediate chain 1, cytosolic;
GN Name=Dync1li1; Synonyms=Dncli1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND INTERACTION WITH PCNT.
RX PubMed=10893222; DOI=10.1074/jbc.m001536200;
RA Tynan S.H., Purohit A., Doxsey S.J., Vallee R.B.;
RT "Light intermediate chain 1 defines a functional subfraction of cytoplasmic
RT dynein which binds to pericentrin.";
RL J. Biol. Chem. 275:32763-32768(2000).
RN [2]
RP INTERACTION WITH PCNT.
RX PubMed=10545494; DOI=10.1083/jcb.147.3.481;
RA Purohit A., Tynan S.H., Vallee R., Doxsey S.J.;
RT "Direct interaction of pericentrin with cytoplasmic dynein light
RT intermediate chain contributes to mitotic spindle organization.";
RL J. Cell Biol. 147:481-492(1999).
RN [3]
RP INTERACTION WITH DYNC1H1.
RX PubMed=10893223; DOI=10.1074/jbc.m001537200;
RA Tynan S.H., Gee M.A., Vallee R.B.;
RT "Distinct but overlapping sites within the cytoplasmic dynein heavy chain
RT for dimerization and for intermediate chain and light intermediate chain
RT binding.";
RL J. Biol. Chem. 275:32769-32774(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-516, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 binding dynein to membranous organelles or chromosomes.
CC Probably involved in the microtubule-dependent transport of
CC pericentrin. Is required for progress through the spindle assembly
CC checkpoint. The phosphorylated form appears to be involved in the
CC selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (Probable). The cytoplasmic dynein 1 complex
CC consists of two catalytic heavy chains (HCs) and a number of non-
CC catalytic subunits presented by intermediate chains (ICs), light
CC intermediate chains (LICs) and light chains (LCs); the composition
CC seems to vary in respect to the IC, LIC and LC composition. The heavy
CC chain homodimer serves as a scaffold for the probable homodimeric
CC assembly of the respective non-catalytic subunits. The ICs and LICs
CC bind directly to the HC dimer and the LCs assemble on the IC dimer.
CC Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind
CC mutually exclusive to DYNC1H1. Interacts with PCNT.
CC {ECO:0000269|PubMed:10545494, ECO:0000269|PubMed:10893222,
CC ECO:0000269|PubMed:10893223, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis but not in interphase.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF181992; AAF22294.1; -; mRNA.
DR RefSeq; NP_665715.1; NM_145772.1.
DR AlphaFoldDB; Q9QXU8; -.
DR SMR; Q9QXU8; -.
DR BioGRID; 251663; 2.
DR CORUM; Q9QXU8; -.
DR IntAct; Q9QXU8; 1.
DR MINT; Q9QXU8; -.
DR STRING; 10116.ENSRNOP00000014532; -.
DR iPTMnet; Q9QXU8; -.
DR PhosphoSitePlus; Q9QXU8; -.
DR SwissPalm; Q9QXU8; -.
DR jPOST; Q9QXU8; -.
DR PaxDb; Q9QXU8; -.
DR PRIDE; Q9QXU8; -.
DR GeneID; 252902; -.
DR KEGG; rno:252902; -.
DR UCSC; RGD:71072; rat.
DR CTD; 51143; -.
DR RGD; 71072; Dync1li1.
DR eggNOG; KOG3905; Eukaryota.
DR InParanoid; Q9QXU8; -.
DR OrthoDB; 1299592at2759; -.
DR PhylomeDB; Q9QXU8; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9646399; Aggrephagy.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q9QXU8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045504; F:dynein heavy chain binding; ISO:RGD.
DR GO; GO:0019003; F:GDP binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; TAS:RGD.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR GO; GO:0046605; P:regulation of centrosome cycle; IDA:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008467; Dynein1_light_intermed_chain.
DR InterPro; IPR022780; Dynein_light_int_chain.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12688; PTHR12688; 1.
DR Pfam; PF05783; DLIC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Dynein; Kinetochore; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..523
FT /note="Cytoplasmic dynein 1 light intermediate chain 1"
FT /id="PRO_0000114668"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 512
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 513
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6G9"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 523 AA; 56792 MW; 3F393348FF90696B CRC64;
MAAVGRVGSF GSSPPGLAST YASGPLANEL ASGSGGPAAG DDEDGQNLWS RILREVSTRS
RSKLPTGKNV LLLGEDGAGK TSLIRRIQGI EEYKKGRGLE YLYLNVHDED RDDQTRCNVW
ILDGDLYHKG LLKFSLDALS LRDTLVMLVV DMSKPWTALD SLQKWASVVR EHVDKLKIPP
EEMKEMEQKL IRDFQEYVEP GEDFPASPQR RATAAQEDRD DSVVLPLGAD TLTHNLGLPV
LVVCTKCDAI SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI
VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKIEDNFE DIITKPPVRK
FVHEKEIMAE DDQVFLMKLQ SLLAKQPPTA AGRPVDASPR VPGGSPRTPN RSVSSNVASV
SPIPAGSKKI DPNMKAGATS EGVLANFFNS LLSKKTGSPG GPGVGGSPGG GAAGASTSLP
PSAKKSGQKP VLSDVHAELD RITRKPASVS PTTPPSPTEG EAS
