TBCD_MOUSE
ID TBCD_MOUSE Reviewed; 1196 AA.
AC Q8BYA0;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Tubulin-specific chaperone D;
DE AltName: Full=Beta-tubulin cofactor D;
DE AltName: Full=Tubulin-folding cofactor D;
GN Name=Tbcd;
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].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Tubulin-folding protein implicated in the first step of the
CC tubulin folding pathway and required for tubulin complex assembly.
CC Involved in the regulation of microtubule polymerization or
CC depolymerization, it modulates microtubule dynamics by capturing GTP-
CC bound beta-tubulin (TUBB). Its ability to interact with beta tubulin is
CC regulated via its interaction with ARL2. Acts as a GTPase-activating
CC protein (GAP) for ARL2. Induces microtubule disruption in absence of
CC ARL2. Increases degradation of beta tubulin, when overexpressed in
CC polarized cells. Promotes epithelial cell detachment, a process
CC antagonized by ARL2. Induces tight adherens and tight junctions
CC disassembly at the lateral cell membrane. Required for correct assembly
CC and maintenance of the mitotic spindle, and proper progression of
CC mitosis. Involved in neuron morphogenesis.
CC {ECO:0000250|UniProtKB:Q28205, ECO:0000250|UniProtKB:Q9BTW9}.
CC -!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD. Interacts with PPP2CB (By similarity). Part
CC of a supercomplex made of cofactors A to E. Cofactors A and D function
CC by capturing and stabilizing tubulin in a quasi-native conformation.
CC Cofactor E binds to the cofactor D-tubulin complex; interaction with
CC cofactor C then causes the release of tubulin polypeptides that are
CC committed to the native state. Interacts with ARL2; interaction is
CC enhanced with the GDP-bound form of ARL2. Does not interact with ARL3,
CC ARL4A and ARL4D. Interacts with beta tubulin. Interacts with TBCE (By
CC similarity). {ECO:0000250|UniProtKB:Q28205,
CC ECO:0000250|UniProtKB:Q9BTW9}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q28205}. Lateral cell membrane
CC {ECO:0000250|UniProtKB:Q28205}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q28205}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q28205}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9BTW9}.
CC Note=Localized in cell-cell contacts. {ECO:0000250|UniProtKB:Q28205}.
CC -!- SIMILARITY: Belongs to the TBCD 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; AK041464; BAC30951.1; -; mRNA.
DR EMBL; BC059843; AAH59843.1; -; mRNA.
DR CCDS; CCDS25778.1; -.
DR RefSeq; NP_084154.1; NM_029878.3.
DR AlphaFoldDB; Q8BYA0; -.
DR BioGRID; 224462; 19.
DR STRING; 10090.ENSMUSP00000099302; -.
DR iPTMnet; Q8BYA0; -.
DR PhosphoSitePlus; Q8BYA0; -.
DR SwissPalm; Q8BYA0; -.
DR EPD; Q8BYA0; -.
DR MaxQB; Q8BYA0; -.
DR PaxDb; Q8BYA0; -.
DR PeptideAtlas; Q8BYA0; -.
DR PRIDE; Q8BYA0; -.
DR ProteomicsDB; 262948; -.
DR Antibodypedia; 33047; 79 antibodies from 20 providers.
DR DNASU; 108903; -.
DR Ensembl; ENSMUST00000103013; ENSMUSP00000099302; ENSMUSG00000039230.
DR GeneID; 108903; -.
DR KEGG; mmu:108903; -.
DR UCSC; uc007mvy.2; mouse.
DR CTD; 6904; -.
DR MGI; MGI:1919686; Tbcd.
DR VEuPathDB; HostDB:ENSMUSG00000039230; -.
DR eggNOG; KOG1943; Eukaryota.
DR GeneTree; ENSGT00390000017103; -.
DR HOGENOM; CLU_003043_0_0_1; -.
DR InParanoid; Q8BYA0; -.
DR OMA; EPHEAWH; -.
DR OrthoDB; 79003at2759; -.
DR PhylomeDB; Q8BYA0; -.
DR TreeFam; TF105754; -.
DR BioGRID-ORCS; 108903; 25 hits in 76 CRISPR screens.
DR ChiTaRS; Tbcd; mouse.
DR PRO; PR:Q8BYA0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BYA0; protein.
DR Bgee; ENSMUSG00000039230; Expressed in epithelium of lens and 245 other tissues.
DR ExpressionAtlas; Q8BYA0; baseline and differential.
DR Genevisible; Q8BYA0; MM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR GO; GO:0007021; P:tubulin complex assembly; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033162; TBCD.
DR InterPro; IPR022577; Tubulin_specific_chaperoneD_C.
DR PANTHER; PTHR12658; PTHR12658; 1.
DR Pfam; PF12612; TFCD_C; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Chaperone; Cytoplasm; Cytoskeleton;
KW GTPase activation; Membrane; Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1196
FT /note="Tubulin-specific chaperone D"
FT /id="PRO_0000080050"
FT REPEAT 363..401
FT /note="HEAT 1"
FT REPEAT 599..634
FT /note="HEAT 2"
FT REPEAT 752..788
FT /note="HEAT 3"
FT REPEAT 1106..1142
FT /note="HEAT 4"
SQ SEQUENCE 1196 AA; 133321 MW; 5439133B4CD54938 CRC64;
MVLSNEPAAS AAEEEVEDDA LVRASALEAF GESAETRALL RSLPAVHRER ASREVAEERF
RVIMDKYQEQ PHLLDPHLEW MMNSLLDLVQ DETSLPDLVH LAFKFLYIIT KVRGYKVFLR
LFPHEVANVQ PVLDMFTGQN PKDHETWETR YMLLLWLSVT CLIPFDFSRL DGNLSTQTGE
TRVPTMDRIL QIAESYLVVS DKARDAAAVL VSKFITRPDV KQRKMASFLD WSLCTLAHSS
FQTIEGVITM DGMLQALAQI FKHGKREDCL PYANTVLQCL DGCRLPESSH TSLRKLGVKL
VQRLGLTFLK PKVATWRYQR GCRSLAANLK LCAPGKSDQK LLSDSLTSDG DEDYDVPEGV
ETVIEQLLVG LKDKDTVVRW SAAKGIGRMA GRLPRELADD VVGSVLDCFS FQETDKAWHG
GCLALAELGR RGLLLPSRLS EVVTVILKAL TYDEKRGACS VGANVRDAAC YVCWAFARAY
EPQELTPFVT AISSALVIAA VFDRNVNCRR AASAAFQENV GRQGTFPHGI DILTTADYFA
VGNISNCFLI ISVFIAGFQE YTKPMIDHLV SMKINHWDGA IRELSAKALH NLTPQVPEYI
AMHVFPALLL MTQSPDLHTR HGAILACAEV TYALYKLATQ SNRLVTDYLD EKAVQSLKQI
HQQLCDRHLY RGLGGELMRQ AVCILIEKLS LSRMPFKGDA TVEGWQWLIN DTLRSLHLVS
SHSRQQIKEV AVSALTALCS EYYVKEPGEA GSSIAKELIP QYLAELQSPE EMARCGFSSA
LGALPGFLLR GHLQQVLSGL RRVTCISPND VSFAEARRDG LKAISRICQT VGVNTRGPPD
EVICKENISE VYAALLGCMS DYTTDSRGDV GAWVREAAMT SLMDLMLLLA RTEPVLIEAH
ICERVMCCVA QQASEKIDRF RAHAARVFLT LLHFDSPPIP HVPHRQELES LFPRSDVATV
NWNAPSQAFP LITQLLGLPT YRYHVLLGLA VSVGGLTEST VRHSTQSLFE YMKGIQKDAQ
VLQSFSETLL KVFEDNLLND RVSVSLLKML DQLLANGCFD IFTAEENHPF CVKLLTLCKE
EIKKSKDIQK LRSSIAVLCG MVQFNGDVRK KILLQLFLLL GHPFPVIRKS TASQVYEMVL
TYSDLVDAEV LDEVMSVLSD TAWDAELPVV REQRNRLCDL LGVPRPQLVP KPIPGS
