DC1I1_RAT
ID DC1I1_RAT Reviewed; 643 AA.
AC Q63100;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 155.
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 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] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=1387402; DOI=10.1083/jcb.118.5.1133;
RA Paschal B.M., Mikami A., Pfister K.K., Vallee R.B.;
RT "Homology of the 74-kD cytoplasmic dynein subunit with a flagellar dynein
RT polypeptide suggests an intracellular targeting function.";
RL J. Cell Biol. 118:1133-1143(1992).
RN [2]
RP INTERACTION WITH DCTN1.
RX PubMed=7499404; DOI=10.1074/jbc.270.48.28806;
RA Karki S., Holzbaur E.L.;
RT "Affinity chromatography demonstrates a direct binding between cytoplasmic
RT dynein and the dynactin complex.";
RL J. Biol. Chem. 270:28806-28811(1995).
RN [3]
RP INTERACTION WITH DCTN1.
RX PubMed=8522607; DOI=10.1083/jcb.131.6.1507;
RA Vaughan K.T., Vallee R.B.;
RT "Cytoplasmic dynein binds dynactin through a direct interaction between the
RT intermediate chains and p150Glued.";
RL J. Cell Biol. 131:1507-1516(1995).
RN [4]
RP IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
RX PubMed=8688562; DOI=10.1091/mbc.7.2.331;
RA Pfister K.K., Salata M.W., Dillman J.F. III, Torre E., Lye R.J.;
RT "Identification and developmental regulation of a neuron-specific subunit
RT of cytoplasmic dynein.";
RL Mol. Biol. Cell 7:331-343(1996).
RN [5]
RP IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
RX PubMed=9790665; DOI=10.1021/bi9810813;
RA King S.M., Barbarese E., Dillman J.F. III, Benashski S.E., Do K.T.,
RA Patel-King R.S., Pfister K.K.;
RT "Cytoplasmic dynein contains a family of differentially expressed light
RT chains.";
RL Biochemistry 37:15033-15041(1998).
RN [6]
RP INTERACTION WITH DYNLT1 AND DYNLT3.
RX PubMed=17965411; DOI=10.1074/jbc.m705991200;
RA Lo K.W., Kogoy J.M., Rasoul B.A., King S.M., Pfister K.K.;
RT "Interaction of the DYNLT (TCTEX1/RP3) light chains and the intermediate
RT chains reveals novel intersubunit regulation during assembly of the dynein
RT complex.";
RL J. Biol. Chem. 282:36871-36878(2007).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), AND INTERACTION WITH DYNC1H1.
RX PubMed=17279546; DOI=10.1002/jnr.21213;
RA Myers K.R., Lo K.W., Lye R.J., Kogoy J.M., Soura V., Hafezparast M.,
RA Pfister K.K.;
RT "Intermediate chain subunit as a probe for cytoplasmic dynein function:
RT biochemical analyses and live cell imaging in PC12 cells.";
RL J. Neurosci. Res. 85:2640-2647(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-177; SER-195 AND
RP SER-633, AND IDENTIFICATION BY 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. 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 Isoform 1, isoform 2 and isoform 3 interact with DYNC1H1. Isoform 1,
CC isoform 2 and isoform 3 interact with DYNLT3. Isoform 1, isoform 2 and
CC isoform 3 interact with DYNLT1. Interacts with DCTN1. {ECO:0000250,
CC ECO:0000269|PubMed:17279546, ECO:0000269|PubMed:17965411,
CC ECO:0000269|PubMed:7499404, ECO:0000269|PubMed:8522607,
CC ECO:0000269|PubMed:8688562, ECO:0000269|PubMed:9790665}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=1A;
CC IsoId=Q63100-1; Sequence=Displayed;
CC Name=2; Synonyms=1B;
CC IsoId=Q63100-3; Sequence=VSP_039087;
CC Name=3; Synonyms=1C;
CC IsoId=Q63100-4; Sequence=VSP_039087, VSP_039088;
CC -!- TISSUE SPECIFICITY: High levels seen in the brain and testis, while a
CC lower level expression is seen in the liver, spleen, kidney, lung,
CC skeletal muscle and heart.
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; X66845; CAA47321.1; -; mRNA.
DR PIR; A43423; A43423.
DR RefSeq; NP_062107.1; NM_019234.1. [Q63100-1]
DR AlphaFoldDB; Q63100; -.
DR SMR; Q63100; -.
DR BioGRID; 248198; 6.
DR CORUM; Q63100; -.
DR IntAct; Q63100; 1.
DR MINT; Q63100; -.
DR STRING; 10116.ENSRNOP00000013184; -.
DR iPTMnet; Q63100; -.
DR PhosphoSitePlus; Q63100; -.
DR SwissPalm; Q63100; -.
DR PaxDb; Q63100; -.
DR PRIDE; Q63100; -.
DR GeneID; 29564; -.
DR KEGG; rno:29564; -.
DR UCSC; RGD:2512; rat. [Q63100-1]
DR CTD; 1780; -.
DR RGD; 2512; Dync1i1.
DR eggNOG; KOG1587; Eukaryota.
DR InParanoid; Q63100; -.
DR OrthoDB; 1453532at2759; -.
DR PhylomeDB; Q63100; -.
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:Q63100; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1904115; C:axon cytoplasm; IDA:SynGO-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:RGD.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:HGNC-UCL.
DR GO; GO:0003777; F:microtubule motor activity; IDA:HGNC-UCL.
DR GO; GO:0030507; F:spectrin binding; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
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; IDA: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..643
FT /note="Cytoplasmic dynein 1 intermediate chain 1"
FT /id="PRO_0000114654"
FT REPEAT 283..332
FT /note="WD 1"
FT REPEAT 336..376
FT /note="WD 2"
FT REPEAT 385..426
FT /note="WD 3"
FT REPEAT 435..475
FT /note="WD 4"
FT REPEAT 480..525
FT /note="WD 5"
FT REPEAT 528..568
FT /note="WD 6"
FT REPEAT 574..613
FT /note="WD 7"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..123
FT /note="Interaction with DCTN1"
FT REGION 96..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..161
FT /note="Interaction with DYNLT1"
FT /evidence="ECO:0000250|UniProtKB:O14576"
FT REGION 167..219
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 188..219
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:0000250|UniProtKB:O88485"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62871"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 75..90
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039087"
FT VAR_SEQ 121..141
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039088"
SQ SEQUENCE 643 AA; 72754 MW; BD126092A6633402 CRC64;
MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKEADMQ QKKEPVPDDS DLDRKRRETE
ALLQSIGISP EPPLVQPLHF LTWDTCYFHY LVPTPMSPSS KSVSTPSEAG SQDDLGPLTR
TLQWDTDPSV LQLQSDSELG RRLNKLGVSK VTQVDFLPRE VVSYSKETQT PLATHQSEED
EEDEEMVEPK VGHDSELENQ DKKQETKEAP PRELTEEEKQ QILHSEEFLI FFDRTIRVIE
RALAEDSDIF FDYSGRELEE KDGDVQAGAN LSFNRQFYDE HWSKHRVVTC MDWSLQYPEL
MVASYSNNED APHEPDGVAL VWNMKFKKTT PEYVFHCQSS VMSVCFARFH PNLVVGGTYS
GQIVLWDNRS HRRTPVQRTP LSAAAHTHPV YCVNVVGTQN AHNLITVSTD GKMCSWSLDM
LSTPQESMEL VYNKSKPVAV TGMAFPTGDV NNFVVGSEEG TVYTACRHGS KAGIGEVFEG
HQGPVTGINC HMAVGPIDFS HLFVTSSFDW TVKLWTTKHN KPLYSFEDNA DYVYDVMWSP
VHPALFACVD GMGRLDLWNL NSDTEVPTAS VAIEGAYALN RVRWAQGGKE VAVGDSEGRI
WIYDVGELAV PHNDEWTRFA RTLVEIRANR ADSEEEGAVE LAA
