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Database: UniProt
Entry: A0A091L3A8_COLST
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Original site: A0A091L3A8_COLST 
ID   A0A091L3A8_COLST        Unreviewed;       331 AA.
AC   A0A091L3A8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
DE   Flags: Fragment;
GN   ORFNames=N325_10895 {ECO:0000313|EMBL:KFP34384.1};
OS   Colius striatus (Speckled mousebird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX   NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP34384.1, ECO:0000313|Proteomes:UP000053615};
RN   [1] {ECO:0000313|EMBL:KFP34384.1, ECO:0000313|Proteomes:UP000053615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP34384.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KK553236; KFP34384.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091L3A8; -.
DR   Proteomes; UP000053615; 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   CDD; cd00882; Ras_like_GTPase; 1.
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:SF2; CYTOPLASMIC DYNEIN 1 LIGHT INTERMEDIATE CHAIN 1; 1.
DR   PANTHER; PTHR12688; 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:UP000053615};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP34384.1"
FT   NON_TER         331
FT                   /evidence="ECO:0000313|EMBL:KFP34384.1"
SQ   SEQUENCE   331 AA;  37962 MW;  C4463EF163410477 CRC64;
     SCILSEVSTR SRSKLPSGKN VLLLGEDGAG KTSLIGKIQG IEEYKKGRGM EYLYLNVHDE
     DREDQTRCNV WILDGDLYHK GLLKFAMEAN SLKDTLVMLA VDMSRPWTAL DSLQKWASVV
     REHIDKLKIP PEEMKEMEQK LVRDFQEYVE PGEDFPASPQ RRNTSLQEDK DDSVILPLGA
     DTLTCNLGIP VVVVCTKCDA ISILEKEHDY RDEHFDFIQS HIRRFCLQYG AALIYTSVKE
     NKNIDLVYKY IVQKLYGFPF NVPAMVVEKD AVFIPAGWDN DKKIGILHEN FQTLKAEDSF
     EDIITKPPVR KFVHEKEIVA EDDQVFLMKQ Q
//
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