DC1L2_MACFA
ID DC1L2_MACFA Reviewed; 492 AA.
AC Q4R5P6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Cytoplasmic dynein 1 light intermediate chain 2;
DE AltName: Full=Dynein light intermediate chain 2, cytosolic;
GN Name=DYNC1LI2; Synonyms=DNCLI2; ORFNames=QccE-11322;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). The cytoplasmic dynein 1 complex
CC consists of two catalytic heavy chains (HCs) and a number of non-
CC catalytic subunits presented by intermediate chains (ICs), light
CC intermediate chains (LICs) and light chains (LCs); the composition
CC seems to vary in respect to the IC, LIC and LC composition. The heavy
CC chain homodimer serves as a scaffold for the probable homodimeric
CC assembly of the respective non-catalytic subunits. The ICs and LICs
CC bind directly to the HC dimer and the LCs assemble on the IC dimer.
CC Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind
CC mutually exclusive to DYNC1H1 (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; AB169497; BAE01579.1; -; mRNA.
DR RefSeq; NP_001306338.1; NM_001319409.1.
DR AlphaFoldDB; Q4R5P6; -.
DR SMR; Q4R5P6; -.
DR STRING; 9541.XP_005592216.1; -.
DR PRIDE; Q4R5P6; -.
DR GeneID; 102143512; -.
DR CTD; 1783; -.
DR eggNOG; KOG3905; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IEA:InterPro.
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 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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Dynein; Methylation; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..492
FT /note="Cytoplasmic dynein 1 light intermediate chain 2"
FT /id="PRO_0000114671"
FT REGION 187..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 397
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
SQ SEQUENCE 492 AA; 54072 MW; 986AA06C16F3E4E1 CRC64;
MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRARSK LPSGKSILVF
GEDGSGKTTL MTKLQGAEHG KKGRGLEYLY LSVHDEDRDD HTRCNVWILD GDLYHKGLLK
FAVSAESLPE TLVIFVADMS RPWTVMESLQ KWASVLREHI DKMKIPPEKM RELERKFVKD
FQDYMEPEEG CQGSPQRRGP LTSGSDEENV ALPLGDNVLT HNLGIPVLVV CTKCDAVSVL
EKEHDYRDEH LDFIQSHLRR FCLQYGAALI YTSVKEEKNL DLLYKYIVHK TYGFHFTTPA
LVVEKDAVFI PAGWDNEKKI AILHENFTTV KPEDAYEDFI VKPPVRKLVH DKELAAEDEQ
VFLMKQQSLL AKQPATPTRA SESPARGPSG SPRTQGRGGP ASVPSSSPGT SVKKPDPNIK
NNAASEGVLA SFFNSLLSKK TGSPGSPGAG GVQSTAKKSG QKTVLSNVQE ELDRMTRKPD
SMVTNSSTEN EA
