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Database: UniProt
Entry: A0A452SVE1_URSAM
LinkDB: A0A452SVE1_URSAM
Original site: A0A452SVE1_URSAM 
ID   A0A452SVE1_URSAM        Unreviewed;       524 AA.
AC   A0A452SVE1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN   Name=DYNC1LI1 {ECO:0000313|Ensembl:ENSUAMP00000036877.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000036877.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000036877.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A452SVE1; -.
DR   STRING; 9643.ENSUAMP00000036877; -.
DR   Ensembl; ENSUAMT00000041045.1; ENSUAMP00000036877.1; ENSUAMG00000027924.1.
DR   GeneTree; ENSGT00390000008295; -.
DR   OMA; VMLEKDF; -.
DR   OrthoDB; 179830at2759; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0030666; C:endocytic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0045504; F:dynein heavy chain binding; IEA:Ensembl.
DR   GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:Ensembl.
DR   GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IEA:Ensembl.
DR   GO; GO:0060627; P:regulation of vesicle-mediated transport; 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:UP000291022};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT   REGION          202..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  56589 MW;  45DB63DA827DB92A CRC64;
     MAAVGRVGSF GSSPPGLAST YTGGPLANEL TSGNGGAAAG DDEDGQNLWS CILSEVSTRS
     RSKLPAGKNV LLLGEDGAGK TSLIRKIQGI EEYKKGRGLE YLYLNVHDED REDQTRCNVW
     ILDGDLYHKG LLKFSLDAIS LKDTLVMLVV DMSKPWTALD SLQKWASVVR EHIDKLKIPP
     EEIKEMEQKL IRDFQEYVEP GEDFPASPQR RNTGSQEDKD DSVVLPLGAD TLTHNLGIPV
     LVVCTKCDAI SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI
     VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKAEDNFE DIITKPPVRK
     FVHEKEIVAE DDQVFLMKLQ SLLAKQPPTA AGRPVDASPR VPGGSPRTPN RSVSSNVASV
     SPIPAGSKKI DPNMKAGATS EGVLANFFNS LLSKKTGSPG GPGVGSGSPG GGAGGGSSGL
     PPSAKKSGQK PVLSDVHAEL DRIARKPVTV SSTTPTSPTE GEAS
//
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