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   24-JAN-2024, entry version 183.
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,
RC   Pancreas, 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: Part of the dynactin complex that activates the molecular
CC       motor dynein for ultra-processive transport along microtubules (By
CC       similarity). Plays a key role in dynein-mediated retrograde transport
CC       of vesicles and organelles along microtubules by recruiting and
CC       tethering dynein to microtubules. Binds to both dynein and microtubules
CC       providing a link between specific cargos, microtubules and dynein.
CC       Essential for targeting dynein to microtubule plus ends, recruiting
CC       dynein to membranous cargos and enhancing dynein processivity (the
CC       ability to move along a microtubule for a long distance without falling
CC       off the 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 (By similarity).
CC       {ECO:0000250|UniProtKB:A0A287B8J2, ECO:0000250|UniProtKB:Q14203}.
CC   -!- SUBUNIT: Monomer and homodimer (By similarity). Subunit of dynactin, a
CC       multiprotein complex part of a tripartite complex with dynein and a
CC       adapter, such as BICDL1, BICD2 or HOOK3. The dynactin complex is built
CC       around ACTR1A/ACTB filament and consists of an actin-related filament
CC       composed of a shoulder domain, a pointed end and a barbed end. Its
CC       length is defined by its flexible shoulder domain. The soulder is
CC       composed of 2 DCTN1 subunits, 4 DCTN2 and 2 DCTN3. DCTN1/p150(glued)
CC       binds directly to microtubules and to cytoplasmic dynein. The 4 DCNT2
CC       (via N-terminus) bind the ACTR1A filament and act as molecular rulers
CC       to determine the length. The pointed end is important for binding
CC       dynein-dynactin cargo adapters. Consists of 4 subunits: ACTR10, DCNT4,
CC       DCTN5 and DCTN6. The barbed end is composed of a CAPZA1:CAPZB
CC       heterodimers, which binds ACTR1A/ACTB filament and dynactin and
CC       stabilizes dynactin (By similarity). Interacts with the C-terminus of
CC       MAPRE1, MAPRE2 and MAPRE3. Interacts with FBXL5. Interacts with ECPAS.
CC       Interacts with CLIP1. Interacts with CLN3 and DYNAP. Interacts with
CC       MISP; this interaction regulates its distribution at the cell cortex.
CC       Interacts with CEP131. Interacts with CEP126. Interacts with dynein
CC       intermediate chain and dynein heavy chain. Interacts with PLK1 (via
CC       POLO-box domain). Interacts with TBCB and PARD6A (By similarity). Binds
CC       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:A0A287B8J2,
CC       ECO:0000250|UniProtKB:Q14203, ECO:0000269|PubMed:14581450,
CC       ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19935774,
CC       ECO:0000269|PubMed:22275436, ECO:0000269|PubMed:22956769,
CC       ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:25189619,
CC       ECO:0000269|PubMed:27474409, 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; 73.
DR   CORUM; O08788; -.
DR   DIP; DIP-32057N; -.
DR   IntAct; O08788; 42.
DR   MINT; O08788; -.
DR   STRING; 10090.ENSMUSP00000109552; -.
DR   ChEMBL; CHEMBL2176787; -.
DR   GlyGen; O08788; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; O08788; -.
DR   PhosphoSitePlus; O08788; -.
DR   SwissPalm; O08788; -.
DR   EPD; O08788; -.
DR   jPOST; O08788; -.
DR   MaxQB; O08788; -.
DR   PaxDb; 10090-ENSMUSP00000109552; -.
DR   PeptideAtlas; O08788; -.
DR   ProteomicsDB; 279895; -. [O08788-1]
DR   ProteomicsDB; 279896; -. [O08788-2]
DR   Pumba; O08788; -.
DR   DNASU; 13191; -.
DR   Ensembl; ENSMUST00000113918.8; ENSMUSP00000109551.2; ENSMUSG00000031865.17. [O08788-2]
DR   Ensembl; ENSMUST00000113919.10; ENSMUSP00000109552.4; ENSMUSG00000031865.17. [O08788-1]
DR   GeneID; 13191; -.
DR   KEGG; mmu:13191; -.
DR   UCSC; uc009cmz.2; mouse. [O08788-1]
DR   AGR; MGI:107745; -.
DR   CTD; 1639; -.
DR   MGI; MGI:107745; Dctn1.
DR   VEuPathDB; HostDB:ENSMUSG00000031865; -.
DR   eggNOG; KOG0971; Eukaryota.
DR   GeneTree; ENSGT00940000155378; -.
DR   InParanoid; O08788; -.
DR   OMA; LFEMEPV; -.
DR   OrthoDB; 9423at2759; -.
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 79 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 255 other cell types or tissues.
DR   ExpressionAtlas; O08788; baseline and differential.
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:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0030904; C:retromer complex; IEA:Ensembl.
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:0060090; F:molecular adaptor activity; ISO:MGI.
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; CAP Gly-rich-like domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR022157; Dynactin.
DR   PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR   PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12455; Dynactin; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
DR   Genevisible; O08788; MM.
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
//