DC1I1_MOUSE
ID DC1I1_MOUSE Reviewed; 628 AA.
AC O88485; O88486; Q80W09;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 1;
DE AltName: Full=Cytoplasmic dynein intermediate chain 1;
DE AltName: Full=Dynein intermediate chain 1, cytosolic;
DE Short=DH IC-1;
GN Name=Dync1i1; Synonyms=Dnci1, Dncic1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B).
RX PubMed=10049579; DOI=10.1006/geno.1998.5665;
RA Crackower M.A., Sinasac D.S., Xia J., Motoyama J., Prochazka M.,
RA Rommens J.M., Scherer S.W., Tsui L.-C.;
RT "Cloning and characterization of two cytoplasmic dynein intermediate chain
RT genes in mouse and human.";
RL Genomics 55:257-267(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH DYNLL2, AND MUTAGENESIS OF 151-LYS--THR-155.
RX PubMed=11148209; DOI=10.1074/jbc.m010320200;
RA Lo K.W., Naisbitt S., Fan J.S., Sheng M., Zhang M.;
RT "The 8-kDa dynein light chain binds to its targets via a conserved
RT (K/R)XTQT motif.";
RL J. Biol. Chem. 276:14059-14066(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-94; SER-97; THR-159;
RP SER-162; SER-180 AND SER-618, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. The
CC intermediate chains mediate the binding of dynein to dynactin via its
CC 150 kDa component (p150-glued) DCTN1. May play a role in mediating the
CC interaction of cytoplasmic dynein with membranous organelles and
CC kinetochores.
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 Interacts with DYNC1H1. Interacts with DYNLT1 and DYNLT3. Interacts
CC with DCTN1 (By similarity). Interacts with DYNLL2. {ECO:0000250,
CC ECO:0000269|PubMed:11148209}.
CC -!- INTERACTION:
CC O88485; Q64368: Dazl; NbExp=4; IntAct=EBI-492834, EBI-2024439;
CC O88485; P63168: Dynll1; NbExp=2; IntAct=EBI-492834, EBI-349121;
CC O88485; Q61768: Kif5b; NbExp=4; IntAct=EBI-492834, EBI-776129;
CC O88485; P06537: Nr3c1; NbExp=2; IntAct=EBI-492834, EBI-492753;
CC O88485; P42858: HTT; Xeno; NbExp=2; IntAct=EBI-492834, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1A;
CC IsoId=O88485-1; Sequence=Displayed;
CC Name=1B;
CC IsoId=O88485-2; Sequence=VSP_001334;
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; AF063229; AAC33444.1; -; mRNA.
DR EMBL; AF063230; AAC33445.1; -; mRNA.
DR EMBL; CH466533; EDL13960.1; -; Genomic_DNA.
DR EMBL; BC051992; AAH51992.1; -; mRNA.
DR CCDS; CCDS19903.1; -. [O88485-1]
DR CCDS; CCDS57408.1; -. [O88485-2]
DR RefSeq; NP_001177952.1; NM_001191023.1.
DR RefSeq; NP_001177954.1; NM_001191025.1. [O88485-2]
DR RefSeq; NP_034193.2; NM_010063.4. [O88485-1]
DR AlphaFoldDB; O88485; -.
DR SMR; O88485; -.
DR BioGRID; 199255; 48.
DR CORUM; O88485; -.
DR DIP; DIP-32048N; -.
DR ELM; O88485; -.
DR IntAct; O88485; 12.
DR MINT; O88485; -.
DR STRING; 10090.ENSMUSP00000111221; -.
DR iPTMnet; O88485; -.
DR PhosphoSitePlus; O88485; -.
DR SwissPalm; O88485; -.
DR EPD; O88485; -.
DR MaxQB; O88485; -.
DR PaxDb; O88485; -.
DR PeptideAtlas; O88485; -.
DR PRIDE; O88485; -.
DR ProteomicsDB; 279170; -. [O88485-1]
DR ProteomicsDB; 279171; -. [O88485-2]
DR Antibodypedia; 15905; 160 antibodies from 26 providers.
DR DNASU; 13426; -.
DR Ensembl; ENSMUST00000115554; ENSMUSP00000111216; ENSMUSG00000029757. [O88485-2]
DR Ensembl; ENSMUST00000115559; ENSMUSP00000111221; ENSMUSG00000029757. [O88485-1]
DR GeneID; 13426; -.
DR KEGG; mmu:13426; -.
DR UCSC; uc009awm.2; mouse. [O88485-2]
DR UCSC; uc012ehw.1; mouse. [O88485-1]
DR CTD; 1780; -.
DR MGI; MGI:107743; Dync1i1.
DR VEuPathDB; HostDB:ENSMUSG00000029757; -.
DR eggNOG; KOG1587; Eukaryota.
DR GeneTree; ENSGT00940000156032; -.
DR HOGENOM; CLU_012999_1_1_1; -.
DR InParanoid; O88485; -.
DR OMA; YVRDYTI; -.
DR TreeFam; TF300553; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 13426; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dync1i1; mouse.
DR PRO; PR:O88485; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O88485; protein.
DR Bgee; ENSMUSG00000029757; Expressed in pontine nuclear group and 192 other tissues.
DR ExpressionAtlas; O88485; baseline and differential.
DR Genevisible; O88485; MM.
DR GO; GO:1904115; C:axon cytoplasm; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR GO; GO:1990257; C:piccolo-bassoon transport vesicle; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR GO; GO:0045503; F:dynein light chain binding; IPI:MGI.
DR GO; GO:0008017; F:microtubule binding; ISS:HGNC-UCL.
DR GO; GO:0003777; F:microtubule motor activity; ISS:HGNC-UCL.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0010970; P:transport along microtubule; IBA:GO_Central.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:HGNC-UCL.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR025956; DYNC1I1/DYNC1I2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF11540; Dynein_IC2; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Centromere; Chromosome; Cytoplasm;
KW Cytoskeleton; Dynein; Kinetochore; Microtubule; Motor protein;
KW Phosphoprotein; Reference proteome; Repeat; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT CHAIN 2..628
FT /note="Cytoplasmic dynein 1 intermediate chain 1"
FT /id="PRO_0000114653"
FT REPEAT 268..317
FT /note="WD 1"
FT REPEAT 321..361
FT /note="WD 2"
FT REPEAT 370..411
FT /note="WD 3"
FT REPEAT 420..460
FT /note="WD 4"
FT REPEAT 465..510
FT /note="WD 5"
FT REPEAT 513..553
FT /note="WD 6"
FT REPEAT 559..598
FT /note="WD 7"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..146
FT /note="Interaction with DYNLT1"
FT /evidence="ECO:0000250|UniProtKB:O14576"
FT REGION 152..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62871"
FT MOD_RES 88
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 106..125
FT /note="Missing (in isoform 1B)"
FT /evidence="ECO:0000303|PubMed:10049579"
FT /id="VSP_001334"
FT MUTAGEN 151..155
FT /note="Missing: Abolishes interaction with DYNLL2."
FT /evidence="ECO:0000269|PubMed:11148209"
FT MUTAGEN 153
FT /note="T->A: Impairs interaction with DYNLL2."
FT MUTAGEN 153
FT /note="T->G: Abolishes interaction with DYNLL2."
FT MUTAGEN 154
FT /note="Q->A: Abolishes interaction with DYNLL2."
FT MUTAGEN 155
FT /note="T->G: Abolishes interaction with DYNLL2."
FT MUTAGEN 155
FT /note="T->S: Impairs interaction with DYNLL2."
FT CONFLICT 384
FT /note="Q -> H (in Ref. 1; AAC33444)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="H -> R (in Ref. 1; AAC33444)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="L -> V (in Ref. 1; AAC33444)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="F -> S (in Ref. 1; AAC33444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 70725 MW; 1DFD9264D63B2CE8 CRC64;
MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKEADMQ QKKEPVQDDS DLDRKRRETE
ALLQSIGISP EPPLVPTPMS PSSKSVSTPS DAGSQDSGDL GPLTRTLQWD TDPSVLQLQS
DSELGRRLHK LGVSKVTQVD FLPREVVSYS KETQTPLATH QSEEDEEDEE MVEPKIGHDS
ELENQEKKQE TKEAPPRELT EEEKQQILHS EEFLIFFDRT IRVIERALAE DSDIFFDYSG
RELEEKDGDV QAGANLSFNR QFYDEHWSKH RVVTCMDWSL QYPELMVASY SNNEDAPHEP
DGVALVWNMK FKKTTPEYVF HCQSSVMSVC FARFHPNLVV GGTYSGQIVL WDNRSHRRTP
VQRTPLSAAA HTHPVYCVNV VGTQNAHNLI TVSTDGKMCS WSLDMLSTPQ ESMELVYNKS
KPVAVTGMAF PTGDVNNFVV GSEEGTVYTA CRHGSKAGIG EVFEGHQGPV TGINCHMAVG
PIDFSHLFVT SSFDWTVKLW TTKHNKPLYS FEDNADYVYD VMWSPVHPAL FACVDGMGRL
DLWNLNSDTE VPTASVAIEG ASALNRVRWA QGGKEVAVGD SEGRIWIYDV GELAVPHNDE
WTRFARTLVE IRANRADSEE EGAVELAA
