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Cytoplasmic dynein 1 intermediate chain 1 (Cytoplasmic dynein intermediate chain 1) (Dynein intermediate chain 1, cytosolic) (DH IC-1)

 DC1I1_RAT               Reviewed;         643 AA.
Q63100;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
20-JUN-2018, entry version 136.
RecName: Full=Cytoplasmic dynein 1 intermediate chain 1;
AltName: Full=Cytoplasmic dynein intermediate chain 1;
AltName: Full=Dynein intermediate chain 1, cytosolic;
Short=DH IC-1;
Name=Dync1i1; Synonyms=Dnci1, Dncic1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=1387402; DOI=10.1083/jcb.118.5.1133;
Paschal B.M., Mikami A., Pfister K.K., Vallee R.B.;
"Homology of the 74-kD cytoplasmic dynein subunit with a flagellar
dynein polypeptide suggests an intracellular targeting function.";
J. Cell Biol. 118:1133-1143(1992).
[2]
INTERACTION WITH DCTN1.
PubMed=7499404; DOI=10.1074/jbc.270.48.28806;
Karki S., Holzbaur E.L.;
"Affinity chromatography demonstrates a direct binding between
cytoplasmic dynein and the dynactin complex.";
J. Biol. Chem. 270:28806-28811(1995).
[3]
INTERACTION WITH DCTN1.
PubMed=8522607; DOI=10.1083/jcb.131.6.1507;
Vaughan K.T., Vallee R.B.;
"Cytoplasmic dynein binds dynactin through a direct interaction
between the intermediate chains and p150Glued.";
J. Cell Biol. 131:1507-1516(1995).
[4]
IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
PubMed=8688562; DOI=10.1091/mbc.7.2.331;
Pfister K.K., Salata M.W., Dillman J.F. III, Torre E., Lye R.J.;
"Identification and developmental regulation of a neuron-specific
subunit of cytoplasmic dynein.";
Mol. Biol. Cell 7:331-343(1996).
[5]
IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
PubMed=9790665; DOI=10.1021/bi9810813;
King S.M., Barbarese E., Dillman J.F. III, Benashski S.E., Do K.T.,
Patel-King R.S., Pfister K.K.;
"Cytoplasmic dynein contains a family of differentially expressed
light chains.";
Biochemistry 37:15033-15041(1998).
[6]
INTERACTION WITH DYNLT1 AND DYNLT3.
PubMed=17965411; DOI=10.1074/jbc.M705991200;
Lo K.W., Kogoy J.M., Rasoul B.A., King S.M., Pfister K.K.;
"Interaction of the DYNLT (TCTEX1/RP3) light chains and the
intermediate chains reveals novel intersubunit regulation during
assembly of the dynein complex.";
J. Biol. Chem. 282:36871-36878(2007).
[7]
ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), AND INTERACTION WITH DYNC1H1.
PubMed=17279546; DOI=10.1002/jnr.21213;
Myers K.R., Lo K.W., Lye R.J., Kogoy J.M., Soura V., Hafezparast M.,
Pfister K.K.;
"Intermediate chain subunit as a probe for cytoplasmic dynein
function: biochemical analyses and live cell imaging in PC12 cells.";
J. Neurosci. Res. 85:2640-2647(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-177; SER-195
AND SER-633, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Acts as one of several non-catalytic accessory
components of the cytoplasmic dynein 1 complex that are thought to
be involved in linking dynein to cargos and to adapter proteins
that regulate dynein function. Cytoplasmic dynein 1 acts as a
motor for the intracellular retrograde motility of vesicles and
organelles along microtubules. The intermediate chains mediate the
binding of dynein to dynactin via its 150 kDa component (p150-
glued) DCNT1. May play a role in mediating the interaction of
cytoplasmic dynein with membranous organelles and kinetochores.
-!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1
complex consists of two catalytic heavy chains (HCs) and a number
of non-catalytic subunits presented by intermediate chains (ICs),
light intermediate chains (LICs) and light chains (LCs); the
composition seems to vary in respect to the IC, LIC and LC
composition. The heavy chain homodimer serves as a scaffold for
the probable homodimeric assembly of the respective non-catalytic
subunits. The ICs and LICs bind directly to the HC dimer and the
LCs assemble on the IC dimer. Isoform 1, isoform 2 and isoform 3
interact with DYNC1H1. Isoform 1, isoform 2 and isoform 3 interact
with DYNLT3. Isoform 1, isoform 2 and isoform 3 interact with
DYNLT1. Interacts with DCTN1. {ECO:0000250,
ECO:0000269|PubMed:17279546, ECO:0000269|PubMed:17965411,
ECO:0000269|PubMed:7499404, ECO:0000269|PubMed:8522607,
ECO:0000269|PubMed:8688562, ECO:0000269|PubMed:9790665}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome,
centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton,
spindle pole {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=1A;
IsoId=Q63100-1; Sequence=Displayed;
Name=2; Synonyms=1B;
IsoId=Q63100-3; Sequence=VSP_039087;
Name=3; Synonyms=1C;
IsoId=Q63100-4; Sequence=VSP_039087, VSP_039088;
-!- TISSUE SPECIFICITY: High levels seen in the brain and testis,
while a lower level expression is seen in the liver, spleen,
kidney, lung, skeletal muscle and heart.
-!- SIMILARITY: Belongs to the dynein intermediate chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X66845; CAA47321.1; -; mRNA.
PIR; A43423; A43423.
RefSeq; NP_062107.1; NM_019234.1. [Q63100-1]
UniGene; Rn.11273; -.
ProteinModelPortal; Q63100; -.
BioGrid; 248198; 6.
CORUM; Q63100; -.
IntAct; Q63100; 1.
MINT; Q63100; -.
STRING; 10116.ENSRNOP00000013184; -.
iPTMnet; Q63100; -.
PhosphoSitePlus; Q63100; -.
SwissPalm; Q63100; -.
PaxDb; Q63100; -.
PRIDE; Q63100; -.
GeneID; 29564; -.
KEGG; rno:29564; -.
UCSC; RGD:2512; rat. [Q63100-1]
CTD; 1780; -.
RGD; 2512; Dync1i1.
eggNOG; KOG1587; Eukaryota.
eggNOG; ENOG410XQ99; LUCA.
HOGENOM; HOG000116383; -.
HOVERGEN; HBG004083; -.
InParanoid; Q63100; -.
KO; K10415; -.
PhylomeDB; Q63100; -.
PRO; PR:Q63100; -.
Proteomes; UP000002494; Unplaced.
GO; GO:1904115; C:axon cytoplasm; IDA:SynGO-UCL.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005868; C:cytoplasmic dynein complex; IDA:RGD.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC.
GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
GO; GO:0031982; C:vesicle; ISS:UniProtKB.
GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
GO; GO:0045503; F:dynein light chain binding; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; IDA:HGNC.
GO; GO:0003777; F:microtubule motor activity; IDA:HGNC.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:2000582; P:positive regulation of ATP-dependent microtubule motor activity, plus-end-directed; IBA:GO_Central.
GO; GO:0047496; P:vesicle transport along microtubule; IDA:HGNC.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR025956; DYNC1I1/DYNC1I2.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF11540; Dynein_IC2; 1.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Centromere; Chromosome;
Complete proteome; Cytoplasm; Cytoskeleton; Dynein; Kinetochore;
Microtubule; Motor protein; Phosphoprotein; Reference proteome;
Repeat; Transport; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q13409}.
CHAIN 2 643 Cytoplasmic dynein 1 intermediate chain
1.
/FTId=PRO_0000114654.
REPEAT 283 332 WD 1.
REPEAT 336 376 WD 2.
REPEAT 385 426 WD 3.
REPEAT 435 475 WD 4.
REPEAT 480 525 WD 5.
REPEAT 528 568 WD 6.
REPEAT 574 613 WD 7.
REGION 2 123 Interaction with DCTN1.
REGION 145 161 Interaction with DYNLT1.
{ECO:0000250|UniProtKB:O14576}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q13409}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:O88485}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:Q62871}.
MOD_RES 105 105 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13409}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000250|UniProtKB:Q13409}.
MOD_RES 111 111 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 174 174 Phosphothreonine.
{ECO:0000250|UniProtKB:O88485}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 75 90 Missing (in isoform 2 and isoform 3).
{ECO:0000305}.
/FTId=VSP_039087.
VAR_SEQ 121 141 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_039088.
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


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