DC1I2_RAT
ID DC1I2_RAT Reviewed; 638 AA.
AC Q62871; Q62872; Q62873;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 2;
DE AltName: Full=Cytoplasmic dynein intermediate chain 2;
DE AltName: Full=Dynein intermediate chain 2, cytosolic;
DE Short=DH IC-2;
GN Name=Dync1i2; Synonyms=Dnci2, Dncic2;
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] (ISOFORMS 2A; 2B AND 2C), AND INTERACTION WITH
RP 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 [2]
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 [3]
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 [4]
RP INTERACTION WITH DYNC1H1.
RX PubMed=10893223; DOI=10.1074/jbc.m001537200;
RA Tynan S.H., Gee M.A., Vallee R.B.;
RT "Distinct but overlapping sites within the cytoplasmic dynein heavy chain
RT for dimerization and for intermediate chain and light intermediate chain
RT binding.";
RL J. Biol. Chem. 275:32769-32774(2000).
RN [5]
RP FUNCTION, PHOSPHORYLATION AT SER-90, SUBCELLULAR LOCATION, INTERACTION WITH
RP DCTN1, MUTAGENESIS OF SER-90, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11340075; DOI=10.1074/jbc.m102649200;
RA Vaughan P.S., Leszyk J.D., Vaughan K.T.;
RT "Cytoplasmic dynein intermediate chain phosphorylation regulates binding to
RT dynactin.";
RL J. Biol. Chem. 276:26171-26179(2001).
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, 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-51 AND SER-104, AND
RP 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).
RN [9]
RP INTERACTION WITH DYNLT1.
RX PubMed=27502274; DOI=10.1074/jbc.m116.736884;
RA Merino-Gracia J., Zamora-Carreras H., Bruix M., Rodriguez-Crespo I.;
RT "Molecular basis for the protein recognition specificity of the dynein
RT light chain DYNLT1/Tctex1: characterization of the interaction with activin
RT receptor IIB.";
RL J. Biol. Chem. 291:20962-20975(2016).
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 (PubMed:11340075). Cytoplasmic dynein 1 acts as a motor for
CC the intracellular retrograde motility of vesicles and organelles along
CC microtubules (PubMed:11340075). The intermediate chains mediate the
CC binding of dynein to dynactin via its 150 kDa component (p150-glued)
CC DCTN1 (PubMed:11340075). Involved in membrane-transport, such as Golgi
CC apparatus, late endosomes and lysosomes (PubMed:11340075).
CC {ECO:0000269|PubMed:11340075}.
CC -!- SUBUNIT: Homodimer (PubMed:8688562, PubMed:9790665, PubMed:10893223,
CC PubMed:17279546). The cytoplasmic dynein 1 complex consists of two
CC catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC presented by intermediate chains (ICs), light intermediate chains
CC (LICs) and light chains (LCs); the composition seems to vary in respect
CC to the IC, LIC and LC composition (PubMed:8688562, PubMed:9790665,
CC PubMed:10893223, PubMed:17279546). The heavy chain homodimer serves as
CC a scaffold for the probable homodimeric assembly of the respective non-
CC catalytic subunits (PubMed:8688562, PubMed:9790665, PubMed:10893223,
CC PubMed:17279546). The ICs and LICs bind directly to the HC dimer and
CC the LCs assemble on the IC dimer (PubMed:8688562, PubMed:9790665,
CC PubMed:10893223, PubMed:17279546). Interacts with DYNLT3
CC (PubMed:17965411). Interacts with DYNLT1 (PubMed:17965411). Interacts
CC (dephosphorylated at Ser-90) with DCTN1 (PubMed:8522607,
CC PubMed:11340075). Interacts with BICD2 (By similarity). Interacts with
CC SPEF2 (By similarity). {ECO:0000250|UniProtKB:O88487,
CC ECO:0000269|PubMed:10893223, ECO:0000269|PubMed:11340075,
CC ECO:0000269|PubMed:17279546, ECO:0000269|PubMed:17965411,
CC ECO:0000269|PubMed:8522607, ECO:0000269|PubMed:8688562,
CC ECO:0000269|PubMed:9790665}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11340075}. Cytoplasm
CC {ECO:0000250|UniProtKB:O88487}. Note=Detected in the cytoplasm of
CC pachytene spermatocytes. Localizes to the manchette in elongating
CC spermatids. {ECO:0000250|UniProtKB:O88487}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=2A;
CC IsoId=Q62871-1; Sequence=Displayed;
CC Name=2B;
CC IsoId=Q62871-2; Sequence=VSP_001339;
CC Name=2C;
CC IsoId=Q62871-3; Sequence=VSP_001339, VSP_001340;
CC -!- TISSUE SPECIFICITY: Skeletal muscle, testis, kidney, brain, heart and
CC spleen.
CC -!- PTM: The phosphorylation status of Ser-90 appears to be involved in
CC dynactin-dependent target binding. {ECO:0000269|PubMed:11340075}.
CC -!- PTM: Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) promotes interaction with DCTN1. Serine pyrophosphorylation is
CC achieved by Mg(2+)-dependent, but enzyme independent transfer of a
CC beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated
CC serine residue. {ECO:0000250|UniProtKB:O88487}.
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; U39044; AAA89163.1; -; mRNA.
DR EMBL; U39045; AAA89164.1; -; mRNA.
DR EMBL; U39046; AAA89165.1; -; mRNA.
DR PDB; 2PG1; X-ray; 2.80 A; I/J/K/L=132-164.
DR PDBsum; 2PG1; -.
DR AlphaFoldDB; Q62871; -.
DR SMR; Q62871; -.
DR CORUM; Q62871; -.
DR DIP; DIP-36880N; -.
DR IntAct; Q62871; 4.
DR STRING; 10116.ENSRNOP00000060919; -.
DR iPTMnet; Q62871; -.
DR PhosphoSitePlus; Q62871; -.
DR jPOST; Q62871; -.
DR PaxDb; Q62871; -.
DR PeptideAtlas; Q62871; -.
DR PRIDE; Q62871; -.
DR UCSC; RGD:620174; rat. [Q62871-1]
DR RGD; 620174; Dync1i2.
DR eggNOG; KOG1587; Eukaryota.
DR InParanoid; Q62871; -.
DR PhylomeDB; Q62871; -.
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-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
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-8854518; AURKA Activation by TPX2.
DR Reactome; R-RNO-9646399; Aggrephagy.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR EvolutionaryTrace; Q62871; -.
DR PRO; PR:Q62871; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; ISO:RGD.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0036157; C:outer dynein arm; ISO:RGD.
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:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
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; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Dynein; Microtubule; Motor protein; Phosphoprotein; Reference proteome;
KW Repeat; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT CHAIN 2..638
FT /note="Cytoplasmic dynein 1 intermediate chain 2"
FT /id="PRO_0000114657"
FT REPEAT 277..326
FT /note="WD 1"
FT REPEAT 330..370
FT /note="WD 2"
FT REPEAT 379..420
FT /note="WD 3"
FT REPEAT 429..469
FT /note="WD 4"
FT REPEAT 474..519
FT /note="WD 5"
FT REPEAT 568..607
FT /note="WD 6"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..165
FT /note="Interaction with DYNLT1"
FT /evidence="ECO:0000269|PubMed:27502274"
FT REGION 154..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..209
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 51
FT /note="Diphosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88487"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11340075"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13409"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 77..82
FT /note="Missing (in isoform 2B and isoform 2C)"
FT /evidence="ECO:0000303|PubMed:8522607"
FT /id="VSP_001339"
FT VAR_SEQ 113..132
FT /note="Missing (in isoform 2C)"
FT /evidence="ECO:0000303|PubMed:8522607"
FT /id="VSP_001340"
FT MUTAGEN 90
FT /note="S->A: No effect on interaction with DCTN1 (mimicks
FT dephosphorylated form)."
FT /evidence="ECO:0000269|PubMed:11340075"
FT MUTAGEN 90
FT /note="S->D: Impairs interaction with DCTN1 (mimicks
FT phosphorylated form)."
FT /evidence="ECO:0000269|PubMed:11340075"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2PG1"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:2PG1"
SQ SEQUENCE 638 AA; 71178 MW; 0A655543CE266E95 CRC64;
MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAAVSVQEE SDLEKKRREA
EALLQSMGLT TDSPIVFSEH WVPPPMSPSS KSVSTPSEAG SQDSGDGAVG SRTLHWDTDP
SALQLHSDSD LGRGPIKLGM AKITQVDFPP REIVTYTKET QTPVTAQPKE DEEEEDDVAA
PKPPVEPEEE KILKKDEEND SKAPPHELTE EEKQQILHSE EFLSFFDHST RIVERALSEQ
INIFFDYSGR DLEDKEGEIQ AGAKLSLNRQ FFDERWSKHR VVSCLDWSSQ YPELLVASYN
NNEEAPHEPD GVALVWNMKY KKTTPEYVFH CQSAVMSATF AKFHPNLVVG GTYSGQIVLW
DNRSNKRTPV QRTPLSAAAH THPVYCVNVV GTQNAHNLIS ISTDGKICSW SLDMLSHPQD
SMELVHKQSK AVAVTSMSFP VGDVNNFVVG SEEGSVYTAC RHGSKAGISE MFEGHQGPIT
GIHCHAAVGA VDFSHLFVTS SFDWTVKLWS TKNNKPLYSF EDNSDYVYDV IGSPTHPALF
ACVDGMGRLD LWNLNNDTEV PTASISVEGN PALNRVRWTH SGREIAVGDS EGQIVIYDVG
EQIAVPRNDE WARFGRTLAE INASRADAEE EAATRIPA
