DCTN4_MOUSE
ID DCTN4_MOUSE Reviewed; 467 AA.
AC Q8CBY8; Q923A0; Q9D4X0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Dynactin subunit 4;
DE AltName: Full=Dynactin subunit p62;
GN Name=Dctn4;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=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 [3]
RP INTERACTION WITH ANK2, AND SUBCELLULAR LOCATION.
RX PubMed=19109891; DOI=10.1016/j.cell.2008.10.018;
RA Ayalon G., Davis J.Q., Scotland P.B., Bennett V.;
RT "An ankyrin-based mechanism for functional organization of dystrophin and
RT dystroglycan.";
RL Cell 135:1189-1200(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: Could have a dual role in dynein targeting and in ACTR1A/Arp1
CC subunit of dynactin pointed-end capping. Could be involved in ACTR1A
CC pointed-end binding and in additional roles in linking dynein and
CC dynactin to the cortical cytoskeleton.
CC -!- SUBUNIT: Member of the pointed-end complex of the dynactin shoulder
CC complex which contains DCTN4, DCTN5 and DCTN6 subunits and ACTR10 (By
CC similarity). Binds directly to the ACTR1A subunit of dynactin (By
CC similarity). Interacts with ATP7B, but not ATP7A, in a copper-dependent
CC manner (By similarity). Interacts with ANK2; this interaction is
CC required for localization at costameres. {ECO:0000250,
CC ECO:0000269|PubMed:19109891}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9UJW0}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9UJW0}.
CC Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9QUR2}.
CC Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9QUR2}. Cytoplasm,
CC myofibril, sarcomere {ECO:0000269|PubMed:19109891}. Note=Has a punctate
CC cytoplasmic distribution as well as centrosomal distribution typical of
CC dynactin (By similarity). Overexpression in cultured mammalian cells
CC revealed colocalization with cortical actin, stress fibers, and focal
CC adhesion sites, sites of potential interaction between microtubules and
CC the cell cortex (By similarity). In skeletal muscles, costamere
CC localization requires the presence of ANK2 (PubMed:19109891).
CC {ECO:0000250|UniProtKB:Q9QUR2, ECO:0000250|UniProtKB:Q9UJW0,
CC ECO:0000269|PubMed:19109891}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CBY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CBY8-2; Sequence=VSP_013573;
CC -!- SIMILARITY: Belongs to the dynactin subunit 4 family. {ECO:0000305}.
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DR EMBL; AK016059; BAB30095.1; -; mRNA.
DR EMBL; AK034292; BAC28661.1; -; mRNA.
DR EMBL; BC006677; AAH06677.1; -; mRNA.
DR EMBL; BC034725; AAH34725.1; -; mRNA.
DR CCDS; CCDS37832.1; -. [Q8CBY8-2]
DR CCDS; CCDS89246.1; -. [Q8CBY8-1]
DR RefSeq; NP_080578.1; NM_026302.3. [Q8CBY8-2]
DR RefSeq; XP_006526252.1; XM_006526189.3.
DR AlphaFoldDB; Q8CBY8; -.
DR SMR; Q8CBY8; -.
DR BioGRID; 212349; 23.
DR IntAct; Q8CBY8; 16.
DR MINT; Q8CBY8; -.
DR STRING; 10090.ENSMUSP00000025505; -.
DR iPTMnet; Q8CBY8; -.
DR PhosphoSitePlus; Q8CBY8; -.
DR SwissPalm; Q8CBY8; -.
DR EPD; Q8CBY8; -.
DR MaxQB; Q8CBY8; -.
DR PaxDb; Q8CBY8; -.
DR PeptideAtlas; Q8CBY8; -.
DR PRIDE; Q8CBY8; -.
DR ProteomicsDB; 279316; -. [Q8CBY8-1]
DR ProteomicsDB; 279317; -. [Q8CBY8-2]
DR Antibodypedia; 4309; 231 antibodies from 28 providers.
DR DNASU; 67665; -.
DR Ensembl; ENSMUST00000025505; ENSMUSP00000025505; ENSMUSG00000024603. [Q8CBY8-2]
DR Ensembl; ENSMUST00000223984; ENSMUSP00000153008; ENSMUSG00000024603. [Q8CBY8-1]
DR GeneID; 67665; -.
DR KEGG; mmu:67665; -.
DR UCSC; uc008fak.1; mouse. [Q8CBY8-1]
DR CTD; 51164; -.
DR MGI; MGI:1914915; Dctn4.
DR VEuPathDB; HostDB:ENSMUSG00000024603; -.
DR eggNOG; KOG3896; Eukaryota.
DR GeneTree; ENSGT00390000006954; -.
DR HOGENOM; CLU_030384_0_0_1; -.
DR InParanoid; Q8CBY8; -.
DR OMA; PIRPMEE; -.
DR OrthoDB; 753907at2759; -.
DR PhylomeDB; Q8CBY8; -.
DR TreeFam; TF105249; -.
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; 67665; 22 hits in 71 CRISPR screens.
DR ChiTaRS; Dctn4; mouse.
DR PRO; PR:Q8CBY8; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8CBY8; protein.
DR Bgee; ENSMUSG00000024603; Expressed in undifferentiated genital tubercle and 245 other tissues.
DR ExpressionAtlas; Q8CBY8; baseline and differential.
DR Genevisible; Q8CBY8; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISO:MGI.
DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR InterPro; IPR008603; DCTN4.
DR PANTHER; PTHR13034; PTHR13034; 1.
DR Pfam; PF05502; Dynactin_p62; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UJW0"
FT CHAIN 2..467
FT /note="Dynactin subunit 4"
FT /id="PRO_0000079824"
FT COILED 152..172
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJW0"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJW0"
FT MOD_RES 414
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QUR2"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJW0"
FT VAR_SEQ 180..186
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013573"
SQ SEQUENCE 467 AA; 53057 MW; EE026ABB13B62F9E CRC64;
MASLLQSERV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS
AEAKLKKNRC ANCFDCPGCM HTLSTRATSI STQLPDDPAK TTMKKAYYLA CGFCRWTSRD
VGMADKSVAS GGWQEPENPH TQRMNKLIEY YQQLAQKEKV ERDRKKLARR RNYMPLAFSQ
HTIHVVDKYS LGTRLQRPRA GASISTLAGL SLREGEDQKE VKIEPAQAVA EVEPLPEDYY
TRPVNLTEVT TLQQRLLQPD LQPVSASQLY PRHKHLLIKR SLRCRKCEHN LSKPEFNPTS
IKFKIQLVAV NYIPEVRIMS IPNLRYMKES QVLLTLTNPV ENLTHVTLLE CDEGDPDNIN
STAKVVVPPK ELILAGKDAA AEYDELAEPQ DFQDDPDIVA FRKANKVGIF IKVTPQREEG
EVTVCFKMKH DFKNLAAPIR PVEEGDQGTE VIWLTQHVEL SFGPLLP
