DCTN1_MOUSE
ID DCTN1_MOUSE Reviewed; 1281 AA.
AC O08788; E9QLJ1; Q3TZG7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Dynactin subunit 1;
DE AltName: Full=150 kDa dynein-associated polypeptide;
DE AltName: Full=DAP-150;
DE Short=DP-150;
DE AltName: Full=p150-glued;
GN Name=Dctn1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=9070275; DOI=10.1006/bbrc.1997.6095;
RA Jang W., Weber J.S., Tokito M.K., Holzbaur E.L., Meisler M.H.;
RT "Mouse p150Glued (dynactin 1) cDNA sequence and evaluation as a candidate
RT for the neuromuscular disease mutation mnd2.";
RL Biochem. Biophys. Res. Commun. 231:344-347(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP INTERACTION WITH DST (ISOFORM 1).
RX PubMed=14581450; DOI=10.1083/jcb.200306075;
RA Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D., Wu C.,
RA Mobley W., Fuchs E., Yang Y.;
RT "BPAG1n4 is essential for retrograde axonal transport in sensory neurons.";
RL J. Cell Biol. 163:223-229(2003).
RN [5]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH MICROTUBULES.
RX PubMed=16954346; DOI=10.1083/jcb.200512058;
RA Peris L., Thery M., Faure J., Saoudi Y., Lafanechere L., Chilton J.K.,
RA Gordon-Weeks P., Galjart N., Bornens M., Wordeman L., Wehland J.,
RA Andrieux A., Job D.;
RT "Tubulin tyrosination is a major factor affecting the recruitment of CAP-
RT Gly proteins at microtubule plus ends.";
RL J. Cell Biol. 174:839-849(2006).
RN [6]
RP INTERACTION WITH SNX6.
RX PubMed=19935774; DOI=10.1038/cr.2009.130;
RA Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.;
RT "The retromer component SNX6 interacts with dynactin p150(Glued) and
RT mediates endosome-to-TGN transport.";
RL Cell Res. 19:1334-1349(2009).
RN [7]
RP 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 [8]
RP IDENTIFICATION IN A COMPLEX WITH MREG AND RILP.
RX PubMed=22275436; DOI=10.1242/jcs.094185;
RA Ohbayashi N., Maruta Y., Ishida M., Fukuda M.;
RT "Melanoregulin regulates retrograde melanosome transport through
RT interaction with the RILP-p150Glued complex in melanocytes.";
RL J. Cell Sci. 125:1508-1518(2012).
RN [9]
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 [10]
RP INTERACTION WITH KIF3A, AND SUBCELLULAR LOCATION.
RX PubMed=23386061; DOI=10.1038/emboj.2013.3;
RA Kodani A., Salome Sirerol-Piquer M., Seol A., Garcia-Verdugo J.M.,
RA Reiter J.F.;
RT "Kif3a interacts with Dynactin subunit p150 Glued to organize centriole
RT subdistal appendages.";
RL EMBO J. 32:597-607(2013).
RN [11]
RP INTERACTION WITH HPS6.
RX PubMed=25189619; DOI=10.1242/jcs.141978;
RA Li K., Yang L., Zhang C., Niu Y., Li W., Liu J.J.;
RT "HPS6 interacts with dynactin p150Glued to mediate retrograde trafficking
RT and maturation of lysosomes.";
RL J. Cell Sci. 127:4574-4588(2014).
RN [12]
RP INTERACTION WITH DYNC1I2.
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 [13]
RP INTERACTION WITH AKNA.
RX PubMed=30787442; DOI=10.1038/s41586-019-0962-4;
RA Camargo Ortega G., Falk S., Johansson P.A., Peyre E., Broix L., Sahu S.K.,
RA Hirst W., Schlichthaerle T., De Juan Romero C., Draganova K., Vinopal S.,
RA Chinnappa K., Gavranovic A., Karakaya T., Steininger T., Merl-Pham J.,
RA Feederle R., Shao W., Shi S.H., Hauck S.M., Jungmann R., Bradke F.,
RA Borrell V., Geerlof A., Reber S., Tiwari V.K., Huttner W.B.,
RA Wilsch-Braeuninger M., Nguyen L., Goetz M.;
RT "The centrosome protein AKNA regulates neurogenesis via microtubule
RT organization.";
RL Nature 567:113-117(2019).
CC -!- FUNCTION: Plays a key role in dynein-mediated retrograde transport of
CC vesicles and organelles along microtubules by recruiting and tethering
CC dynein to microtubules. Binds to both dynein and microtubules providing
CC a link between specific cargos, microtubules and dynein. Essential for
CC targeting dynein to microtubule plus ends, recruiting dynein to
CC membranous cargos and enhancing dynein processivity (the ability to
CC move along a microtubule for a long distance without falling off the
CC track). Can also act as a brake to slow the dynein motor during
CC motility along the microtubule. Can regulate microtubule stability by
CC promoting microtubule formation, nucleation and polymerization and by
CC inhibiting microtubule catastrophe in neurons. Inhibits microtubule
CC catastrophe by binding both to microtubules and to tubulin, leading to
CC enhanced microtubule stability along the axon. Plays a role in
CC metaphase spindle orientation. Plays a role in centriole cohesion and
CC subdistal appendage organization and function. Its recruitment to the
CC centriole in a KIF3A-dependent manner is essential for the maintenance
CC of centriole cohesion and the formation of subdistal appendage. Also
CC required for microtubule anchoring at the mother centriole. Plays a
CC role in primary cilia formation. {ECO:0000250|UniProtKB:Q14203}.
CC -!- SUBUNIT: Monomer and homodimer. Dynactin is a large macromolecular
CC complex of at least 10 components; p150(glued) binds directly to
CC microtubules and to cytoplasmic dynein. Interacts with the C-terminus
CC of MAPRE1, MAPRE2 and MAPRE3. Interacts with FBXL5. Interacts with
CC ECPAS. Interacts with CLIP1. Interacts with CLN3 and DYNAP. Interacts
CC with MISP; this interaction regulates its distribution at the cell
CC cortex. Interacts with CEP131. Interacts with CEP126. Interacts with
CC dynein intermediate chain and dynein heavy chain. Interacts with PLK1
CC (via POLO-box domain). Interacts with TBCB and PARD6A (By similarity).
CC Binds preferentially to tyrosinated microtubules than to detyrosinated
CC microtubules (PubMed:16954346). Interacts with KIF3A (PubMed:23386061).
CC Interacts with HPS6 (PubMed:25189619). Interacts with SNX6
CC (PubMed:19935774). Interacts with BICD2 (PubMed:22956769). Interacts
CC with DST (isoform 1) (PubMed:14581450). Identified in a complex with
CC MREG and RILP (PubMed:22275436). Interacts with BCCIP. Interacts with
CC DCDC1 (By similarity). Interacts with AKNA (PubMed:30787442). Interacts
CC with DYNC1I2 (PubMed:27474409). {ECO:0000250|UniProtKB:Q14203,
CC ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:16954346,
CC ECO:0000269|PubMed:19935774, ECO:0000269|PubMed:22275436,
CC ECO:0000269|PubMed:22956769, ECO:0000269|PubMed:23386061,
CC ECO:0000269|PubMed:25189619, ECO:0000269|PubMed:27474409,
CC ECO:0000269|PubMed:30787442}.
CC -!- INTERACTION:
CC O08788; Q6A078: Cep290; NbExp=2; IntAct=EBI-776180, EBI-1811999;
CC O08788; P28741: Kif3a; NbExp=4; IntAct=EBI-776180, EBI-6169413;
CC O08788; P33175: Kif5a; NbExp=2; IntAct=EBI-776180, EBI-349710;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14203}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14203}.
CC Nucleus envelope {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus
CC ends. Localizes preferentially to the ends of tyrosinated microtubules
CC (PubMed:16954346). Localization at centrosome is regulated by SLK-
CC dependent phosphorylation. Localizes to centrosome in a PARKDA-
CC dependent manner. PLK1-mediated phosphorylation at Ser-179 is essential
CC for its localization in the nuclear envelope (By similarity). Localizes
CC to the subdistal appendage region of the centriole in a KIF3A-dependent
CC manner (PubMed:23386061). {ECO:0000250|UniProtKB:Q14203,
CC ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:23386061}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O08788-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O08788-2; Sequence=VSP_029584;
CC -!- DOMAIN: The CAP-Gly domain is essential for interactions with
CC microtubules and its binding partners and for its motion along the
CC microtubules. Essential for its preferential binding to tyrosinated
CC microtubules and for promoting the sustained interaction of the dynein
CC motor with microtubules. {ECO:0000250|UniProtKB:Q14203}.
CC -!- PTM: Ubiquitinated by a SCF complex containing FBXL5, leading to its
CC degradation by the proteasome. {ECO:0000250|UniProtKB:Q14203}.
CC -!- PTM: Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147 targets
CC DCTN1 to the centrosome. It is uncertain if SLK phosphorylates all
CC three threonines or one or two of them. PLK1-mediated phosphorylation
CC at Ser-179 is essential for its localization in the nuclear envelope
CC and promotes its dissociation from microtubules during early mitosis
CC and positively regulates nuclear envelope breakdown during prophase.
CC {ECO:0000250|UniProtKB:Q14203}.
CC -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; U60312; AAB57773.1; -; mRNA.
DR EMBL; AK157867; BAE34241.1; -; mRNA.
DR EMBL; AC160400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS39532.1; -. [O08788-1]
DR PIR; JC5368; JC5368.
DR RefSeq; NP_031861.2; NM_007835.2. [O08788-1]
DR AlphaFoldDB; O08788; -.
DR BMRB; O08788; -.
DR SMR; O08788; -.
DR BioGRID; 199072; 70.
DR CORUM; O08788; -.
DR DIP; DIP-32057N; -.
DR IntAct; O08788; 41.
DR MINT; O08788; -.
DR STRING; 10090.ENSMUSP00000109552; -.
DR ChEMBL; CHEMBL2176787; -.
DR iPTMnet; O08788; -.
DR PhosphoSitePlus; O08788; -.
DR SwissPalm; O08788; -.
DR EPD; O08788; -.
DR jPOST; O08788; -.
DR MaxQB; O08788; -.
DR PaxDb; O08788; -.
DR PeptideAtlas; O08788; -.
DR PRIDE; O08788; -.
DR ProteomicsDB; 279895; -. [O08788-1]
DR ProteomicsDB; 279896; -. [O08788-2]
DR DNASU; 13191; -.
DR Ensembl; ENSMUST00000113918; ENSMUSP00000109551; ENSMUSG00000031865. [O08788-2]
DR Ensembl; ENSMUST00000113919; ENSMUSP00000109552; ENSMUSG00000031865. [O08788-1]
DR GeneID; 13191; -.
DR KEGG; mmu:13191; -.
DR UCSC; uc009cmz.2; mouse. [O08788-1]
DR CTD; 1639; -.
DR MGI; MGI:107745; Dctn1.
DR VEuPathDB; HostDB:ENSMUSG00000031865; -.
DR eggNOG; KOG0971; Eukaryota.
DR GeneTree; ENSGT00940000155378; -.
DR InParanoid; O08788; -.
DR OMA; ADKNMRY; -.
DR PhylomeDB; O08788; -.
DR TreeFam; TF105246; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
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-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 13191; 13 hits in 74 CRISPR screens.
DR ChiTaRS; Dctn1; mouse.
DR PRO; PR:O08788; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O08788; protein.
DR Bgee; ENSMUSG00000031865; Expressed in retinal neural layer and 251 other tissues.
DR ExpressionAtlas; O08788; baseline and differential.
DR Genevisible; O08788; MM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0099738; C:cell cortex region; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0120103; C:centriolar subdistal appendage; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005875; C:microtubule associated complex; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0030904; C:retromer complex; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010457; P:centriole-centriole cohesion; ISS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; IMP:MGI.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; ISS:UniProtKB.
DR GO; GO:0061744; P:motor behavior; ISO:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; ISO:MGI.
DR GO; GO:0050905; P:neuromuscular process; ISO:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISO:MGI.
DR GO; GO:1990535; P:neuron projection maintenance; ISO:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; ISS:UniProtKB.
DR GO; GO:0051081; P:nuclear membrane disassembly; ISS:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:1904398; P:positive regulation of neuromuscular junction development; ISO:MGI.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR GO; GO:0021517; P:ventral spinal cord development; ISO:MGI.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR022157; Dynactin.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF12455; Dynactin; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Dynein; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..1281
FT /note="Dynactin subunit 1"
FT /id="PRO_0000083519"
FT DOMAIN 48..90
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1281
FT /note="Interaction with HPS6"
FT /evidence="ECO:0000269|PubMed:25189619"
FT COILED 214..547
FT /evidence="ECO:0000255"
FT COILED 943..1049
FT /evidence="ECO:0000255"
FT COILED 1185..1214
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..150
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14203"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14203"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14203"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14203"
FT MOD_RES 179
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q14203"
FT MOD_RES 212
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q14203"
FT VAR_SEQ 1049..1086
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029584"
FT CONFLICT 406
FT /note="R -> W (in Ref. 2; BAE34241)"
FT /evidence="ECO:0000305"
FT CONFLICT 721..723
FT /note="TKA -> NKG (in Ref. 1; AAB57773)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="S -> R (in Ref. 1; AAB57773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1202
FT /note="I -> V (in Ref. 2; BAE34241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1281 AA; 141676 MW; A6CEDCAAA7022EB5 CRC64;
MAQSRRHMSS RTPSGSRMST EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV
ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG ADTTSPETPD SSASKVLKRE
GADAAAKTSK LRGLKPKKAP TARKTTTRRP KPTRPASTGV AGPSSSLGPS GSASAGELSS
SEPSTPAQTP LAAPIIPTPA LTSPGAAPPL PSPSKEEEGL RAQVRDLEEK LETLRLKRSE
DKAKLKELEK HKIQLEQVQE WKSKMQEQQA DLQRRLKEAR KEAKEALEAK ERYMEEMADT
ADAIEMATLD KEMAEERAES LQQEVEALKE RVDELTTDLE ILKAEIEEKG SDGAASSYQL
KQLEEQNARL KDALVRMRDL SSSEKQEHVK LQKLMEKKNQ ELEVVRQQRE RLQEELSQAE
STIDELKEQV DAALGAEEMV EMLTDRNLNL EEKVRELRET VGDLEAMNEM NDELQENARE
TELELREQLD MAGARVREAQ KRVEAAQETV ADYQQTIKKY RQLTAHLQDV NRELTNQQEA
SVERQQQPPP ETFDFKIKFA ETKAHAKAIE MELRQMEVAQ ANRHMSLLTA FMPDSFLRPG
GDHDCVLVLL LMPRLICKAE LIRKQAQEKF DLSENCSERP GLRGAAGEQL SFAAGLVYSL
SLLQATLHRY EHALSQCSVD VYKKVGSLYP EMSAHERSLD FLIELLHKDQ LDETVNVEPL
TKAIKYYQHL YSIHLAEQPE DSTMQLADHI KFTQSALDCM GVEVGRLRAF LQGGQEATDI
ALLLRDLETS CSDTRQFCKK IRRRMPGTDA PGIPAALAFG SQVSDTLLDC RKHLTWVVAV
LQEVAAAAAQ LIAPLAENEG LPVAALEELA FKASEQIYGS PSSSPYECLR QSCTILISTM
NKLATAMQEG EYDAERPPSK PPPVELRAAA LRAEITDAEG LGLKLEDRET VIKELKKSLK
IKGEELSEAN VRLSLLEKKL DSAAKDADER IEKVQTRLDE TQTLLRKKEK DFEETMDALQ
ADIDQLEAEK AELKQRLNSQ SKRTIEGLRG PPPSGIATLV SGIAGEEPQR GGAPGQAPGA
LPGPGLVKDS PLLLQQISAM RLHISQLQHE NSILRGAQMK ASLAALPPLH VAKLSLPPHE
GPGGNLVAGA LYRKTSQLLE KLNQLSTHTH VVDITRSSPA AKSPSAQLME QVAQLKSLSD
TIEKLKDEVL KETVTQRPGA TVPTDFATFP SSAFLRAKEE QQDDTVYMGK VTFSCAAGLG
QRHRLVLTQE QLHQLHSRLI S
