ID BICD1_MOUSE Reviewed; 835 AA. AC Q8BR07; O55206; Q8BQ18; Q8BRR8; Q8C4D3; Q8CAK6; Q8R2J4; Q8R2J5; AC Q8R2J6; Q91YP7; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 15-AUG-2003, sequence version 2. DT 16-SEP-2015, entry version 99. DE RecName: Full=Protein bicaudal D homolog 1; DE Short=Bic-D 1; GN Name=Bicd1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; RC TISSUE=Brain, Brain cortex, Cerebellum, Hypothalamus, and RC Spinal ganglion; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 231-775 (ISOFORM 1). RX PubMed=9367685; DOI=10.1006/geno.1997.4971; RA Baens M., Marynen P.; RT "A human homologue (BICD1) of the Drosophila bicaudal-D gene."; RL Genomics 45:601-606(1997). RN [4] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), INTERACTION RP WITH CLIP-115 AND KIFC2, AND SUBCELLULAR LOCATION. RA Hoogenraad C.C., Akhmanova A., Galjart N.; RT "Mammalian BicD is a Golgi-associated protein that transiently RT interacts with the neuronal proteins CLIP-115 and KIFC2."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Regulates coat complex coatomer protein I (COPI)- CC independent Golgi-endoplasmic reticulum transport by recruiting CC the dynein-dynactin motor complex. {ECO:0000250}. CC -!- SUBUNIT: Interacts with RAB6A. Interacts (via C-terminus) with CC RAB6B (GTP-bound); the interaction is direct (By similarity). CC Interacts with CLIP-115 and KIFC2. {ECO:0000250, CC ECO:0000269|Ref.4}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|Ref.4}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8BR07-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BR07-2; Sequence=VSP_007965, VSP_007966; CC Note=Due to intron retention.; CC Name=3; CC IsoId=Q8BR07-3; Sequence=VSP_007967; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=Q8BR07-4; Sequence=VSP_007968; CC Note=Due to intron retention. Contains a phosphoserine at CC position 865 (By similarity). {ECO:0000250}; CC -!- TISSUE SPECIFICITY: Expressed in the brain, heart and skeletal CC muscle. CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development. CC -!- PTM: Isoform 4 is phosphorylated on Ser-865. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the BicD family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK038585; BAC30057.1; -; mRNA. DR EMBL; AK043650; BAC31607.1; -; mRNA. DR EMBL; AK045975; BAC32557.1; -; mRNA. DR EMBL; AK051718; BAC34733.1; -; mRNA. DR EMBL; AK082523; BAC38518.1; -; mRNA. DR EMBL; BC016192; AAH16192.1; -; mRNA. DR EMBL; U90029; AAB94807.1; -; mRNA. DR EMBL; AJ288054; CAC81709.1; -; mRNA. DR EMBL; AJ288055; CAC81710.1; -; mRNA. DR EMBL; AJ288056; CAC81711.1; -; mRNA. DR CCDS; CCDS39723.1; -. [Q8BR07-1] DR CCDS; CCDS51962.1; -. [Q8BR07-3] DR RefSeq; NP_001106267.1; NM_001112796.2. [Q8BR07-3] DR RefSeq; NP_033883.2; NM_009753.4. [Q8BR07-1] DR UniGene; Mm.177181; -. DR UniGene; Mm.260763; -. DR PDB; 4YTD; X-ray; 1.50 A; A/B=711-808. DR PDBsum; 4YTD; -. DR ProteinModelPortal; Q8BR07; -. DR SMR; Q8BR07; 711-808. DR STRING; 10090.ENSMUSP00000084039; -. DR PhosphoSite; Q8BR07; -. DR MaxQB; Q8BR07; -. DR PaxDb; Q8BR07; -. DR PRIDE; Q8BR07; -. DR Ensembl; ENSMUST00000086829; ENSMUSP00000084039; ENSMUSG00000003452. [Q8BR07-1] DR Ensembl; ENSMUST00000111513; ENSMUSP00000107138; ENSMUSG00000003452. [Q8BR07-3] DR GeneID; 12121; -. DR KEGG; mmu:12121; -. DR UCSC; uc009eug.3; mouse. [Q8BR07-2] DR UCSC; uc009euh.3; mouse. [Q8BR07-1] DR UCSC; uc009eui.3; mouse. [Q8BR07-3] DR CTD; 636; -. DR MGI; MGI:1101760; Bicd1. DR eggNOG; NOG291306; -. DR GeneTree; ENSGT00390000004114; -. DR HOVERGEN; HBG050686; -. DR InParanoid; Q8BR07; -. DR KO; K18739; -. DR OrthoDB; EOG7BZVRK; -. DR TreeFam; TF323833; -. DR NextBio; 280435; -. DR PRO; PR:Q8BR07; -. DR Proteomes; UP000000589; Chromosome 6. DR Bgee; Q8BR07; -. DR CleanEx; MM_BICD1; -. DR ExpressionAtlas; Q8BR07; baseline and differential. DR Genevisible; Q8BR07; MM. DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0072517; C:host cell viral assembly compartment; ISO:MGI. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI. DR GO; GO:0008093; F:cytoskeletal adaptor activity; ISO:MGI. DR GO; GO:0034452; F:dynactin binding; ISO:MGI. DR GO; GO:0045502; F:dynein binding; ISO:MGI. DR GO; GO:0031871; F:proteinase activated receptor binding; IPI:BHF-UCL. DR GO; GO:0017137; F:Rab GTPase binding; ISO:MGI. DR GO; GO:0072393; P:microtubule anchoring at microtubule organizing center; IMP:BHF-UCL. DR GO; GO:0072385; P:minus-end-directed organelle transport along microtubule; ISO:MGI. DR GO; GO:1900275; P:negative regulation of phospholipase C activity; IDA:BHF-UCL. DR GO; GO:1900737; P:negative regulation of phospholipase C-activating G-protein coupled receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:MGI. DR GO; GO:0033365; P:protein localization to organelle; ISO:MGI. DR GO; GO:1900276; P:regulation of proteinase activated receptor activity; IDA:BHF-UCL. DR GO; GO:0034063; P:stress granule assembly; IMP:BHF-UCL. DR GO; GO:0016032; P:viral process; ISO:MGI. DR InterPro; IPR018477; Bicaudal-D_microtubule-assoc. DR PANTHER; PTHR31233; PTHR31233; 1. DR Pfam; PF09730; BicD; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome; KW Golgi apparatus; Phosphoprotein; Reference proteome. FT CHAIN 1 835 Protein bicaudal D homolog 1. FT /FTId=PRO_0000205358. FT REGION 663 803 Interacts with RAB6A. {ECO:0000250}. FT COILED 1 264 {ECO:0000255}. FT COILED 320 519 {ECO:0000255}. FT COILED 663 803 {ECO:0000255}. FT VAR_SEQ 195 210 EYEGLKHEIKRFEEET -> RLKIFKKLYHRWIHMF (in FT isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_007965. FT VAR_SEQ 211 835 Missing (in isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_007966. FT VAR_SEQ 821 835 IVSSLLPPYRHSAHN -> SGHCPQ (in isoform 3). FT {ECO:0000305}. FT /FTId=VSP_007967. FT VAR_SEQ 821 835 IVSSLLPPYRHSAHN -> VSGEAPDTVPTIDTYLLHSQGP FT QIPTIRVSSGTQRKRYACSYCHSVVQCTGFS (in FT isoform 4). {ECO:0000305}. FT /FTId=VSP_007968. FT CONFLICT 70 70 R -> K (in Ref. 4; CAC81709). FT {ECO:0000305}. FT CONFLICT 86 86 D -> N (in Ref. 1; BAC34733). FT {ECO:0000305}. FT CONFLICT 90 90 R -> Q (in Ref. 1; BAC38518). FT {ECO:0000305}. FT CONFLICT 111 111 E -> K (in Ref. 1; BAC30057). FT {ECO:0000305}. FT CONFLICT 312 312 H -> D (in Ref. 1; BAC32557). FT {ECO:0000305}. FT CONFLICT 470 470 E -> K (in Ref. 3; AAB94807). FT {ECO:0000305}. FT CONFLICT 632 632 I -> V (in Ref. 1; BAC32557). FT {ECO:0000305}. FT CONFLICT 796 796 D -> G (in Ref. 4; CAC81711). FT {ECO:0000305}. FT HELIX 711 738 {ECO:0000244|PDB:4YTD}. FT HELIX 741 802 {ECO:0000244|PDB:4YTD}. FT HELIX 804 807 {ECO:0000244|PDB:4YTD}. SQ SEQUENCE 835 AA; 95896 MW; 33E8D83C56077C40 CRC64; MAAEEALKTV DQYKTEIERL TKELTETTHE KIQAAEYGLV VLEEKLTLKQ QYDELEAEYD GLKQELEQLR EAFGQSFSIH RKVAEDGETR EETLLQESAS KEAYYLNKIL EMQNELKQSR AVVTNVQAEN ERLSAVVQEL KENNEMVELQ RIRMKDEIRE YKFREARLLQ DYTELEEENI TLQKLVSTLK QNQVEYEGLK HEIKRFEEET VLLNSQLEDA IRLKEIAEHQ LEEALETLKN EREQKNNLRK ELSQYINLSD SHISISVDGL KFAEDGSEPN NDDKMNGHIH GPLGKLNGDY RTPTTRKGES LHPVSDLFSE LNISEIQKLK QQLIQVEREK AILLANLQES QTQLEHTKGA LTEQHERVHR LTEHVNAMRG LQNSKEIKAE LDCEKGRNSA EEAHDYEVDI NGLEILECKY RVAVTEVIDL KAEIKALKEK YNKSVENYTE EKTKYESKIQ MYDEQVTNLE KTSKESGEKM AHMEKELQKM TGIANENHNT LNTAQDELVT FSEELAQLYH HVCLCNNETP NRVMLDYYRQ SRVTRSGSLK GPDDPRGLLS PRLSRRGVSS PVESRTSSEP VSKENTETSK EPSPTKTPTI SPVITAPPSS PVLDTSDIRK EPMNIYNLNA IIRDQIKHLQ KAVDRSLQLS RQRAAARELA PMIDKDKEAL MEEILKLKSL LSTKREQIAT LRAVLKANKQ TAEVALANLK NKYENEKAMV TETMTKLRNE LKALKEDAAT FSSLRAMFAT RCDEYVTQLD EMQRQLAAAE DEKKTLNTLL RMAIQQKLAL TQRLEDLEFD HEQSRRSKGK LGKSKIGSPK IVSSLLPPYR HSAHN //