ID A0A452FYJ5_CAPHI Unreviewed; 1262 AA.
AC A0A452FYJ5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Dynactin subunit 1 {ECO:0000256|ARBA:ARBA00016574};
GN Name=DCTN1 {ECO:0000313|Ensembl:ENSCHIP00000029510.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000029510.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000029510.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000029510.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00011010}.
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; LWLT01000009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452FYJ5; -.
DR STRING; 9925.ENSCHIP00000029510; -.
DR Ensembl; ENSCHIT00000037380.1; ENSCHIP00000029510.1; ENSCHIG00000024570.1.
DR GeneTree; ENSGT00940000155378; -.
DR Proteomes; UP000291000; Chromosome 11.
DR Bgee; ENSCHIG00000024570; Expressed in prefrontal cortex and 17 other cell types or tissues.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0120103; C:centriolar subdistal appendage; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0035371; C:microtubule plus-end; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0030904; C:retromer complex; IEA:Ensembl.
DR GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0010457; P:centriole-centriole cohesion; IEA:Ensembl.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:Ensembl.
DR GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IEA:Ensembl.
DR GO; GO:0061744; P:motor behavior; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR GO; GO:1990535; P:neuron projection maintenance; IEA:Ensembl.
DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0051081; P:nuclear membrane disassembly; IEA:Ensembl.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IEA:Ensembl.
DR GO; GO:1904398; P:positive regulation of neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:Ensembl.
DR GO; GO:0021517; P:ventral spinal cord development; IEA:Ensembl.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR022157; Dynactin.
DR PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF12455; Dynactin; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Dynein {ECO:0000256|ARBA:ARBA00023017};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000}.
FT DOMAIN 48..90
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..520
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 932..1024
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1262 AA; 139473 MW; F5729AD2648F6F0B CRC64;
MAQSKRHVYS RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV
ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG ADTTSPETPD SSASKVLRRE
GADSNPKTSK LPTRPASTGV AGASGSLGPS GSASAGELSS SEPSTPAQTP LAAPIIPTPA
LTSPGAVLPL PSPSKEEEGL RAQVRDLEEK LETLRLKRAE DKAKLKELEK HKIQLEQVQE
WKSKMQEQQA DLQRRLKEAR KEAKEALEAK ERYMEEMADT ADAIEMATLD KEMAEERAES
LQQEAEVLRE RVEELTTDLE ILKAEIEEKG SDGAASSYQL KQLEEQNARL KDALVRMRDL
SSSEKQEHVK LQKLMEKKNQ ELEVVRQQRE RLQEELSQAE RTIDELKEQV DAALGAEEMV
ETLTDRNLDL EEKVRKLKET VGDLEAINEM NDELQENARE TELELREQLD MAGAQVRDAQ
KRVEAAQETV ADYQQTIRKY RQLTAHLQDV NRALTNQQEA SVERQQQPPP ETFDFKIKFA
ETKAHAKAIE MELRQMEVVQ ANRHMGLLTA FMPDSFLRPG GDHDCVLVLL LMPRLICKAE
LIRKQAQEKF ELSESCSERP GLRGAAGEQL SFAAGLVYSL SLLQATLHRY EHALSQCSVD
VYKKVGSLYP EMSAHERSLD FLIELLHKDQ LDETVNVEPL TKAIKYYQHL YSIHLAEQPE
DSTMQLADHI KFTQSALDCM SVEVGRLRAF LQGGQEASDI ALLLRDLETS CSDTRQFCKK
IRRRMPGTDA PGIPSALAFG PQVSDTLLDC RKHLTWVVAV LQEVAAAAAQ LIAPLAENEG
LPVAALEELA FKASEQIYGA PSSNPYECLR QSCSLLISTM NKLATAMQEG EYDAERPPSK
PPPVELRAAA LRAEIMDAEG LGLKLEDRET VIKELKKSLK IKGEELSEAN VRLSLLEKKL
DSAAKDADER IEKVQTRLEE TQTLLRKKEK SEFEETMDAL QADIDQLEAE KAELKQRLNS
QSKRTIEGLR GPPPSGIATL VSGIAGGECR GAGAPGQAPG SVPGPGLVKD SPLLLQQISA
MRLHISQLQH ENSTLKGAQM KASLAALPPL HVAKLSLPPH EGPGSELAAG ALYRKTNQLL
ETLNQLSART HVVDITRSNP AAKSPSAQLL EQVAQLKSLS DTIEKLKDEV LKETVSQRPG
ATVPTDFATF PSSAFLRAKE EQQDDTVYMG KVTFSCAAGL GQRHRLVLTQ EQLHQLHDRL
IS
//
