DCTN1_DROME
ID DCTN1_DROME Reviewed; 1265 AA.
AC P13496; B5X0J0; Q8MT52; Q9VUA1;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Dynactin subunit 1;
DE AltName: Full=150 kDa dynein-associated polypeptide;
DE Short=DAP-150;
DE Short=DP-150;
DE AltName: Full=Dynactin 1 subunit p150 {ECO:0000312|FlyBase:FBgn0001108};
DE AltName: Full=Protein glued {ECO:0000303|PubMed:2819881};
GN Name=DCTN1-p150 {ECO:0000312|FlyBase:FBgn0001108};
GN Synonyms=Gl {ECO:0000312|FlyBase:FBgn0001108};
GN ORFNames=CG9206 {ECO:0000312|FlyBase:FBgn0001108};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S, and Oregon-R;
RX PubMed=2819881; DOI=10.1073/pnas.84.18.6501;
RA Swaroop A., Swaroop M., Garen A.;
RT "Sequence analysis of the complete cDNA and encoded polypeptide for the
RT Glued gene of Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6501-6505(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-110; SER-114;
RP SER-117; SER-121; SER-183 AND SER-1117, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required for the cytoplasmic dynein-driven retrograde
CC movement of vesicles and organelles along microtubules. Dynein-dynactin
CC interaction is a key component of the mechanism of axonal transport of
CC vesicles and organelles.
CC -!- SUBUNIT: Large macromolecular complex of at least 10 components;
CC p150(glued) binds directly to microtubules and to cytoplasmic dynein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=J02932; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J02932; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AE014296; AAF49788.1; -; Genomic_DNA.
DR EMBL; AY118377; AAM48406.1; -; mRNA.
DR EMBL; BT044559; ACI15754.1; -; mRNA.
DR PIR; A28313; A28313.
DR RefSeq; NP_524061.1; NM_079337.3.
DR AlphaFoldDB; P13496; -.
DR SMR; P13496; -.
DR BioGRID; 64877; 55.
DR DIP; DIP-21099N; -.
DR IntAct; P13496; 6.
DR STRING; 7227.FBpp0075498; -.
DR iPTMnet; P13496; -.
DR PaxDb; P13496; -.
DR PRIDE; P13496; -.
DR DNASU; 39536; -.
DR EnsemblMetazoa; FBtr0075756; FBpp0075498; FBgn0001108.
DR GeneID; 39536; -.
DR KEGG; dme:Dmel_CG9206; -.
DR UCSC; CG9206-RA; d. melanogaster.
DR CTD; 39536; -.
DR FlyBase; FBgn0001108; DCTN1-p150.
DR VEuPathDB; VectorBase:FBgn0001108; -.
DR eggNOG; KOG0971; Eukaryota.
DR GeneTree; ENSGT00940000155378; -.
DR HOGENOM; CLU_002523_0_1_1; -.
DR InParanoid; P13496; -.
DR OMA; ADKNMRY; -.
DR OrthoDB; 1550378at2759; -.
DR PhylomeDB; P13496; -.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR SignaLink; P13496; -.
DR BioGRID-ORCS; 39536; 0 hits in 1 CRISPR screen.
DR ChiTaRS; DCTN1-p150; fly.
DR GenomeRNAi; 39536; -.
DR PRO; PR:P13496; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001108; Expressed in second segment of antenna (Drosophila) and 24 other tissues.
DR Genevisible; P13496; DM.
DR GO; GO:0005818; C:aster; IDA:FlyBase.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:1904115; C:axon cytoplasm; IDA:FlyBase.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061803; C:posterior cell cortex; IDA:FlyBase.
DR GO; GO:0005876; C:spindle microtubule; IDA:FlyBase.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0061176; C:type Ib terminal bouton; IDA:FlyBase.
DR GO; GO:0070840; F:dynein complex binding; IDA:FlyBase.
DR GO; GO:0045505; F:dynein intermediate chain binding; IPI:FlyBase.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0048675; P:axon extension; IGI:FlyBase.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IMP:FlyBase.
DR GO; GO:0001709; P:cell fate determination; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IGI:FlyBase.
DR GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR GO; GO:0051299; P:centrosome separation; IMP:FlyBase.
DR GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IDA:FlyBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0061670; P:evoked neurotransmitter secretion; IMP:FlyBase.
DR GO; GO:0001754; P:eye photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IMP:FlyBase.
DR GO; GO:0051383; P:kinetochore organization; IMP:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:UniProtKB.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:FlyBase.
DR GO; GO:0051028; P:mRNA transport; IMP:FlyBase.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:FlyBase.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:FlyBase.
DR GO; GO:0008090; P:retrograde axonal transport; IMP:FlyBase.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; IMP:FlyBase.
DR GO; GO:0048491; P:retrograde synaptic vesicle transport; IDA:FlyBase.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR GO; GO:0016330; P:second mitotic wave involved in compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IGI:FlyBase.
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 Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1265
FT /note="Dynactin subunit 1"
FT /id="PRO_0000083523"
FT DOMAIN 27..69
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 81..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 213..570
FT /evidence="ECO:0000255"
FT COILED 812..836
FT /evidence="ECO:0000255"
FT COILED 967..1084
FT /evidence="ECO:0000255"
FT COILED 1128..1160
FT /evidence="ECO:0000255"
FT COMPBIAS 88..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 708
FT /note="D -> A (in Ref. 1; J02932)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="S -> P (in Ref. 4; AAM48406)"
FT /evidence="ECO:0000305"
FT CONFLICT 875
FT /note="L -> V (in Ref. 1; J02932)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="A -> R (in Ref. 1; J02932)"
FT /evidence="ECO:0000305"
FT CONFLICT 1043
FT /note="S -> C (in Ref. 1; J02932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1265 AA; 141218 MW; 2038A200282B2755 CRC64;
MSEKNLKVGA RVELTGKDLL GTVAYVGMTS FAVGKWVGVV LDEPKGKNSG SIKGQQYFQC
DENCGMFVRP TQLRLLEAAP GSRRSIEDVS GATPTAAQPT KARLSSSRTS LSSSRQSLLG
SRTQLTTSLS ERTASSSSIG PRKSLAPQNS KDKESPSTSL AEGAPAASGG NGAASHASSK
RASFVETGFL EILKPQFTPS QPLRSPSFTM PSNSGAEDKV ALLEAQKTSA ELQAQLADLT
EKLETLKQRR NEDKERLREF DKMKIQFEQL QEFRTKIMGA QASLQKELLR AKQEAKDAIE
AKEQHAQEMA DLADNVEMIT LDKEMAEEKA DTLQLELESS KERIEELEVD LELLRSEMQN
KAESAIGNIS GGGDSPGLST YEFKQLEQQN IRLKETLVRL RDLSAHDKHD IQKLSKELEM
KRSEVTELER TKEKLSAKID ELEAIVADLQ EQVDAALGAE EMVEQLAEKK MELEDKVKLL
EEEIAQLEAL EEVHEQLVES NHELELDLRE ELDLANGAKK EVLRERDAAI ETIYDRDQTI
VKFRELVQKL NDQLTELRDR NSSNEKESLQ DPSLKMVTET IDYKQMFAES KAYTRAIDVQ
LRQIELSQAN EHVQMLTAFM PESFMSRGGD HDSILVILLI SRIVFKCDIV VSQTRERFPP
VDAITREAVT QGHAVQQYAF KCRLLHYVHS LQCALHQILY GLNSCQPDTL LRAGSSLPEM
VAQEKIVDGI IELLKSNQLD ENSTTDNIEK CVAFFNAMNS VLLAGEQLLN EIQMIRDCVA
SLGAACESIL SDTAIAKVII QEAGATSDSV LLIQFLNENM ESVRQQVKLI KRRLPSDQHV
IKSGLSQHKV EAMRGLAQNI SRIMSAMHQA TKQSLAAIVS TIESDNAAEH TLPQEKYWAL
LTASCERIYE QDDRGPTQNF KTLLAQANSD LQLIAQHLLD KEYDIISAAN NASNQQKSGA
HSTPITQRAQ LIKKQLEQKN VLAATLENRE ADVKQLKVAA KMKQNELSEM QIRKDLAEKK
LSVLQNEYEH AVDKWKQKYE ETSLQLQLKE KEFEETMDHL QSDIDALESE KSDLRDKLKL
NSTTGKVQPG SESHSPHNIS LSGNTSTAPG ISNVSYSAPA GTAPVVAEEV ELLKNAFNQE
RNQRLRLQAQ DMRAKLSQFE PLHVPQPQDQ RITALESELT RMKHAWVLSL LQVRSQDSVN
SGTRIDAVAL QRRNQPVPLK GEISSKASQL ASDILTEYLQ RKPHRATHGQ FASFPTVDVK
RVLQI
