DC1L2_RAT
ID DC1L2_RAT Reviewed; 497 AA.
AC Q62698;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cytoplasmic dynein 1 light intermediate chain 2;
DE AltName: Full=Dynein light intermediate chain 2, cytosolic;
DE Short=LIC-2;
DE AltName: Full=LIC53/55;
GN Name=Dync1li2; Synonyms=Dncli2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7738094; DOI=10.1242/jcs.108.1.17;
RA Hughes S.M., Vaughan K.T., Herskovits J.S., Vallee R.B.;
RT "Molecular analysis of a cytoplasmic dynein light intermediate chain
RT reveals homology to a family of ATPases.";
RL J. Cell Sci. 108:17-24(1995).
RN [2]
RP SUBUNIT.
RX PubMed=10893222; DOI=10.1074/jbc.m001536200;
RA Tynan S.H., Purohit A., Doxsey S.J., Vallee R.B.;
RT "Light intermediate chain 1 defines a functional subfraction of cytoplasmic
RT dynein which binds to pericentrin.";
RL J. Biol. Chem. 275:32763-32768(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- 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. {ECO:0000250,
CC ECO:0000269|PubMed:10893222}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; U15138; AAA80334.1; -; mRNA.
DR PIR; I55514; I55514.
DR RefSeq; NP_112288.1; NM_031026.1.
DR AlphaFoldDB; Q62698; -.
DR SMR; Q62698; -.
DR BioGRID; 249555; 2.
DR IntAct; Q62698; 1.
DR STRING; 10116.ENSRNOP00000029646; -.
DR iPTMnet; Q62698; -.
DR PhosphoSitePlus; Q62698; -.
DR SwissPalm; Q62698; -.
DR jPOST; Q62698; -.
DR PaxDb; Q62698; -.
DR PRIDE; Q62698; -.
DR Ensembl; ENSRNOT00000034472; ENSRNOP00000029646; ENSRNOG00000025791.
DR GeneID; 81655; -.
DR KEGG; rno:81655; -.
DR UCSC; RGD:621130; rat.
DR CTD; 1783; -.
DR RGD; 621130; Dync1li2.
DR eggNOG; KOG3905; Eukaryota.
DR GeneTree; ENSGT00390000008295; -.
DR HOGENOM; CLU_021937_2_1_1; -.
DR InParanoid; Q62698; -.
DR OMA; WKEEEFD; -.
DR OrthoDB; 1299592at2759; -.
DR PhylomeDB; Q62698; -.
DR TreeFam; TF352602; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9646399; Aggrephagy.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q62698; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000025791; Expressed in Ammon's horn and 20 other tissues.
DR ExpressionAtlas; Q62698; baseline and differential.
DR Genevisible; Q62698; RN.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; IDA:RGD.
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:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:RGD.
DR GO; GO:0051642; P:centrosome localization; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Dynein; Methylation; Microtubule;
KW Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..497
FT /note="Cytoplasmic dynein 1 light intermediate chain 2"
FT /id="PRO_0000114674"
FT REGION 187..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..408
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:0007744|PubMed:22673903"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 383
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 427
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43237"
SQ SEQUENCE 497 AA; 54745 MW; D4E2715880E194B4 CRC64;
MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRARSK LPSGKNILVF
GEDGSGKTTL MTKLQGAEHG KKGRGLEYLY LSVHDEDRDD HTRCNVWILD GDLYHKGLLK
FAVSAESLRE TLVIFVADMS RPWTIMESLQ KWASVLREHI DKMKIPPEEM RDLERKFMKD
FQDYIEPEEG CQGSPQRRGP LTSGSDEDNV ALPLGDNVLT HNLGIPVLVV CTKCDAVSIL
EKEHDYRDEH LDFIQAHLRG FCLQYGAALI YTSVKEEKNL DLLYKYIVHK TYGFHFTIPA
LVVEKDAVFI PAGWDNEKKI AILHENFTTV KPEDAYEDFI VKPPVRKLVH DKELAAEDEQ
VFLMKQQESP ARGPSGSPRT QGRGGPASVP SASPGTSVKK PDPNIKNNAA SEGVLASFFN
SLLSKKTGSP GSPSAGGVQS TAKKSGTEGE PQSFRSLTEQ CCQTGQKTVL SNVQEELDRM
TRKPDSMVTN SSTENEA
