ID DCTN1_MOUSE Reviewed; 1281 AA. AC O08788; Q3TZG7; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 2. DT 22-JUL-2008, entry version 58. 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 Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; RX MEDLINE=97223454; PubMed=9070275; DOI=10.1006/bbrc.1997.6095; RA Jang W., Weber J.S., Tokito M.K., Holzbaur E.L., Meisler M.H.; RT "Mouse p150Glued (dynactin 1) cDNA sequence and evaluation as a RT candidate for the neuromuscular disease mutation mnd2."; RL Biochem. Biophys. Res. Commun. 231:344-347(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Inner ear; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=17203969; DOI=10.1021/pr0604155; RA Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; RT "Protein phosphorylation and expression profiling by Yin-yang RT multidimensional liquid chromatography (Yin-yang MDLC) mass RT spectrometry."; RL J. Proteome Res. 6:250-262(2007). CC -!- FUNCTION: Required for the cytoplasmic dynein-driven retrograde CC movement of vesicles and organelles along microtubules. Dynein- CC dynactin interaction is a key component of the mechanism of axonal CC transport of vesicles and organelles. CC -!- SUBUNIT: Large macromolecular complex of at least 10 components; CC p150(glued) binds directly to microtubules and to cytoplasmic CC dynein. Interacts with the C-terminus of MAPRE1, MAPRE2 and MAPRE3 CC (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O08788-1; Sequence=Displayed; CC Name=2; CC IsoId=O08788-2; Sequence=VSP_029584; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family. CC -!- SIMILARITY: Contains 1 CAP-Gly domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U60312; AAB57773.1; -; mRNA. DR EMBL; AK157867; BAE34241.1; -; mRNA. DR PIR; JC5368; JC5368. DR UniGene; Mm.6919; -. DR HSSP; Q20728; 1LPL. DR SMR; O08788; 1-104. DR IntAct; O08788; -. DR PhosphoSite; O08788; -. DR Ensembl; ENSMUSG00000031865; Mus musculus. DR MGI; MGI:107745; Dctn1. DR HOGENOM; O08788; -. DR HOVERGEN; O08788; -. DR ArrayExpress; O08788; -. DR CleanEx; MM_DCTN1; -. DR GermOnline; ENSMUSG00000031865; Mus musculus. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR InterPro; IPR000938; Cytoskel-assoc-prot_CAP-Gly. DR Pfam; PF01302; CAP_GLY; 1. DR PROSITE; PS00845; CAP_GLY_1; 1. DR PROSITE; PS50245; CAP_GLY_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Dynein; KW Microtubule; Motor protein; Phosphoprotein. FT CHAIN 1 1281 Dynactin subunit 1. FT /FTId=PRO_0000083519. FT DOMAIN 48 90 CAP-Gly. FT COILED 214 547 Potential. FT COILED 943 1049 Potential. FT COILED 1185 1214 Potential. FT COMPBIAS 157 184 Ser-rich. FT MOD_RES 541 541 Phosphoserine. FT VAR_SEQ 1049 1086 Missing (in isoform 2). FT /FTId=VSP_029584. FT CONFLICT 406 406 W -> R (in Ref. 1; AAB57773). FT CONFLICT 721 723 TKA -> NKG (in Ref. 1; AAB57773). FT CONFLICT 732 732 S -> R (in Ref. 1; AAB57773). FT CONFLICT 1202 1202 V -> I (in Ref. 1; AAB57773). SQ SEQUENCE 1281 AA; 141692 MW; 7DE78A105DE38C4C CRC64; MAQSRRHMSS RTPSGSRMST EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG ADTTSPETPD SSASKVLKRE GADAAAKTSK LRGLKPKKAP TARKTTTRRP KPTRPASTGV AGPSSSLGPS GSASAGELSS SEPSTPAQTP LAAPIIPTPA LTSPGAAPPL PSPSKEEEGL RAQVRDLEEK LETLRLKRSE DKAKLKELEK HKIQLEQVQE WKSKMQEQQA DLQRRLKEAR KEAKEALEAK ERYMEEMADT ADAIEMATLD KEMAEERAES LQQEVEALKE RVDELTTDLE ILKAEIEEKG SDGAASSYQL KQLEEQNARL KDALVRMRDL SSSEKQEHVK LQKLMEKKNQ ELEVVWQQRE RLQEELSQAE STIDELKEQV DAALGAEEMV EMLTDRNLNL EEKVRELRET VGDLEAMNEM NDELQENARE TELELREQLD MAGARVREAQ KRVEAAQETV ADYQQTIKKY RQLTAHLQDV NRELTNQQEA SVERQQQPPP ETFDFKIKFA ETKAHAKAIE MELRQMEVAQ ANRHMSLLTA FMPDSFLRPG GDHDCVLVLL LMPRLICKAE LIRKQAQEKF DLSENCSERP GLRGAAGEQL SFAAGLVYSL SLLQATLHRY EHALSQCSVD VYKKVGSLYP EMSAHERSLD FLIELLHKDQ LDETVNVEPL TKAIKYYQHL YSIHLAEQPE DSTMQLADHI KFTQSALDCM GVEVGRLRAF LQGGQEATDI ALLLRDLETS CSDTRQFCKK IRRRMPGTDA PGIPAALAFG SQVSDTLLDC RKHLTWVVAV LQEVAAAAAQ LIAPLAENEG LPVAALEELA FKASEQIYGS PSSSPYECLR QSCTILISTM NKLATAMQEG EYDAERPPSK PPPVELRAAA LRAEITDAEG LGLKLEDRET VIKELKKSLK IKGEELSEAN VRLSLLEKKL DSAAKDADER IEKVQTRLDE TQTLLRKKEK DFEETMDALQ ADIDQLEAEK AELKQRLNSQ SKRTIEGLRG PPPSGIATLV SGIAGEEPQR GGAPGQAPGA LPGPGLVKDS PLLLQQISAM RLHISQLQHE NSILRGAQMK ASLAALPPLH VAKLSLPPHE GPGGNLVAGA LYRKTSQLLE KLNQLSTHTH VVDITRSSPA AKSPSAQLME QVAQLKSLSD TVEKLKDEVL KETVTQRPGA TVPTDFATFP SSAFLRAKEE QQDDTVYMGK VTFSCAAGLG QRHRLVLTQE QLHQLHSRLI S //