DC1I1_BOVIN
ID DC1I1_BOVIN Reviewed; 608 AA.
AC Q29RQ3;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
RX PubMed=11967380; DOI=10.1110/ps.2520102;
RA King S.J., Bonilla M., Rodgers M.E., Schroer T.A.;
RT "Subunit organization in cytoplasmic dynein subcomplexes.";
RL Protein Sci. 11:1239-1250(2002).
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 (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 Interacts with DYNC1H1. Interacts with DYNLT1 and DYNLT3. Interacts
CC with DCTN1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; BC114074; AAI14075.1; -; mRNA.
DR RefSeq; NP_001039981.1; NM_001046516.1.
DR RefSeq; XP_005205222.1; XM_005205165.3.
DR AlphaFoldDB; Q29RQ3; -.
DR SMR; Q29RQ3; -.
DR BioGRID; 541426; 2.
DR STRING; 9913.ENSBTAP00000020774; -.
DR PaxDb; Q29RQ3; -.
DR PRIDE; Q29RQ3; -.
DR Ensembl; ENSBTAT00000020774; ENSBTAP00000020774; ENSBTAG00000027134.
DR GeneID; 613724; -.
DR KEGG; bta:613724; -.
DR CTD; 1780; -.
DR VEuPathDB; HostDB:ENSBTAG00000027134; -.
DR VGNC; VGNC:28270; DYNC1I1.
DR eggNOG; KOG1587; Eukaryota.
DR GeneTree; ENSGT00940000156032; -.
DR HOGENOM; CLU_012999_1_1_1; -.
DR InParanoid; Q29RQ3; -.
DR OrthoDB; 1453532at2759; -.
DR TreeFam; TF300553; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000027134; Expressed in Ammon's horn and 83 other tissues.
DR ExpressionAtlas; Q29RQ3; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0010970; P:transport along microtubule; IBA:GO_Central.
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; Centromere; Chromosome; Cytoplasm; Cytoskeleton; Dynein;
KW Kinetochore; Microtubule; Motor protein; Phosphoprotein;
KW Reference proteome; Repeat; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT CHAIN 2..608
FT /note="Cytoplasmic dynein 1 intermediate chain 1"
FT /id="PRO_0000393960"
FT REPEAT 248..297
FT /note="WD 1"
FT REPEAT 301..341
FT /note="WD 2"
FT REPEAT 350..391
FT /note="WD 3"
FT REPEAT 400..440
FT /note="WD 4"
FT REPEAT 445..490
FT /note="WD 5"
FT REPEAT 493..533
FT /note="WD 6"
FT REPEAT 539..578
FT /note="WD 7"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..126
FT /note="Interaction with DYNLT1"
FT /evidence="ECO:0000250|UniProtKB:O14576"
FT REGION 132..184
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..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..184
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 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:0000250|UniProtKB:O88485"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88485"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14576"
SQ SEQUENCE 608 AA; 68556 MW; B387D03F55B5D998 CRC64;
MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKEADMQ QKKEPVPDDS DLDRKRRETE
ALLQSIGISP EPPLVPTPMS PSSKSVSTPS EAGSQDSGDL GPLTRRRLHK LGVSKITQVD
FLPREVVSYS KETQTPLATH QSEEDEDDEE MVEPKGDQDS EQENEDKKQE VKEAPPRELT
EEEKQQILHS EEFLIFFDRT IRVIERALAE DSDIFFDYSG RELEEKDGDV QAGANLSFNR
QFYDEHWSKH RVVTCMDWSL QYPELMVASY NNNEDAPHEP DGVALVWNMK FKKTTPEYVF
HCQSSVMSVC FARFHPNLVV GGTYSGQIVL WDNRSHRRTP VQRTPLSAAA HTHPVYCVNV
VGTQNAHNLI TVSTDGKMCS WSLDMLSTPQ ESMELVYNKS KPVAVTGMAF PTGDVNNFVV
GSEEGTVYTA CRHGSKAGIG EVFEGHQGPV TGINCHMAVG PIDFSHLFVT SSFDWTVKLW
TTKHNKPLYS FEDNADYVYD VMWSPVHPAL FACVDGMGRL DLWNLNNDTE VPTASVAIEG
ASALNRVRWA QGGKEVAVGD SEGRIWIYDV GELAVPHNDE WTRFARTLVE IRANRADSEE
EGAVELSA
