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TBCE_DROME
ID   TBCE_DROME              Reviewed;         523 AA.
AC   A1Z6J5; A1Z6J4; Q8MT85;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Tubulin-specific chaperone E {ECO:0000303|PubMed:19297412};
DE   AltName: Full=Tubulin-folding cofactor E {ECO:0000305};
GN   Name=Tbce {ECO:0000303|PubMed:19297412, ECO:0000312|FlyBase:FBgn0033055};
GN   ORFNames=CG7861 {ECO:0000312|FlyBase:FBgn0033055};
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 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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   [2] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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   [3] {ECO:0000312|EMBL:AAM48343.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAM48343.1};
RC   TISSUE=Ovary {ECO:0000312|EMBL:AAM48343.1};
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   [4] {ECO:0000312|EMBL:ACH92265.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:ACH92265.1};
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=19297412; DOI=10.1242/dev.029983;
RA   Jin S., Pan L., Liu Z., Wang Q., Xu Z., Zhang Y.Q.;
RT   "Drosophila Tubulin-specific chaperone E functions at neuromuscular
RT   synapses and is required for microtubule network formation.";
RL   Development 136:1571-1581(2009).
CC   -!- FUNCTION: Tubulin-folding protein which is required for the development
CC       of the neuronal microtubule network. Essential for the development and
CC       function of neuromuscular synapses. Likely to promote microtubule
CC       formation by acting in the negative regulation of the microtubule-
CC       severing protein spas. {ECO:0000269|PubMed:19297412}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19297412}.
CC   -!- DEVELOPMENTAL STAGE: In embryos, expressed ubiquitously with higher
CC       expression levels in the central nervous system and muscles (at protein
CC       level). Expression levels decrease from the embryonic to larval stage
CC       (at protein level). In third-stage larva, high levels of expression in
CC       the epidermal cells with lower levels of expression in the muscles,
CC       central neurons and peripheral axons (at protein level).
CC       {ECO:0000269|PubMed:19297412}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethal, with a few escapers that
CC       develop to first-instar larvae. In larval muscles the microtubule (MT)
CC       network is greatly reduced with a decrease in the number and length of
CC       MT fibers. RNAi-mediated knockdown in larval neurons and muscles
CC       results in a significant increase in roll-over time. RNAi-mediated
CC       knockdown in pre- and post-synaptic neurons results in increased
CC       branching number, increased bouton number and decreased bouton size at
CC       the neuromuscular junction (NMJ) synaptic terminals. Presynaptic
CC       knockdown also results in increased excitatory junction potentials
CC       (EJPs) and miniature excitatory junction potentials (mEJPs) of NMJ
CC       synapses, whereas knockdown in postsynaptic neurons has no effect on
CC       neurotransmission parameters. {ECO:0000269|PubMed:19297412}.
CC   -!- SIMILARITY: Belongs to the TBCE family. {ECO:0000305}.
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DR   EMBL; AE013599; AAF57288.3; -; Genomic_DNA.
DR   EMBL; AE013599; AAS64773.1; -; Genomic_DNA.
DR   EMBL; AY118314; AAM48343.1; -; mRNA.
DR   EMBL; BT044200; ACH92265.1; -; mRNA.
DR   RefSeq; NP_610197.2; NM_136353.2.
DR   RefSeq; NP_995747.1; NM_206025.2.
DR   AlphaFoldDB; A1Z6J5; -.
DR   SMR; A1Z6J5; -.
DR   IntAct; A1Z6J5; 1.
DR   STRING; 7227.FBpp0085327; -.
DR   PaxDb; A1Z6J5; -.
DR   PRIDE; A1Z6J5; -.
DR   DNASU; 35532; -.
DR   EnsemblMetazoa; FBtr0085974; FBpp0085327; FBgn0033055.
DR   EnsemblMetazoa; FBtr0335286; FBpp0307274; FBgn0033055.
DR   GeneID; 35532; -.
DR   KEGG; dme:Dmel_CG7861; -.
DR   UCSC; CG7861-RA; d. melanogaster.
DR   UCSC; CG7861-RB; d. melanogaster.
DR   CTD; 6905; -.
DR   FlyBase; FBgn0033055; Tbce.
DR   VEuPathDB; VectorBase:FBgn0033055; -.
DR   eggNOG; KOG3207; Eukaryota.
DR   GeneTree; ENSGT00530000063405; -.
DR   HOGENOM; CLU_017716_5_0_1; -.
DR   OMA; KKYALDW; -.
DR   OrthoDB; 249920at2759; -.
DR   PhylomeDB; A1Z6J5; -.
DR   BioGRID-ORCS; 35532; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 35532; -.
DR   PRO; PR:A1Z6J5; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0033055; Expressed in embryonic/larval hemocyte (Drosophila) and 23 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0046785; P:microtubule polymerization; IMP:FlyBase.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IBA:GO_Central.
DR   GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR   GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR   CDD; cd17044; Ubl_TBCE; 1.
DR   Gene3D; 2.30.30.190; -; 1.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR044994; TBCE.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR044079; Ubl_TBCE.
DR   PANTHER; PTHR15140; PTHR15140; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   SUPFAM; SSF74924; SSF74924; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cytoplasm; Leucine-rich repeat; Neurogenesis;
KW   Reference proteome; Repeat.
FT   CHAIN           1..523
FT                   /note="Tubulin-specific chaperone E"
FT                   /id="PRO_0000439453"
FT   DOMAIN          31..75
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT   REPEAT          155..180
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          181..204
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          209..232
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          235..258
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          260..284
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          285..310
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          315..337
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        103
FT                   /note="E -> V (in Ref. 3; AAM48343)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   523 AA;  59424 MW;  814DF349F33D53FD CRC64;
     MVGIIDEVQL FYPLGTRIKI GDNYGTVRYV GEVSGHMGSW LGIEWDDGLR GKHNGIVDGK
     RYFQTQTPTG GSFIRPGKVG PCATLEDAAR ERYLNYDSSN VDESLIREAQ ASLQASLFEV
     VGMDKIARKQ SKFEQLEEVS VDQTPVNAAG YLKELTHLTT LNVSHTLIWN WEIVASIAQQ
     LPSLTNLNLS SNRLVLPTSS QITELEPSFR QLKRINLRSC GFSDWKDVMH TALLWPNILS
     LGLQENSLGQ LAEVDRTKIF KQLHELDLHR TNIMDFDQVT KLGNLTTLRL LNIMENGIEE
     IKLPDCDSQE KLNIFVSLEQ LNLLHNPIWN EADAFNELDK LPQLKRLSKT PHLKSNFDEM
     FSKAVASIAS LQFINKAEVT AEQRRGAEYD IWKKYALDWM QATQGGTDSL REFCRRHRTY
     PLLVKKYGSP ADFVPRSQAK QSNLINVSIR HQLTGETWEK KVPRMITVQT LQGLVMKRFR
     LSGDVPQLCY VDALHPDLVV PLDNNAKTLD FYSVQEHDTV LVQ
 
 
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