DCTN1_CHICK
ID DCTN1_CHICK Reviewed; 1224 AA.
AC P35458;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Dynactin subunit 1;
DE AltName: Full=150 kDa dynein-associated polypeptide;
DE AltName: Full=DAP-150;
DE Short=DP-150;
DE AltName: Full=p150-glued;
GN Name=DCTN1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cleveland D.W.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 172-1224, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryonic brain;
RX PubMed=1836789; DOI=10.1083/jcb.115.6.1639;
RA Gill S.R., Schroer T.A., Szilak I., Steuer E.R., Sheetz M.P.,
RA Cleveland D.W.;
RT "Dynactin, a conserved, ubiquitously expressed component of an activator of
RT vesicle motility mediated by cytoplasmic dynein.";
RL J. Cell Biol. 115:1639-1650(1991).
CC -!- FUNCTION: Plays a key role in dynein-mediated retrograde transport of
CC vesicles and organelles along microtubules by recruiting and tethering
CC dynein to microtubules. Binds to both dynein and microtubules providing
CC a link between specific cargos, microtubules and dynein. Plays a role
CC in metaphase spindle orientation. {ECO:0000250|UniProtKB:Q14203}.
CC -!- SUBUNIT: Binds to microtubules and to cytoplasmic dynein. Binds
CC preferentially to tyrosinated microtubules than to detyrosinated
CC microtubules. {ECO:0000250|UniProtKB:Q14203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1836789}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:1836789}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:1836789}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus
CC ends. Localizes preferentially to tyrosinated microtubules than to
CC detyrosinated microtubules. {ECO:0000250|UniProtKB:Q14203}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=At least 3 isoforms are produced.;
CC Name=1;
CC IsoId=P35458-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:1836789}.
CC -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; X62773; CAA44617.2; -; mRNA.
DR PIR; A41642; A41642.
DR RefSeq; NP_001026538.1; NM_001031367.1. [P35458-1]
DR PDB; 4RFX; X-ray; 2.90 A; A/B/C/D/E=412-533.
DR PDBsum; 4RFX; -.
DR SMR; P35458; -.
DR STRING; 9031.ENSGALP00000041577; -.
DR PRIDE; P35458; -.
DR GeneID; 426238; -.
DR KEGG; gga:426238; -.
DR CTD; 1639; -.
DR VEuPathDB; HostDB:geneid_426238; -.
DR InParanoid; P35458; -.
DR OrthoDB; 1550378at2759; -.
DR PhylomeDB; P35458; -.
DR PRO; PR:P35458; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0099738; C:cell cortex region; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR022157; Dynactin.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF12455; Dynactin; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Dynein; Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..1224
FT /note="Dynactin subunit 1"
FT /id="PRO_0000083521"
FT DOMAIN 49..91
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 205..540
FT /evidence="ECO:0000255"
FT COILED 936..1042
FT /evidence="ECO:0000255"
FT COILED 1081..1117
FT /evidence="ECO:0000255"
FT COMPBIAS 120..144
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 435..530
FT /evidence="ECO:0007829|PDB:4RFX"
SQ SEQUENCE 1224 AA; 135565 MW; 03B7FFE68E7C01D7 CRC64;
MAQSRRHPHG RASSAGPRMS TEASSKPLKV GSRVEVIGKG HRGTVAYVGA TLXATGKWVG
VILDEAKGKN DGTVQGRKYF TCEENHGIFV RQSQIQVFED GADTTSPETP ESAALKVPKR
HSRXAAKGSK LRGAKPKKTT ARRPKPTRTP TSAPSSGTAG PSGSASASGG EMSSSEPSTP
AQTPLVAPVI PSPSLTSPVA PMVPSPTKEE ENLRSQVRDL EEKLETLKIK RNEDKAKLKE
LEKYKIQLEQ VQEWKSKMQE QQADLQRRLK EAKKEAKDAL EAKERYMEEM ADTADAIEMA
TLDKEMAEER AESLQQEVDS LKEKVEYLTM DLEILKHEIE EKGSDGAASS YQVKQLEEQN
ARLKEALVRM RDLSASEKQE HVKLQKQMEK KNTELESLRQ QREKLQEEVK QAEKTVDELK
EQVDAALGAE EMVETLTERN LDLEEKVREL RETVGDLEAM NEMNDELQEN ARETELELRE
QLDLAAARVR EAEKRVEAAQ ETVADYQQTI KKYRELTAHL QDVNRELMSQ QEASAEKQQQ
PPPEIFDFKI KFAETKAHAK AIEMELRQME VQQANRHVSL LTSFMPDSFL RHGGDHDCIL
VLLLIPRLIC KADVISKQAQ EKFELNENCT ARAGLRGAAG EQLSFAAGLV YSLSLLQATL
HKYEQALNKC SVEVYKKVGM LYPEMSVHER SLDFLIELLH KDQLDETVNV EPLTKAIKYY
QHLYSIHLAE QAEDCTMQLA DHIKFTQSAL DCMGVEVCRL RAFLQAGQEA SDLAILLKDL
ETSCSDIRQF CKKIRRRMPG TDAPGIPAAL GFGQQVSDTL LDCRKHLTWV VAVLQEVAAA
GAQLIAPLAE NGAAGGEAGG LGLQSQRADL QRSGHQPLRV PAPVLQHPHC HHEQDATAMQ
EGEYDADRPQ SKPTPPAELR AAALRAEITD AEGLGLKLED RETVIKELKK SLKIKGEELS
EANVRLSLLE KKLDSASKDA DDRVEKIQTK LDETQTLLKK KEKEFEETMD ALQADIDQLE
SEKVELKQRL NNQSKRTIEG LRGAPASGVA SIVSGIAGEE QQRGVGAGQA AGGSAGPVQV
KDSPLLLQQI EALQLSIRHL KNENNRLKGA QMKLELAGLK PLQVAKVSLP QSKQGEGPAT
LTLYRKSTQL LETLYQMSTN AKVVDTKQTK SGRSGARLLE QTARLWAMKG SIEALRTRPC
GRWCSSSRAR ASPPASACSP PRPS
