ID M3XH93_LATCH Unreviewed; 502 AA.
AC M3XH93;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN Name=DYNC1LI1 {ECO:0000313|Ensembl:ENSLACP00000022099.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000022099.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000022099.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AFYH01112921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006000638.1; XM_006000576.2.
DR AlphaFoldDB; M3XH93; -.
DR STRING; 7897.ENSLACP00000022099; -.
DR Ensembl; ENSLACT00000026293.1; ENSLACP00000022099.1; ENSLACG00000012570.2.
DR GeneID; 102347726; -.
DR KEGG; lcm:102347726; -.
DR CTD; 51143; -.
DR eggNOG; KOG3905; Eukaryota.
DR GeneTree; ENSGT00390000008295; -.
DR InParanoid; M3XH93; -.
DR OMA; VMLEKDF; -.
DR OrthoDB; 179830at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000012570; Expressed in post-anal tail muscle and 6 other cell types or tissues.
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 GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IEA:Ensembl.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IEA:Ensembl.
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:UP000008672};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 55264 MW; EBDAD3F54BCE1A13 CRC64;
MAAVSRAGSS SSASPQFGGS HSSPSSGGAV EDRYGEDDDG HNLWSSILSE VSTRSRSKLP
SGKTVLVLGE DGAGKTNLIA RLQGIEEYKK GRGMEFLYFN VHDEDRDDSA RCNVWILDGD
LYHKGLLKFA MNSCPVKDML VMLVVDVARP WSALETLHKW ASVIREHVDK LKIPPEEMKE
MEQQLIRQFQ EYTEPGEAFP ASPQRRNTSL QEEQDENVVL PLGEDTLTHN LGIPVVVVCT
KCDTISVLEK EHDYRDEHFD FVQSHIRRFC LHYGAALIYT SIKESKNIDL VYKYLVHRLY
GFPFNTPALV VEKDAVFIPA GWDNDKKIGI LHENFQTIKA DDPFEDIIVK PPIRKFVHEK
EIVTEDDQVF LMKLQSQLAK QPPIAAGRPV DASPRPPGGS PRTPSRSGSA NVASVTPIPA
GTKKIDPNMK AGTTSEGVLA NFFNSLLSKK TGTAGSGSTP SSAKKSGQKP VLTDVQAELN
RISRKPEAVS PTSPTSPIDE AS
//
