ID   DCTN5_HUMAN             Reviewed;         182 AA.
AC   Q9BTE1; A8K9X8; H3BN51; H3BQA4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=Dynactin subunit 5;
DE   AltName: Full=Dynactin subunit p25;
GN   Name=DCTN5 {ECO:0000312|HGNC:HGNC:24594};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary gland, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney, and Trophoblast;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [9]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=23455152; DOI=10.1038/emboj.2013.30;
RA   Yeh T.Y., Kowalska A.K., Scipioni B.R., Cheong F.K., Zheng M.,
RA   Derewenda U., Derewenda Z.S., Schroer T.A.;
RT   "Dynactin helps target Polo-like kinase 1 to kinetochores via its left-
RT   handed beta-helical p27 subunit.";
RL   EMBO J. 32:1023-1035(2013).
CC   -!- FUNCTION: Part of the dynactin complex that activates the molecular
CC       motor dynein for ultra-processive transport along microtubules.
CC       {ECO:0000269|PubMed:23455152}.
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 (PubMed:23455152). The dynactin complex is built around
CC       ACTR1A/ACTB filament and consists of an actin-related filament composed
CC       of a shoulder domain, a pointed end and a barbed end. Its length is
CC       defined by its flexible shoulder domain. The soulder is composed of 2
CC       DCTN1 subunits, 4 DCTN2 and 2 DCTN3. The 4 DCNT2 (via N-terminus) bind
CC       the ACTR1A filament and act as molecular rulers to determine the
CC       length. The pointed end is important for binding dynein-dynactin cargo
CC       adapters. Consists of 4 subunits: ACTR10, DCNT4, DCTN5 and DCTN6.
CC       Within the complex DCTN6 forms a heterodimer with DCTN5
CC       (PubMed:23455152). The barbed end is composed of a CAPZA1:CAPZB
CC       heterodimers, which binds ACTR1A/ACTB filament and dynactin and
CC       stabilizes dynactin (By similarity). {ECO:0000250|UniProtKB:A0A286ZK88,
CC       ECO:0000269|PubMed:23455152}.
CC   -!- INTERACTION:
CC       Q9BTE1; P63167: DYNLL1; NbExp=3; IntAct=EBI-747324, EBI-349105;
CC       Q9BTE1; Q969F0: FATE1; NbExp=3; IntAct=EBI-747324, EBI-743099;
CC       Q9BTE1; Q93062: RBPMS; NbExp=3; IntAct=EBI-747324, EBI-740322;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:A0A286ZK88}. Chromosome, centromere, kinetochore
CC       {ECO:0000269|PubMed:23455152}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9BTE1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BTE1-2; Sequence=VSP_046023;
CC       Name=3;
CC         IsoId=Q9BTE1-3; Sequence=VSP_046697;
CC   -!- SIMILARITY: Belongs to the dynactin subunits 5/6 family. Dynactin
CC       subunit 5 subfamily. {ECO:0000305}.
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DR   EMBL; AK027387; BAB55077.1; -; mRNA.
DR   EMBL; AK292843; BAF85532.1; -; mRNA.
DR   EMBL; AC008870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471145; EAW55809.1; -; Genomic_DNA.
DR   EMBL; CH471145; EAW55810.1; -; Genomic_DNA.
DR   EMBL; BC004191; AAH04191.1; -; mRNA.
DR   EMBL; CD388246; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS10615.1; -. [Q9BTE1-1]
DR   CCDS; CCDS58435.1; -. [Q9BTE1-3]
DR   CCDS; CCDS58436.1; -. [Q9BTE1-2]
DR   RefSeq; NP_001185940.1; NM_001199011.1. [Q9BTE1-3]
DR   RefSeq; NP_001186672.1; NM_001199743.1. [Q9BTE1-2]
DR   RefSeq; NP_115875.1; NM_032486.3. [Q9BTE1-1]
DR   PDB; 5NW4; EM; 8.70 A; h=1-182.
DR   PDBsum; 5NW4; -.
DR   AlphaFoldDB; Q9BTE1; -.
DR   EMDB; EMD-3706; -.
DR   SMR; Q9BTE1; -.
DR   BioGRID; 124110; 98.
DR   IntAct; Q9BTE1; 31.
DR   MINT; Q9BTE1; -.
DR   STRING; 9606.ENSP00000300087; -.
DR   iPTMnet; Q9BTE1; -.
DR   PhosphoSitePlus; Q9BTE1; -.
DR   BioMuta; DCTN5; -.
DR   DMDM; 62900103; -.
DR   EPD; Q9BTE1; -.
DR   jPOST; Q9BTE1; -.
DR   MassIVE; Q9BTE1; -.
DR   MaxQB; Q9BTE1; -.
DR   PaxDb; 9606-ENSP00000300087; -.
DR   PeptideAtlas; Q9BTE1; -.
DR   ProteomicsDB; 41095; -.
DR   ProteomicsDB; 41730; -.
DR   ProteomicsDB; 78981; -. [Q9BTE1-1]
DR   Pumba; Q9BTE1; -.
DR   Antibodypedia; 43088; 126 antibodies from 20 providers.
DR   DNASU; 84516; -.
DR   Ensembl; ENST00000300087.7; ENSP00000300087.2; ENSG00000166847.10. [Q9BTE1-1]
DR   Ensembl; ENST00000563998.5; ENSP00000454691.1; ENSG00000166847.10. [Q9BTE1-2]
DR   Ensembl; ENST00000568272.1; ENSP00000455685.1; ENSG00000166847.10. [Q9BTE1-3]
DR   GeneID; 84516; -.
DR   KEGG; hsa:84516; -.
DR   MANE-Select; ENST00000300087.7; ENSP00000300087.2; NM_032486.4; NP_115875.1.
DR   UCSC; uc002dly.3; human. [Q9BTE1-1]
DR   AGR; HGNC:24594; -.
DR   CTD; 84516; -.
DR   DisGeNET; 84516; -.
DR   GeneCards; DCTN5; -.
DR   HGNC; HGNC:24594; DCTN5.
DR   HPA; ENSG00000166847; Low tissue specificity.
DR   MIM; 612962; gene.
DR   neXtProt; NX_Q9BTE1; -.
DR   OpenTargets; ENSG00000166847; -.
DR   PharmGKB; PA142672007; -.
DR   VEuPathDB; HostDB:ENSG00000166847; -.
DR   eggNOG; KOG3121; Eukaryota.
DR   GeneTree; ENSGT00390000015360; -.
DR   HOGENOM; CLU_088622_2_0_1; -.
DR   InParanoid; Q9BTE1; -.
DR   OMA; SQIHGTQ; -.
DR   OrthoDB; 275352at2759; -.
DR   PhylomeDB; Q9BTE1; -.
DR   TreeFam; TF314194; -.
DR   PathwayCommons; Q9BTE1; -.
DR   Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR   Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   SignaLink; Q9BTE1; -.
DR   BioGRID-ORCS; 84516; 783 hits in 1157 CRISPR screens.
DR   ChiTaRS; DCTN5; human.
DR   GeneWiki; DCTN5; -.
DR   GenomeRNAi; 84516; -.
DR   Pharos; Q9BTE1; Tbio.
DR   PRO; PR:Q9BTE1; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9BTE1; Protein.
DR   Bgee; ENSG00000166847; Expressed in islet of Langerhans and 201 other cell types or tissues.
DR   ExpressionAtlas; Q9BTE1; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR   GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR   GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
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; Q9BTE1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Centromere; Chromosome;
KW   Cytoplasm; Cytoskeleton; Kinetochore; Reference proteome.
FT   CHAIN           1..182
FT                   /note="Dynactin subunit 5"
FT                   /id="PRO_0000079827"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   VAR_SEQ         40..182
FT                   /note="TIVMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGVAFFPLHIGDHV
FT                   FIEEDCVVNAAQIGSYVHVGKNCVIGRRCVLKDCCKILDNTVLPPETVVPPFTVFSGCP
FT                   GLFSGELPECTQELMIDVTKSYYQKFLPLTQV -> NFVISVFLSPYIRCHSACRDRKR
FT                   SDESVRLSVNNREWWGLVNWRM (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046697"
FT   VAR_SEQ         151..182
FT                   /note="GLFSGELPECTQELMIDVTKSYYQKFLPLTQV -> AP (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046023"
SQ   SEQUENCE   182 AA;  20127 MW;  476DBD27A6CA1C35 CRC64;
     MELGELLYNK SEYIETASGN KVSRQSVLCG SQNIVLNGKT IVMNDCIIRG DLANVRVGRH
     CVVKSRSVIR PPFKKFSKGV AFFPLHIGDH VFIEEDCVVN AAQIGSYVHV GKNCVIGRRC
     VLKDCCKILD NTVLPPETVV PPFTVFSGCP GLFSGELPEC TQELMIDVTK SYYQKFLPLT
     QV
//