ID U3K3C9_FICAL Unreviewed; 531 AA.
AC U3K3C9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN Name=DYNC1LI1 {ECO:0000313|Ensembl:ENSFALP00000009533.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000009533.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000009533.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000009533.2}
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; U3K3C9; -.
DR STRING; 59894.ENSFALP00000009533; -.
DR Ensembl; ENSFALT00000009573.2; ENSFALP00000009533.2; ENSFALG00000009138.2.
DR eggNOG; KOG3905; Eukaryota.
DR GeneTree; ENSGT00390000008295; -.
DR HOGENOM; CLU_021937_2_1_1; -.
DR Proteomes; UP000016665; Chromosome 2.
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 CDD; cd00882; Ras_like_GTPase; 1.
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:UP000016665};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 56985 MW; 03276C139EE92FA2 CRC64;
GGGGGGGGGG ASSSSGLGSA ASFSSASSAA STATANNNNA ELRAGGDEDD GQNLWSCILS
EVSTRSRSKL PSGKNVLLLG EDGAGKTSLI GKIQGIEEYK KGRGMEYLYL NVHDEDRDDQ
TRCNVWILDG DLYHKGLLKF AMEASSLKDT LVMLVVDMSR PWTALDSLQK WASVVREHID
KLKIPPEEMK EMEQKLVRDF QEYIEPGEDF PASPQRRNTS LQEDKDDSVI LPLGADTLTC
NLGIPVVVVC TKCDAISVLE KEHDYRDEHF DFIQSHIRRF CLQYGAALIY TSVKENKNID
LVYKYIVQKL YGFPFNVPAV VVEKDAVFIP AGWDNDKKIG ILHENFQTLK ADDNFEDIIT
KPPVRKFVHE KEIVAEDDQV FLMKQQSQLA KQPPTAAGRP VDASPRVPGG SPRTPNRSVT
SNVASVTPIP TGSKKIDPNM KAGATSEGVL ANFFNSLLSK KTGSPGGPGG VGGSPGGGGT
GGAGSNLPPS AKKSGQKPVL TDVQAELDRI SRKPEMVSPT SSTSPTEGEA S
//
