DC1L1_DICDI
ID DC1L1_DICDI Reviewed; 504 AA.
AC Q54CI8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cytoplasmic dynein 1 light intermediate chain 1;
DE AltName: Full=Dynein light intermediate chain 1, cytosolic;
GN Name=dync1li1; ORFNames=DDB_G0292904;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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), light intermediate chains
CC (LICs) and light chains (LCs) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000197; EAL61001.1; -; Genomic_DNA.
DR RefSeq; XP_629428.1; XM_629426.1.
DR AlphaFoldDB; Q54CI8; -.
DR SMR; Q54CI8; -.
DR STRING; 44689.DDB0233302; -.
DR PaxDb; Q54CI8; -.
DR EnsemblProtists; EAL61001; EAL61001; DDB_G0292904.
DR GeneID; 8628947; -.
DR KEGG; ddi:DDB_G0292904; -.
DR dictyBase; DDB_G0292904; dync1li1.
DR eggNOG; KOG3905; Eukaryota.
DR HOGENOM; CLU_021937_2_0_1; -.
DR InParanoid; Q54CI8; -.
DR OMA; WKEEEFD; -.
DR PhylomeDB; Q54CI8; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR PRO; PR:Q54CI8; -.
DR Proteomes; UP000002195; Chromosome 6.
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 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; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1..504
FT /note="Cytoplasmic dynein 1 light intermediate chain 1"
FT /id="PRO_0000327573"
FT REGION 167..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 504 AA; 56713 MW; 8254CE11969E6463 CRC64;
MVEQQQQEED IWGQILRESS NKNNYFEKRD VAILGDPTSG KSLLLSKFDT VSNVESLKSI
ALSYTFSDIY EDDTSEDPVG RINYWSLEGE ASQNDLLKFS LNKENIKNCM VIITLDFSQP
WNLVESLKKW LGILEEHIKS IFKDDKNGFK NLQDKLSIKW HEYEEPTTTA ATTTTTTTSN
NIENNTNKTS PTTDKIQTNN VQKKKKKKVN ISSAEDASVL PPLSENILIN NLGVPILVAC
CKSDSVVMLE KDFDYKDELF DYIQQYLRRI CLQYGAGLIY TSARKEINCG VTLEYIENIL
FGFELKSKTQ LIEKDQIFVP AGWDTLAKIQ VDFENQKVCK DTDEPYENIV KKPSIIKRRE
QTQTNSIICD DDQDFLGKIK SQLDNDDQSS INSPSTPSPL SQSSNNNNSN NNINNTSTPS
INTPLQPTDK PLSDIKSSNN PVAASPSAER AALANFFTSL ISKDKTSSRK DLKSSLASPP
TTSVSSNARE DAKKELDKLK QQKK
