DCTN4_RAT
ID DCTN4_RAT Reviewed; 467 AA.
AC Q9QUR2; Q9QXP8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Dynactin subunit 4;
DE AltName: Full=Dynactin subunit p62;
GN Name=Dctn4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP POSSIBLE FUNCTION.
RC TISSUE=Brain;
RX PubMed=10607597; DOI=10.1016/s0960-9822(00)80122-0;
RA Garces J.A., Clark I.B., Meyer D.I., Vallee R.B.;
RT "Interaction of the p62 subunit of dynactin with Arp1 and the cortical
RT actin cytoskeleton.";
RL Curr. Biol. 9:1497-1500(1999).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-414, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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). 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 (By similarity). Binds directly
CC to the ACTR1A subunit of dynactin. {ECO:0000250}.
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:0000269|PubMed:10607597}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:10607597}. Cytoplasm,
CC myofibril, sarcomere {ECO:0000250|UniProtKB:Q8CBY8}. Note=Has a
CC punctate cytoplasmic distribution as well as centrosomal distribution
CC typical of dynactin (By similarity). Overexpression in cultured
CC mammalian cells revealed colocalization with cortical actin, stress
CC fibers, and focal adhesion sites, sites of potential interaction
CC between microtubules and the cell cortex (PubMed:10607597). In skeletal
CC muscles, costamere localization requires the presence of ANK2 (By
CC similarity). {ECO:0000250|UniProtKB:Q8CBY8,
CC ECO:0000250|UniProtKB:Q9UJW0, ECO:0000269|PubMed:10607597}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QUR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QUR2-2; Sequence=VSP_013574;
CC -!- SIMILARITY: Belongs to the dynactin subunit 4 family. {ECO:0000305}.
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DR EMBL; AF190798; AAF05618.1; -; mRNA.
DR EMBL; AF192493; AAF03421.1; -; mRNA.
DR EMBL; AF192494; AAF03422.1; -; mRNA.
DR RefSeq; NP_445856.1; NM_053404.2. [Q9QUR2-1]
DR RefSeq; XP_006254845.1; XM_006254783.3. [Q9QUR2-2]
DR AlphaFoldDB; Q9QUR2; -.
DR SMR; Q9QUR2; -.
DR BioGRID; 249964; 4.
DR IntAct; Q9QUR2; 2.
DR STRING; 10116.ENSRNOP00000026394; -.
DR iPTMnet; Q9QUR2; -.
DR PhosphoSitePlus; Q9QUR2; -.
DR jPOST; Q9QUR2; -.
DR PaxDb; Q9QUR2; -.
DR PRIDE; Q9QUR2; -.
DR Ensembl; ENSRNOT00000026334; ENSRNOP00000026334; ENSRNOG00000019298. [Q9QUR2-2]
DR Ensembl; ENSRNOT00000026394; ENSRNOP00000026394; ENSRNOG00000019298. [Q9QUR2-1]
DR GeneID; 84428; -.
DR KEGG; rno:84428; -.
DR UCSC; RGD:71023; rat. [Q9QUR2-1]
DR CTD; 51164; -.
DR RGD; 71023; Dctn4.
DR eggNOG; KOG3896; Eukaryota.
DR GeneTree; ENSGT00390000006954; -.
DR HOGENOM; CLU_030384_0_0_1; -.
DR InParanoid; Q9QUR2; -.
DR OMA; PIRPMEE; -.
DR OrthoDB; 753907at2759; -.
DR PhylomeDB; Q9QUR2; -.
DR TreeFam; TF105249; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q9QUR2; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000019298; Expressed in testis and 18 other tissues.
DR ExpressionAtlas; Q9QUR2; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:MGI.
DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:RGD.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IDA:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
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_0000079826"
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:0007744|PubMed:16641100"
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:10607597"
FT /id="VSP_013574"
SQ SEQUENCE 467 AA; 53089 MW; 2134F40E21108E08 CRC64;
MASLLQSERV LYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS
AEAKLKKNRC ANCFDCPGCM HTLSTRATSI STQLPDDPAK TTMKKAYYLA CGFCRWTSRD
VGMADKSVAS GGWQEPENPH AQRMNKLIEY YQQLAQKEKV ERDRKKLARR RNYMPLAFSQ
HTIHVVDKYS LGTRLQRPRA GASISTLAGL SLREGEDQKE VKIEPAQAVA EVEPLPEDYY
TRPVNLTEVT TLQQRLLQPD LQPVSASQLY PRHKHLLIKR SLRCRKCEHN LSKPEFNPTS
IKFKIQLVAV NYIPEVRIMS IPNLRYMKES QVLLTLTNPV ENLTHVTLLE CEEGDPDNIN
STAKVVVPPK ELILAGKDAA AEYDELAEPQ DFQDDPDIVA FRKANKVGIF IKVTPQREEG
DVTVCFKMKH DFKNLAAPIR PMEESDQGTE VIWLTQHVEL SFGPLLP
