ID   A0A3P8X7R7_ESOLU        Unreviewed;      1295 AA.
AC   A0A3P8X7R7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Dynactin subunit 1 {ECO:0000256|ARBA:ARBA00016574};
GN   Name=DCTN1 {ECO:0000313|Ensembl:ENSELUP00000000430.2};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000000430.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000000430.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000000430.2}
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}.
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DR   Ensembl; ENSELUT00000019094.2; ENSELUP00000000430.2; ENSELUG00000002022.2.
DR   GeneTree; ENSGT00940000155378; -.
DR   OrthoDB; 9423at2759; -.
DR   Proteomes; UP000265140; LG15.
DR   Bgee; ENSELUG00000002022; Expressed in brain and 4 other cell types or tissues.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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:UP000265140}.
FT   DOMAIN          67..109
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1010..1069
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1115..1142
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1202..1229
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1295 AA;  144259 MW;  00FBDEBB3836E5DB CRC64;
     MNTELFIQKD HRKGSMSSQT TRRNTYTRTT SSGSSRMSSD GGSRPAKVGS LVEVIGKGHR
     GTVAYIGATL FATGKWVGVI LDEAKGKNDG TVQGKRYFTC QENHGIFVRQ SQIQVVDDGA
     DTTSPDTPEP ASNRVPKREI LETPKSTKLQ RGPKPKKVVH ASRTSTPAPR KTTTRRPKPS
     RPAGTGASKA GPSGSASASA GEISSSELST PAQTPLGAPI IPSPGGLLSP NAAPPPLPSK
     EEESLRAQVK DLEEKLETLK IKRAEDKAKL KELEKHKIQL EQLQEWKNKM QEQQNELTKQ
     LKEAKKEAKE AQEAKEHYME EMADTADAIE MATLDKEMAE ERAESLQQEV ESLKERQEEL
     TMDLEILKHE IEEKGSDGAA SSYHVRQLEE QNSRLKEALV RMRDLSASEK QEHVKLQKQS
     EKKSTELDIL RAQKEKLQEE MKLAERTIDE LKEQVDAALG AEEMVETLTE RNLDLEEKVR
     ELRETVIDLE AINEMNDELQ ENARETELEL REMLDLGGAR VREAEKRVEA AQETVADYQQ
     TIKKYRELTA HLTEVNRELT SQQEATAEQL QQPPAEMFDF KIKFAETKAY AKAIEMELRK
     MEVSQANRQV SLLTSFMPDS FLRHGGDHDC ILVLLLIPRL ICKAELISKQ AQEKFDLNDS
     CVERSGVRGA LGEQLSFAAG LVYSLSLLQA TLHKYEQSLN QCSVEVYKKI GTLYPEMSVH
     ERSLDFLIDL LHRDQLDETV HVEPLTKAIK YYQHLYSIHL AEQTEDCTVQ LADHIKFTQS
     ALDCMSVEVG RLRAFLHTGQ EKADLAVLLK DLETSCSDIR QFCKKIRRRM PGTDVPGIPA
     ALTFPQQVSD TLLDCRKHLT WLVAVLQEVA AAGAQMVAPL GEQEGLSALK LEDVAFKAGE
     QIYGNPGSNP YECLRQSCCI VIATMNKMAT AMQEGEYDAE RPQITTPPPV ELRAAALRAE
     ISDAEGLGMK IEDRETVIKE LKKSLKIKGE ELSEASVRLS LLEKKLDSSS KDADERVEKI
     QTRLDETQTL LKKKEKEFEE TMDALQADID QLESEKAELK QRLNSQSKVT IDGLRGAPSS
     GIASTVTGMT GATISSLGSG SGVQVIDSPL LKQQIEAQRL SIKHLKNENN RLKAEKMRAQ
     LASLPPLHVP KLPTRDGSQP EVLSSALYRK TDQLLDTLLQ MSANVKVVDI TGKSPVTPSA
     QLLEQTARLQ SLSDTLERLK DEVSEHVVTQ RPGARASSDF ATFPCTSFVK AKEEKRGDTV
     LVGKVMMPCS RGQEQVHRLV LSQPQLHRVH RLLLT
//