ID DCTN5_MOUSE Reviewed; 182 AA. AC Q9QZB9; Q3U9A4; Q8BPE5; Q91XC6; Q99J17; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 148. DE RecName: Full=Dynactin subunit 5; DE AltName: Full=Dynactin subunit p25; GN Name=Dctn5; 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], AND SUBUNIT. RX PubMed=10525537; DOI=10.1083/jcb.147.2.307; RA Eckley D.M., Gill S.R., Melkonian K.A., Bingham J.B., Goodson H.V., RA Heuser J.E., Schroer T.A.; RT "Analysis of dynactin subcomplexes reveals a novel actin-related protein RT associated with the Arp1 minifilament pointed end."; RL J. Cell Biol. 147:307-320(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Amnion, Bone marrow, Embryo, Eye, Testis, and Tongue; 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 MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, Liver, Lung, and Spleen; 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). CC -!- FUNCTION: Part of the dynactin complex that activates the molecular CC motor dynein for ultra-processive transport along microtubules. CC {ECO:0000250|UniProtKB:Q9BTE1}. CC -!- SUBUNIT: Subunit of dynactin, a multiprotein complex part of a CC tripartite complex with dynein and a adapter, such as BICDL1, BICD2 or CC HOOK3. The dynactin complex is built around ACTR1A/ACTB filament and CC consists of an actin-related filament composed of a shoulder domain, a CC pointed end and a barbed end. Its length is defined by its flexible CC shoulder domain. The soulder is composed of 2 DCTN1 subunits, 4 DCTN2 CC and 2 DCTN3. The 4 DCNT2 (via N-terminus) bind the ACTR1A filament and CC act as molecular rulers to determine the length. The pointed end is CC important for binding dynein-dynactin cargo adapters. Consists of 4 CC subunits: ACTR10, DCNT4, DCTN5 and DCTN6. Within the complex DCTN6 CC forms a heterodimer with DCTN5 (PubMed:10525537). The barbed end is CC composed of a CAPZA1:CAPZB heterodimers, which binds ACTR1A/ACTB CC filament and dynactin and stabilizes dynactin (By similarity). CC {ECO:0000250|UniProtKB:A0A286ZK88, ECO:0000269|PubMed:10525537}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:A0A286ZK88}. Chromosome, centromere, kinetochore CC {ECO:0000250|UniProtKB:Q9BTE1}. CC -!- SIMILARITY: Belongs to the dynactin subunits 5/6 family. Dynactin CC subunit 5 subfamily. {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; AF190795; AAF05615.1; -; mRNA. DR EMBL; AK010238; BAB26789.1; -; mRNA. DR EMBL; AK051957; BAC34820.1; -; mRNA. DR EMBL; AK076100; BAC36183.1; -; mRNA. DR EMBL; AK076738; BAC36460.1; -; mRNA. DR EMBL; AK151193; BAE30190.1; -; mRNA. DR EMBL; AK151876; BAE30763.1; -; mRNA. DR EMBL; AK168983; BAE40783.1; -; mRNA. DR EMBL; BC010834; AAH10834.1; -; mRNA. DR EMBL; BC005671; AAH05671.1; -; mRNA. DR CCDS; CCDS21811.1; -. DR RefSeq; NP_067621.3; NM_021608.3. DR AlphaFoldDB; Q9QZB9; -. DR SMR; Q9QZB9; -. DR BioGRID; 208544; 19. DR IntAct; Q9QZB9; 19. DR MINT; Q9QZB9; -. DR STRING; 10090.ENSMUSP00000033156; -. DR GlyGen; Q9QZB9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9QZB9; -. DR PhosphoSitePlus; Q9QZB9; -. DR SwissPalm; Q9QZB9; -. DR EPD; Q9QZB9; -. DR MaxQB; Q9QZB9; -. DR PaxDb; 10090-ENSMUSP00000033156; -. DR PeptideAtlas; Q9QZB9; -. DR ProteomicsDB; 279841; -. DR Pumba; Q9QZB9; -. DR Antibodypedia; 43088; 126 antibodies from 20 providers. DR DNASU; 59288; -. DR Ensembl; ENSMUST00000033156.5; ENSMUSP00000033156.5; ENSMUSG00000030868.7. DR GeneID; 59288; -. DR KEGG; mmu:59288; -. DR UCSC; uc009jon.2; mouse. DR AGR; MGI:1891689; -. DR CTD; 84516; -. DR MGI; MGI:1891689; Dctn5. DR VEuPathDB; HostDB:ENSMUSG00000030868; -. DR eggNOG; KOG3121; Eukaryota. DR GeneTree; ENSGT00390000015360; -. DR HOGENOM; CLU_088622_2_0_1; -. DR InParanoid; Q9QZB9; -. DR OMA; SQIHGTQ; -. DR OrthoDB; 275352at2759; -. DR PhylomeDB; Q9QZB9; -. DR TreeFam; TF314194; -. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport. DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR BioGRID-ORCS; 59288; 28 hits in 78 CRISPR screens. DR ChiTaRS; Dctn5; mouse. DR PRO; PR:Q9QZB9; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q9QZB9; Protein. DR Bgee; ENSMUSG00000030868; Expressed in floor plate of midbrain and 264 other cell types or tissues. DR ExpressionAtlas; Q9QZB9; baseline and differential. DR GO; GO:0005813; C:centrosome; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central. DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW. DR GO; GO:0031965; C:nuclear membrane; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0035904; P:aorta development; IMP:MGI. DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI. DR GO; GO:0003281; P:ventricular septum development; IMP:MGI. DR CDD; cd03359; LbH_Dynactin_5; 1. DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1. DR InterPro; IPR047125; DCTN5. DR InterPro; IPR011004; Trimer_LpxA-like_sf. DR PANTHER; PTHR46126; DYNACTIN SUBUNIT 5; 1. DR PANTHER; PTHR46126:SF1; DYNACTIN SUBUNIT 5; 1. DR Pfam; PF21711; DCTN5; 1. DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1. DR Genevisible; Q9QZB9; MM. PE 1: Evidence at protein level; KW Acetylation; Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinetochore; KW Reference proteome. FT CHAIN 1..182 FT /note="Dynactin subunit 5" FT /id="PRO_0000079828" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q9BTE1" FT CONFLICT 11 FT /note="S -> L (in Ref. 3; AAH10834)" FT /evidence="ECO:0000305" FT CONFLICT 95 FT /note="E -> G (in Ref. 2; BAC36183)" FT /evidence="ECO:0000305" SQ SEQUENCE 182 AA; 20141 MW; 476DAB4B7805D496 CRC64; MELGELLYNK SEYIETASGN KVSRQSVLCG SQNIVLNGKT IIMNDCIIRG DLANVRVGRH CVVKSRSVIR PPFKKFSKGV AFFPLHIGDH VFIEEDCVVN AAQIGSYVHV GKNCVIGRRC VLKDCCKILD NTVLPPETVV PPFTVFSGCP GLFSGELPEC TQELMIDVTK SYYQKFLPLT QV //