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BICD1_MOUSE
ID   BICD1_MOUSE             Reviewed;         835 AA.
AC   Q8BR07; O55206; Q8BQ18; Q8BRR8; Q8C4D3; Q8CAK6; Q8R2J4; Q8R2J5; Q8R2J6;
AC   Q91YP7;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 133.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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 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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT   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 WITH
RP   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 interacts
RT   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)-independent
CC       Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin
CC       motor complex. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RAB6A. Interacts (via C-terminus) with RAB6B
CC       (GTP-bound); the interaction is direct (By similarity). Interacts with
CC       CLIP-115 and KIFC2. {ECO:0000250, 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       Name=3;
CC         IsoId=Q8BR07-3; Sequence=VSP_007967;
CC       Name=4;
CC         IsoId=Q8BR07-4; Sequence=VSP_007968;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, heart and skeletal muscle.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryonic development.
CC   -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Due to intron retention. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the BicD family. {ECO:0000305}.
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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   PDB; 4YTD; X-ray; 1.50 A; A/B=711-808.
DR   PDBsum; 4YTD; -.
DR   AlphaFoldDB; Q8BR07; -.
DR   SMR; Q8BR07; -.
DR   BioGRID; 198348; 3.
DR   IntAct; Q8BR07; 1.
DR   STRING; 10090.ENSMUSP00000084039; -.
DR   iPTMnet; Q8BR07; -.
DR   PhosphoSitePlus; Q8BR07; -.
DR   MaxQB; Q8BR07; -.
DR   PaxDb; Q8BR07; -.
DR   PRIDE; Q8BR07; -.
DR   ProteomicsDB; 273684; -. [Q8BR07-1]
DR   ProteomicsDB; 273685; -. [Q8BR07-2]
DR   ProteomicsDB; 273686; -. [Q8BR07-3]
DR   ProteomicsDB; 273687; -. [Q8BR07-4]
DR   Antibodypedia; 24706; 65 antibodies from 22 providers.
DR   DNASU; 12121; -.
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   VEuPathDB; HostDB:ENSMUSG00000003452; -.
DR   eggNOG; KOG0999; Eukaryota.
DR   GeneTree; ENSGT00940000154471; -.
DR   HOGENOM; CLU_014107_1_0_1; -.
DR   InParanoid; Q8BR07; -.
DR   OrthoDB; 542877at2759; -.
DR   TreeFam; TF323833; -.
DR   Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   BioGRID-ORCS; 12121; 1 hit in 59 CRISPR screens.
DR   ChiTaRS; Bicd1; mouse.
DR   PRO; PR:Q8BR07; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q8BR07; protein.
DR   Bgee; ENSMUSG00000003452; Expressed in sciatic nerve and 204 other tissues.
DR   ExpressionAtlas; Q8BR07; baseline and differential.
DR   Genevisible; Q8BR07; MM.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
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:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0099503; C:secretory vesicle; ISO:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR   GO; GO:0008093; F:cytoskeletal anchor activity; ISO:MGI.
DR   GO; GO:0034452; F:dynactin binding; ISO:MGI.
DR   GO; GO:0070840; F:dynein complex binding; ISO:MGI.
DR   GO; GO:0045505; F:dynein intermediate chain binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0031871; F:proteinase activated receptor binding; IPI:BHF-UCL.
DR   GO; GO:0031267; F:small 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:1904781; P:positive regulation of protein localization to centrosome; ISO:MGI.
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:0070507; P:regulation of microtubule cytoskeleton organization; 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; BICD.
DR   PANTHER; PTHR31233; PTHR31233; 1.
DR   Pfam; PF09730; BicD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Golgi apparatus;
KW   Reference proteome.
FT   CHAIN           1..835
FT                   /note="Protein bicaudal D homolog 1"
FT                   /id="PRO_0000205358"
FT   REGION          278..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..803
FT                   /note="Interaction with RAB6A"
FT                   /evidence="ECO:0000250"
FT   REGION          800..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..264
FT                   /evidence="ECO:0000255"
FT   COILED          320..519
FT                   /evidence="ECO:0000255"
FT   COILED          663..803
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        567..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         195..210
FT                   /note="EYEGLKHEIKRFEEET -> RLKIFKKLYHRWIHMF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_007965"
FT   VAR_SEQ         211..835
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_007966"
FT   VAR_SEQ         821..835
FT                   /note="IVSSLLPPYRHSAHN -> SGHCPQ (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_007967"
FT   VAR_SEQ         821..835
FT                   /note="IVSSLLPPYRHSAHN -> VSGEAPDTVPTIDTYLLHSQGPQIPTIRVSSGT
FT                   QRKRYACSYCHSVVQCTGFS (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_007968"
FT   CONFLICT        70
FT                   /note="R -> K (in Ref. 4; CAC81709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="D -> N (in Ref. 1; BAC34733)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90
FT                   /note="R -> Q (in Ref. 1; BAC38518)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="E -> K (in Ref. 1; BAC30057)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="H -> D (in Ref. 1; BAC32557)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        470
FT                   /note="E -> K (in Ref. 3; AAB94807)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        632
FT                   /note="I -> V (in Ref. 1; BAC32557)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        796
FT                   /note="D -> G (in Ref. 4; CAC81711)"
FT                   /evidence="ECO:0000305"
FT   HELIX           711..738
FT                   /evidence="ECO:0007829|PDB:4YTD"
FT   HELIX           741..802
FT                   /evidence="ECO:0007829|PDB:4YTD"
FT   HELIX           804..807
FT                   /evidence="ECO:0007829|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
 
 
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