ID   DCTN4_PONAB             Reviewed;         460 AA.
AC   Q5R7U7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Dynactin subunit 4;
DE   AltName: Full=Dynactin subunit p62;
GN   Name=DCTN4;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Member of the pointed-end complex of the dynactin shoulder
CC       complex which contains DCTN4, DCTN5 and DCTN6 subunits and ACTR10.
CC       Binds directly to the ACTR1A subunit of dynactin. Interacts with ATP7B,
CC       but not ATP7A, in a copper-dependent manner. Interacts with ANK2; this
CC       interaction is required for localization at costameres. {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:0000250|UniProtKB:Q9QUR2}.
CC       Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9QUR2}. 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 (By similarity). In skeletal
CC       muscles, costamere localization requires the presence of ANK2 (By
CC       similarity). {ECO:0000250|UniProtKB:Q8CBY8,
CC       ECO:0000250|UniProtKB:Q9QUR2, ECO:0000250|UniProtKB:Q9UJW0}.
CC   -!- SIMILARITY: Belongs to the dynactin subunit 4 family. {ECO:0000305}.
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DR   EMBL; CR860012; CAH92163.1; -; mRNA.
DR   RefSeq; NP_001126268.1; NM_001132796.1.
DR   AlphaFoldDB; Q5R7U7; -.
DR   SMR; Q5R7U7; -.
DR   STRING; 9601.ENSPPYP00000017856; -.
DR   PRIDE; Q5R7U7; -.
DR   GeneID; 100173240; -.
DR   KEGG; pon:100173240; -.
DR   CTD; 51164; -.
DR   eggNOG; KOG3896; Eukaryota.
DR   InParanoid; Q5R7U7; -.
DR   OrthoDB; 753907at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005869; C:dynactin complex; IEA:InterPro.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008603; DCTN4.
DR   PANTHER; PTHR13034; PTHR13034; 1.
DR   Pfam; PF05502; Dynactin_p62; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJW0"
FT   CHAIN           2..460
FT                   /note="Dynactin subunit 4"
FT                   /id="PRO_0000079825"
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         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJW0"
FT   MOD_RES         407
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QUR2"
FT   CROSSLNK        215
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJW0"
SQ   SEQUENCE   460 AA;  52291 MW;  FD4FA78831BCA1D2 CRC64;
     MASLLQSDRV VYLVQGEKKV RAPLSQLYFC RYCSELRSLE CVSHEVDSHY CPSCLENMPS
     AEAKLKKNRC ANCFDCPGCM HTLSTRATSI STQLPDDPAK TTMKKAYYLA CGFCRWTSRD
     VGMADKSVAS GGWQEPENPH TQRMNKLIEY YQQLAQKEKV ERDRKKLARR RNYMPLAFSD
     KYGLGTRLQR PRAGASISTL AGLSLKEGED QKEIKIEPAQ AVDEVEPLPE DYYTRPVNLT
     EVTTLQQRLL QPDFQPVCAS QLYPRHKHLL IKRSLRCRKC EHNLSKPEFN PTSIKFKIQQ
     VAVNYIPEVR IMSIPNLRYM KESQVLLTLT NPVENLTHVT LLECEEGDPD NTNSTAKVVV
     PPKELVLAGK DAAAEYDELA EPQDFQDDPD IIAFRKANKV GIFIKVTPQR EEGEVTVCFK
     MKHDFKNLAA PIRPIEESDQ GTEVIWLTQH VELSLGPLLP