TBCD_BOVIN
ID TBCD_BOVIN Reviewed; 1199 AA.
AC Q28205;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8706133; DOI=10.1016/s0092-8674(00)80100-2;
RA Tian G., Huang Y., Rommelaere H., Vandekerckhove J., Ampe C., Cowan N.J.;
RT "Pathway leading to correctly folded beta-tubulin.";
RL Cell 86:287-296(1996).
RN [2]
RP INTERACTION WITH PPP2CB, AND IDENTIFICATION IN A COMPLEX WITH ARL2; PPP2CB;
RP PPP2R2A; PPP2R5E AND TBCD.
RX PubMed=12912990; DOI=10.1074/jbc.m308678200;
RA Shern J.F., Sharer J.D., Pallas D.C., Bartolini F., Cowan N.J., Reed M.S.,
RA Pohl J., Kahn R.A.;
RT "Cytosolic Arl2 is complexed with cofactor D and protein phosphatase 2A.";
RL J. Biol. Chem. 278:40829-40836(2003).
RN [3]
RP FUNCTION, INTERACTION WITH ARL2, AND SUBCELLULAR LOCATION.
RX PubMed=17704193; DOI=10.1096/fj.06-7786com;
RA Shultz T., Shmuel M., Hyman T., Altschuler Y.;
RT "Beta-tubulin cofactor D and ARL2 take part in apical junctional complex
RT disassembly and abrogate epithelial structure.";
RL FASEB J. 22:168-182(2008).
RN [4]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20740604; DOI=10.1002/cm.20480;
RA Tian G., Thomas S., Cowan N.J.;
RT "Effect of TBCD and its regulatory interactor Arl2 on tubulin and
RT microtubule integrity.";
RL Cytoskeleton 67:706-714(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:Q9BTW9, ECO:0000269|PubMed:17704193,
CC ECO:0000269|PubMed:20740604}.
CC -!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD. Interacts with PPP2CB. Part of a
CC supercomplex made of cofactors A to E. Cofactors A and D function by
CC 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) (PubMed:12912990, PubMed:17704193).
CC {ECO:0000250|UniProtKB:Q9BTW9, ECO:0000269|PubMed:12912990,
CC ECO:0000269|PubMed:17704193}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:17704193}. Lateral cell membrane
CC {ECO:0000269|PubMed:17704193}. Cytoplasm {ECO:0000269|PubMed:17704193}.
CC Cell junction, adherens junction {ECO:0000269|PubMed:17704193}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9BTW9}. Note=Localized in cell-cell contacts.
CC {ECO:0000269|PubMed:17704193}.
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; U61233; AAB17537.1; -; mRNA.
DR PIR; T18522; T18522.
DR RefSeq; NP_776619.1; NM_174194.2.
DR AlphaFoldDB; Q28205; -.
DR STRING; 9913.ENSBTAP00000020484; -.
DR PaxDb; Q28205; -.
DR PRIDE; Q28205; -.
DR Ensembl; ENSBTAT00000020484; ENSBTAP00000020484; ENSBTAG00000015414.
DR GeneID; 281515; -.
DR KEGG; bta:281515; -.
DR CTD; 6904; -.
DR VEuPathDB; HostDB:ENSBTAG00000015414; -.
DR VGNC; VGNC:35652; TBCD.
DR eggNOG; KOG1943; Eukaryota.
DR GeneTree; ENSGT00390000017103; -.
DR HOGENOM; CLU_003043_0_0_1; -.
DR InParanoid; Q28205; -.
DR OrthoDB; 79003at2759; -.
DR TreeFam; TF105754; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000015414; Expressed in cortex of kidney and 105 other tissues.
DR ExpressionAtlas; Q28205; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0034333; P:adherens junction assembly; IDA:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; IDA: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; IDA:UniProtKB.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 3.
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..1199
FT /note="Tubulin-specific chaperone D"
FT /id="PRO_0000080048"
FT REPEAT 368..406
FT /note="HEAT 1"
FT REPEAT 603..639
FT /note="HEAT 2"
FT REPEAT 757..793
FT /note="HEAT 3"
FT REPEAT 1111..1147
FT /note="HEAT 4"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 133014 MW; 2FCF9CCA972599BA CRC64;
MALSEEPAAG AAEDPVEDPV EDAGEDAALA CGAALESFGE SAETRELLGH LPAVLADRSA
REGALERFRV IMDKYQEQPH LLDPHLEWML NLLLEFVQNK TSPADLVHLA FKFLYIISKV
RGYKTFLRLF PHEVADVQPV LDMFTNQNPK DHETWETRYM LLLWLSVTCL IPFDFSRLDG
NLSQPGQERA STMDRILQVA ESYLVVSDKA RDAAAVLVSK FVTRPDVKQK KMASFLDWSL
CTLARSSFQT IEGVIAMDGT LQALAQIFKH GKREDCLPYA ATVLQCLDSC RLPDSNQTLL
RKLGVKLVQR LGLTFLKPQV AKWRYQRGCR SLAESLQHSI QNPREPVTQA ETPDSDGQDD
VPEEVESVIE QLLVGLKDKD TIVRWSAAKG IGRMAGRLPK ELADDVTGSV LDCFSFQETD
SAWHGGCLAL AELGRRGLLL PSRLSDVVPV ILRALTYEEK RGACSVGSNV RDAACYVCWA
FARAYEPQEL KPFVAAISSA LVIATVFDRD VNCRRAASAA FQENVGRQGT FPHGIDILTT
ADYFAVGNRS NCFLVISMFI AGFPEYTQPM IEHLVTMKVG HWDGTIRELS AKALRNLAQR
APEHTAREVF PRLLSMTQSP DLHTRHGAVL ACAEVARSLH TLATQQGRPV SDFLDEKAMH
GLKQIHQQLY DRQLYRGLGG ELMRQAVCIL IENVALSKMP FRGDAVIDGW QWLINDTLKN
LHLISSHSRQ HIKEAAVSAL AALCSEYHAQ EPGEAEAAAQ EELVKLYLAE LQSPEEMTRC
GCALALGALP AFFLKGRLRQ VLAGLRAVTH ISPKDVSFAE ARRDALKAIS RICQTVGVRA
EGPPDEAVCR ENVSQIYCTL LDCLKDYTTD SRGDVGAWVR EAAMTSLMDL TLLLGRNQPE
LIEAPLCQQL MCCLAQQASE KIDRFRAHAA RVFLALLHAD SPAIPHVPAR PELERLFPRA
AVASVNWGAP SQAFPRMARL LGLPAYRYHV LLGLAVSVGG LTESTVRYST QGLFEYMKEI
QNDPAALEDF GGTLLQVFED NLLNDRVSVP LLKTLDQMLA NGCFDIFTAQ ENHPFCVKLL
ALCKEEIKKS KDVQKLRSSI AVFCGLVQFP GDVRRKVLLQ LFLLLCHPFP VIRKNTASQV
YEMVLTYDVV PTAVLDEVMA VLSSTAWDAE LPVVRAQRNR LCDLLGVPRP QLVPKPAVR
