DC1L1_CHICK
ID DC1L1_CHICK Reviewed; 515 AA.
AC Q90828;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
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;
DE AltName: Full=LIC57/59;
GN Name=DYNC1LI1; Synonyms=DNCLI1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 90-98.
RC TISSUE=Embryonic brain;
RX PubMed=7949421; DOI=10.1091/mbc.5.6.645;
RA Gill S.R., Cleveland D.W., Schroer T.A.;
RT "Characterization of DLC-A and DLC-B, two families of cytoplasmic dynein
RT light chain subunits.";
RL Mol. Biol. Cell 5:645-654(1994).
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 (By similarity). {ECO:0000250}.
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) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; X79088; CAA55698.1; -; mRNA.
DR PIR; I50637; I50637.
DR RefSeq; NP_001161209.1; NM_001167737.1.
DR AlphaFoldDB; Q90828; -.
DR SMR; Q90828; -.
DR BioGRID; 681601; 1.
DR STRING; 9031.ENSGALP00000018705; -.
DR iPTMnet; Q90828; -.
DR PaxDb; Q90828; -.
DR PRIDE; Q90828; -.
DR Ensembl; ENSGALT00000018728; ENSGALP00000018705; ENSGALG00000011491.
DR GeneID; 420668; -.
DR KEGG; gga:420668; -.
DR CTD; 51143; -.
DR VEuPathDB; HostDB:geneid_420668; -.
DR eggNOG; KOG3905; Eukaryota.
DR GeneTree; ENSGT00390000008295; -.
DR HOGENOM; CLU_021937_2_1_1; -.
DR InParanoid; Q90828; -.
DR OMA; RCNIWIL; -.
DR OrthoDB; 1299592at2759; -.
DR PhylomeDB; Q90828; -.
DR TreeFam; TF352602; -.
DR Reactome; R-GGA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-GGA-2467813; Separation of Sister Chromatids.
DR Reactome; R-GGA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-GGA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-GGA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-GGA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-GGA-9646399; Aggrephagy.
DR Reactome; R-GGA-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q90828; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000011491; Expressed in heart and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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; Cytoplasm; Cytoskeleton; Direct protein sequencing; Dynein;
KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..515
FT /note="Cytoplasmic dynein 1 light intermediate chain 1"
FT /id="PRO_0000114669"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 515 AA; 55893 MW; F163848CCDC7854E CRC64;
MAAVGRAGSF GSSSASGAAN NASAELRAGG EEDDGQNLWS CILSEVSTRS RSKLPSGKSV
LLLGEDGAGK TSLIGKIQGI EEYKKGRGME YLYLNVHDED RDDQTRCNVR ILDGDLYHKG
LLKFAMEANS LKDTLIMLVV DMSRPWTAMD SLQKWASVVR EHIDKLKIPP EEMKEMEQKL
VRDFQEYVEP GEDFPASPQR RNTSLQEDKD DSVILPLGAD TLTCNLGIPV VVVCTKCDAI
SVLEKEHDYR DEHFDFIQSH IRRFCLQYGA ALIYTSVKEN KNIDLVYKYI VQKLYGFPFN
VPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKAEDSFE DSIRKPPVRK FVHEKEIVAE
DDQVFLMKQQ SQLAKQPPTA AGRPVDASPR VPGGSPRTPN RSVTSNVASV TPIPAGSKKI
DPNMKAGATS EGVLANFFNS LLSKKTGSPG GPGGVGGSPG GGSAGGTGSN LPPSAKKSGQ
KPVLTDVQAE LDRISRKPEM VSPTSPTSPT EGEAS
