DC1I2_MOUSE
ID DC1I2_MOUSE Reviewed; 612 AA.
AC O88487; Q3TGH7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 173.
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 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].
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 MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Heart, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89; SER-91; SER-95 AND
RP SER-98, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [5]
RP INTERACTION WITH BICD2.
RX PubMed=22956769; DOI=10.1091/mbc.e12-03-0210;
RA Splinter D., Razafsky D.S., Schlager M.A., Serra-Marques A., Grigoriev I.,
RA Demmers J., Keijzer N., Jiang K., Poser I., Hyman A.A., Hoogenraad C.C.,
RA King S.J., Akhmanova A.;
RT "BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to
RT cellular structures.";
RL Mol. Biol. Cell 23:4226-4241(2012).
RN [6]
RP FUNCTION, INTERACTION WITH DCTN1, PHOSPHORYLATION AT SER-51
RP PYROPHOSPHORYLATION AT SER-51, AND MUTAGENESIS OF SER-51.
RX PubMed=27474409; DOI=10.1042/bcj20160610;
RA Chanduri M., Rai A., Malla A.B., Wu M., Fiedler D., Mallik R., Bhandari R.;
RT "Inositol hexakisphosphate kinase 1 (IP6K1) activity is required for
RT cytoplasmic dynein-driven transport.";
RL Biochem. J. 473:3031-3047(2016).
RN [7]
RP INTERACTION WITH SPEF2, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=28619825; DOI=10.1242/dev.152108;
RA Lehti M.S., Zhang F.P., Kotaja N., Sironen A.;
RT "SPEF2 functions in microtubule-mediated transport in elongating spermatids
RT to ensure proper male germ cell differentiation.";
RL Development 144:2683-2693(2017).
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 (By similarity). Cytoplasmic dynein 1 acts as a motor for the
CC intracellular retrograde motility of vesicles and organelles along
CC microtubules (By similarity). The intermediate chains mediate the
CC binding of dynein to dynactin via its 150 kDa component (p150-glued)
CC DCTN1 (PubMed:27474409). Involved in membrane-transport, such as Golgi
CC apparatus, late endosomes and lysosomes (PubMed:27474409).
CC {ECO:0000250|UniProtKB:Q62871, ECO:0000269|PubMed:27474409}.
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 (By
CC similarity). The heavy chain homodimer serves as a scaffold for the
CC probable homodimeric assembly of the respective non-catalytic subunits
CC (By similarity). The ICs and LICs bind directly to the HC dimer and the
CC LCs assemble on the IC dimer (By similarity). Interacts with DYNLT3 (By
CC similarity). Interacts with DYNLT1 (By similarity). Interacts
CC (dephosphorylated at Ser-84) with DCTN1 (PubMed:27474409). Interacts
CC with BICD2 (PubMed:22956769). Interacts with SPEF2 (PubMed:28619825).
CC {ECO:0000250|UniProtKB:Q62871, ECO:0000269|PubMed:22956769,
CC ECO:0000269|PubMed:27474409, ECO:0000269|PubMed:28619825}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:28619825}. Cytoplasm {ECO:0000269|PubMed:28619825}.
CC Note=Detected in the cytoplasm of pachytene spermatocytes. Localizes to
CC the manchette in elongating spermatids. {ECO:0000269|PubMed:28619825}.
CC -!- PTM: The phosphorylation status of Ser-84 appears to be involved in
CC dynactin-dependent target binding. {ECO:0000250|UniProtKB:Q62871}.
CC -!- PTM: Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) promotes interaction with DCTN1 (PubMed:27474409). Serine
CC pyrophosphorylation is achieved by Mg(2+)-dependent, but enzyme
CC independent transfer of a beta-phosphate from a inositol pyrophosphate
CC to a pre-phosphorylated serine residue (PubMed:27474409).
CC {ECO:0000269|PubMed:27474409}.
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF063231; AAC33446.1; -; mRNA.
DR EMBL; AK088015; BAC40097.1; -; mRNA.
DR EMBL; AK164437; BAE37788.1; -; mRNA.
DR EMBL; AK168730; BAE40571.1; -; mRNA.
DR CCDS; CCDS16112.1; -.
DR RefSeq; NP_001185805.1; NM_001198876.1.
DR RefSeq; NP_001185806.1; NM_001198877.1.
DR RefSeq; NP_001185807.1; NM_001198878.1.
DR RefSeq; NP_034194.1; NM_010064.4.
DR AlphaFoldDB; O88487; -.
DR SMR; O88487; -.
DR BioGRID; 199256; 33.
DR ComplexPortal; CPX-5699; Cytoplasmic dynein complex, variant 1.
DR IntAct; O88487; 10.
DR STRING; 10090.ENSMUSP00000080410; -.
DR iPTMnet; O88487; -.
DR PhosphoSitePlus; O88487; -.
DR REPRODUCTION-2DPAGE; O88487; -.
DR EPD; O88487; -.
DR jPOST; O88487; -.
DR MaxQB; O88487; -.
DR PaxDb; O88487; -.
DR PRIDE; O88487; -.
DR ProteomicsDB; 279829; -.
DR Antibodypedia; 33847; 150 antibodies from 30 providers.
DR DNASU; 13427; -.
DR Ensembl; ENSMUST00000081710; ENSMUSP00000080410; ENSMUSG00000027012.
DR Ensembl; ENSMUST00000112138; ENSMUSP00000107766; ENSMUSG00000027012.
DR GeneID; 13427; -.
DR KEGG; mmu:13427; -.
DR UCSC; uc008kai.2; mouse.
DR CTD; 1781; -.
DR MGI; MGI:107750; Dync1i2.
DR VEuPathDB; HostDB:ENSMUSG00000027012; -.
DR eggNOG; KOG1587; Eukaryota.
DR GeneTree; ENSGT00940000155442; -.
DR InParanoid; O88487; -.
DR OMA; EEGSIYP; -.
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-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
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-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 13427; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Dync1i2; mouse.
DR PRO; PR:O88487; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O88487; protein.
DR Bgee; ENSMUSG00000027012; Expressed in cortical plate and 285 other tissues.
DR ExpressionAtlas; O88487; baseline and differential.
DR Genevisible; O88487; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0036157; C:outer dynein arm; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
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; Cytoplasm; Cytoskeleton; Dynein; 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..612
FT /note="Cytoplasmic dynein 1 intermediate chain 2"
FT /id="PRO_0000114656"
FT REPEAT 251..300
FT /note="WD 1"
FT REPEAT 304..344
FT /note="WD 2"
FT REPEAT 353..394
FT /note="WD 3"
FT REPEAT 403..443
FT /note="WD 4"
FT REPEAT 448..493
FT /note="WD 5"
FT REPEAT 496..536
FT /note="WD 6"
FT REPEAT 542..581
FT /note="WD 7"
FT REGION 1..188
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 154..188
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:0000269|PubMed:27474409"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27474409"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62871"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 51
FT /note="S->A: Abolished both phosphorylation and
FT pyrophosphorylation."
FT /evidence="ECO:0000269|PubMed:27474409"
SQ SEQUENCE 612 AA; 68394 MW; 1D14CEECF62A5E33 CRC64;
MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAAVSVQEE SDLEKKRREA
EALLQSMGLT TDSPIVPPPM SPSSKSVSTP SEAGSQDSGD GAVGSRRGPI KLGMAKITQV
DFPPREIVTY TKETQTPVTA QPKEDEEEED DVATPKPPVE PEEEKTLKKD EENDSKAPPH
ELTEEEKQQI LHSEEFLSFF DHSTRIVERA LSEQINIFFD YSGRDLEDKE GEIQAGAKLS
LNRQFFDERW SKHRVVSCLD WSSQYPELLV ASYNNNEEAP HEPDGVALVW NMKYKKTTPE
YVFHCQSAVM SATFAKFHPN LVVGGTYSGQ IVLWDNRSNK RTPVQRTPLS AAAHTHPVYC
VNVVGTQNAH NLISISTDGK ICSWSLDMLS HPQDSMELVH KQSKAVAVTS MSFPVGDVNN
FVVGSEEGSV YTACRHGSKA GISEMFEGHQ GPITGIHCHA AVGAVDFSHL FVTSSFDWTV
KLWTTKNNKP LYSFEDNSDY VYDVMWSPTH PALFACVDGM GRLDLWNLNN DTEVPTASIS
VEGNPALNRV RWTHSGREIA VGDSEGQIVI YDVGEQIAVP RNDEWARFGR TLAEINANRA
DAEEEAATRI PA
