ID A0A443R2U5_9ACAR Unreviewed; 471 AA.
AC A0A443R2U5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN ORFNames=B4U79_01056 {ECO:0000313|EMBL:RWS09577.1}, B4U79_05234
GN {ECO:0000313|EMBL:RWS03393.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS09577.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS09577.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS09577.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:RWS09577.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS09577.1};
RA Dong X.;
RT "Trombidioid mite genomics.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|RuleBase:RU366047}.
CC -!- SUBUNIT: Homodimer. 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).
CC {ECO:0000256|RuleBase:RU366047}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|RuleBase:RU366047}.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000256|ARBA:ARBA00006831, ECO:0000256|RuleBase:RU366047}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWS09577.1}.
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; NCKU01006547; RWS03393.1; -; Genomic_DNA.
DR EMBL; NCKU01002444; RWS09577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443R2U5; -.
DR STRING; 1965070.A0A443R2U5; -.
DR Proteomes; UP000285301; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR008467; Dynein1_light_intermed_chain.
DR InterPro; IPR022780; Dynein_light_int_chain.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12688; DYNEIN LIGHT INTERMEDIATE CHAIN; 1.
DR PANTHER; PTHR12688:SF0; DYNEIN LIGHT INTERMEDIATE CHAIN; 1.
DR Pfam; PF05783; DLIC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366047};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU366047};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|RuleBase:RU366047}; Dynein {ECO:0000256|RuleBase:RU366047};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU366047};
KW Motor protein {ECO:0000256|RuleBase:RU366047};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366047};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT REGION 369..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 52461 MW; 8F860CA85F2CD072 CRC64;
MNNGECSEEE HVWLTILQQV QSCSSNKLPS NKALLVIGEN ETGKTSLIAK IQGNDDPKKG
SGLEYHHLLV RDEYRDEQTR LGVWVLDGDL YHQNLLKFAL NEASFPNTTV LLIASMTNPW
DILDSLEKWA NILEEHIERL KMKPEKLNHF KQLVMKRYLD YISPGDEIEG LVTSPVKSRS
ESISDNLVES SNSTHTNCNA DTLGENVLTH NLGLDIVVVI TKTDYMSTLE KEYDYKEEAF
DFIQQAVRKF CLKYGASLFY VSAKVNKNCD LLYKYLVHRI YGLPFKTPAL VVEKDAVFIP
AGWDSEKKIA ILYENIQSCS PDDNYNDIIA KPVSKRPLQK DIEITSEDDQ VFLLKMQAQL
NQNVPSVGVT NQTPTIRTSP AIQKPLDRRS MGTSPVSGVP IDGPKNSPAG EGVLQNFFNS
LLNRKSGAGS GGSPRHGSER DTRSIAEELH RMTGGTGIAT TGTPTANANN K
//
