ID I3LXR7_ICTTR Unreviewed; 1281 AA.
AC I3LXR7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Dynactin subunit 1 {ECO:0000256|ARBA:ARBA00016574};
GN Name=DCTN1 {ECO:0000313|Ensembl:ENSSTOP00000000893.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000000893.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000000893.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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DR EMBL; AGTP01057538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 43179.ENSSTOP00000000893; -.
DR Ensembl; ENSSTOT00000000997.3; ENSSTOP00000000893.3; ENSSTOG00000000987.3.
DR eggNOG; KOG0971; Eukaryota.
DR GeneTree; ENSGT00940000155378; -.
DR HOGENOM; CLU_002523_0_0_1; -.
DR InParanoid; I3LXR7; -.
DR OrthoDB; 9423at2759; -.
DR TreeFam; TF105246; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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; 1.10.287.2610; -; 1.
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:UP000005215}.
FT DOMAIN 48..90
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 952..1043
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..150
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1281 AA; 141926 MW; A8E39992656180B1 CRC64;
MAQSKRHVYN RTPSGSRMSA EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV
ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG ADTTSPETPD SSTSKVLKRE
GAETAAKTSK LRGLKPKKAP TARKTTTRRP KPTRPASTGV AGASSSLGPS GSASAGELSS
SEPSTPAQTP LAAPIIPTPA LTSPGAAPPL PSPSKEEEGL RAQVRDLEEK LETLRLKRAE
DKAKLKELEK HKIQLEQVQE WKSKMQEQQA DLQRRLKEAR KEAKEALEAK ERYMEEMADT
ADAIEMATLD KEMAEERAES LQQEVEALKE RVDELTTDLE ILKAEIEEKG SDGAASSYQL
KQLEEQNARL KDALVRMRDL SSSEKQEHVK LQKLMEKKNQ ELEIVRQQRE RLQEELSQAE
STIDELKEQV DAALGAEEMV EMLTDRNLNL EEKVRELRET VGDLEAMNEM NDELQENARE
TELELREQLD MAGARVREAQ KRVEAAQETV ADYQQTIKKY RQLTAHLQDV NRELTNQQEA
SVERQQQPPP ETFDFKIKFA ETKAHAKAIE MELRQMEVAQ ANRHMSLLTA FMPDSFLRPG
GDHDCVLVLL LMPRLICKAE LIRKQAQEKF ELSENCSERP GLRGAAGEQL SFAAGLVYSL
SLLQATLHRY EHALSQCNVD VYKKVGSLYP EMSAHERSLD FLIELLHKDQ LDETVNVEPL
TKAIKYYQHL YSIHLAEQPE ESTMQLADHI KFTQSALDCM SVEVGRLRAF LQGGQEATDI
ALLLRDLETS CSDIRQFCKK IRRRMPGTDA PGIPAALAFG PQVSDTLLDC RKHLTWVVAV
LQEVAAAAAQ LIAPLAENEG LPVAALEELA FKASEQIYGS PSSSPYECLR QSCNILISTM
NKLATAMQEG EYDAERPPSK PPPVELRAAA LRAEITDAEG LGLKLEDRET VIKELKKSLK
IKGEELSEAN VRLSLLEKKL DSAAKDADER IEKVQTRLEE TQALLRKKEK EFEETMDALQ
ADIDQLEAEK AELKQRLNSQ SKRTIEGLRG PPPSGIATLV SGIAGEEQQR GVVPGQAPGS
LPGPGLVKDS PLLLQQISAM RLHISQLQHE NSILKGAQMK ASLAALPPLH VAKLSLPPQE
GPGGEIAAGA LYRKTSQLLE TLNQLSTRTH VVDITRTSPA AKSPSAQLME QVAQLKSLSD
TIEKLKDEVL KETVSQRPGA TVPTDFATFP STAFLRAKEE QQDDTVYMGK VTFSCAAGLG
QRHRLVLTQE QLHQLHSRLI S
//
