ID W7U234_9STRA Unreviewed; 607 AA.
AC W7U234;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN Name=D1LIC {ECO:0000313|EMBL:EWM26714.1};
GN ORFNames=Naga_100001g9 {ECO:0000313|EMBL:EWM26714.1};
OS Nannochloropsis gaditana.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM26714.1, ECO:0000313|Proteomes:UP000019335};
RN [1] {ECO:0000313|EMBL:EWM26714.1, ECO:0000313|Proteomes:UP000019335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-31 {ECO:0000313|EMBL:EWM26714.1,
RC ECO:0000313|Proteomes:UP000019335};
RX PubMed=23966634; DOI=10.1093/mp/sst120;
RA Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT Nannochloropsis gaditana in Nitrogen Depletion.";
RL Mol. Plant 7:323-335(2014).
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:EWM26714.1}.
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DR EMBL; AZIL01000609; EWM26714.1; -; Genomic_DNA.
DR AlphaFoldDB; W7U234; -.
DR EnsemblProtists; EWM26714; EWM26714; Naga_100001g9.
DR OrthoDB; 48125at2759; -.
DR Proteomes; UP000019335; Chromosome 8.
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 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; 2.
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:UP000019335};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT REGION 530..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 65998 MW; 4F57FC8F5DEA7228 CRC64;
MSAGENAGVA QRETELIWGP LLAEAARSEQ SNFTPGTILF LGDAAVGKTR LIDRFITSYD
ALERQAAATG RNFIAEEEKE DEEGQEGSGA LSSHDHSLLS YAFFPAIDPV GCKAGGQSWD
NGTVGRSSDC LPGRCPAGAS KGLAEDDQDA GVDENEMDAG ARVNVWSLSD PALKDLLHVA
LDDPGVRRRA ASIRSEVPTD PRFDTSSLNS KSTPAQTLQR TICMIAIDLT RPWACESALE
RWVGVLRSVL GEKARAGCHK GEEEGEEERV RKARLVAYLS RCYQGEDMDR VWLERGELKE
EDEGGGLEEP KVVFRINRME SSGGRPLSSP QPARSTPLPA GVLEENLGVP LVVVGLKADL
APVPDSYDDG LRSLFFQQYL RRVCLKYGAS LVYTSASNGD NCLLLQRYLL HRLYPEHFSF
LLPVQAPRAL TFVPSGWDTP ELVQKLLSPQ AVPWPPSLTF SEIFVPPKGA RAYLDRGDGG
AEVCSETWEQ ESSERHTEIT PTQAWLERLW EQQQQQRQRC PQNLGDGDCG RTMAGEADGS
AGNHDAGGLR EGPMGSTGKG RSTRYGNSNR SIGEANQRSE PYNAGGGADK AEIRNFFEGL
LAGGGKK
//
