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Database: UniProt
Entry: A0A091HTB8_CALAN
LinkDB: A0A091HTB8_CALAN
Original site: A0A091HTB8_CALAN 
ID   A0A091HTB8_CALAN        Unreviewed;       455 AA.
AC   A0A091HTB8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
DE   Flags: Fragment;
GN   ORFNames=N300_03389 {ECO:0000313|EMBL:KFO99191.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO99191.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFO99191.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO99191.1};
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|ARBA:ARBA00037133, 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|ARBA:ARBA00004245, 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; KL217815; KFO99191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091HTB8; -.
DR   STRING; 9244.A0A091HTB8; -.
DR   Proteomes; UP000054308; 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:SF1; CYTOPLASMIC DYNEIN 1 LIGHT INTERMEDIATE CHAIN 2; 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   Methylation {ECO:0000256|ARBA:ARBA00022481};
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT   REGION          153..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO99191.1"
FT   NON_TER         455
FT                   /evidence="ECO:0000313|EMBL:KFO99191.1"
SQ   SEQUENCE   455 AA;  50640 MW;  1553DB98EF747F71 CRC64;
     SSILSEVSTR SRSKLPSGKN ILVFGDDGSG KTTLMAKIQG AEHGKKGRGL EYLYLNIHDE
     DRDDHTRCNV WILDGDLYHK GLLKFAVSAE SLQDTIVVFV ADMSRPWTVM ESLQKWASVL
     QEHIDKMKIP PEEMRDMEQK FIKEFQEYVE PEEGYQGSPQ RRGPSGQEDE HVSLPLGENV
     LTHNLGIPVL VVCTKCDAVS VLEKEHDYRE EHFDFIQSHI RRFCLQYGAA LIYTSVKEEK
     NLDLLYKYIV HKTYGFQFTT PALVVEKDAV FIPAGWDNEK KIAILHENFT TVKPEDAYED
     FIVKPPVRKL VHDKELAAED EQVFLMKQQS FLAKQPATPT RASESPARGP AGSPRTQGRA
     GPANVPSASP ITPVKKPDPN IKNNAASEGV LASFFNSLLS KKTGSPGSPG AGGVQSTAKK
     SGQKTVLTNV QEELDRMTRK PDSMVTTNSP TENEA
//
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