TBCD_CHICK
ID TBCD_CHICK Reviewed; 1019 AA.
AC Q5ZI87;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Tubulin-specific chaperone D;
DE AltName: Full=Beta-tubulin cofactor D;
DE AltName: Full=Tubulin-folding cofactor D;
GN Name=TBCD; ORFNames=RCJMB04_29e8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
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DR EMBL; AJ720897; CAG32556.1; -; mRNA.
DR RefSeq; NP_001012819.1; NM_001012801.1.
DR AlphaFoldDB; Q5ZI87; -.
DR STRING; 9031.ENSGALP00000002281; -.
DR PaxDb; Q5ZI87; -.
DR PRIDE; Q5ZI87; -.
DR GeneID; 417334; -.
DR KEGG; gga:417334; -.
DR CTD; 6904; -.
DR VEuPathDB; HostDB:geneid_417334; -.
DR eggNOG; KOG1943; Eukaryota.
DR InParanoid; Q5ZI87; -.
DR PhylomeDB; Q5ZI87; -.
DR PRO; PR:Q5ZI87; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Chaperone; Cytoplasm; Cytoskeleton; Membrane;
KW Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1019
FT /note="Tubulin-specific chaperone D"
FT /id="PRO_0000080051"
FT REPEAT 364..402
FT /note="HEAT 1"
FT REPEAT 856..898
FT /note="HEAT 2"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 113662 MW; EF2FBBE80E159BB6 CRC64;
MAVGETDGAG SEESGSREAD VISRGNILES FTESQEVRAL LGNLRTVYGD PVAQEVIVEK
FIVIMDKYQE QPHLLDRHLE WMMNMLLDII RDSGSPPVLF HLAFKFLYII TKVRGYKLFL
RLFPHEVTDL QPVLDMIVDQ NPKDCETWET RYMLLLWLSM ICLIPFDLAR FDGNILSEEG
HTRMPTMDRI LEIAKCYLVV SDKARDAAAV LVSKFIVRPD VRQKRMADFL DWTLSMLSKS
SFQSMEGTVV MNGMLQALAQ LFKHGKREDC LPYAATVLEC LDNCKLSESN QMVLRKLGMK
LVQRLGLTFV KPKVAKWRYQ RGCRSLAANL QAQSSVMQSQ KITVAANEAE DDEEYDIPGE
IENVVEQLLV GLKDKDTIVR WSAAKGIGRI TGRLPKELAD DVVGSLLDCF SFQETDNAWH
GGCLALAELG RRGLLLPSRI SDVVPVILKA LTYDEKRGSC SVGSNLRDAA CYLSWAFARA
YDPSELIPFI NQISSALVIA AVFDRDVNCR RAASAAFQEN VGRQGTFPHG IDILTAADYF
AVGNRVNCYL TISVYIAGFP EYTQPMIDHL VNMKINHWDS VIRELSTKAL HNLTPRAPEY
MANVVLPRLL PLSVGTDLHT RHGAILACAE ITHALCKLAE ENNRSITYYF NGKSLEGLKQ
IHQELCSRQL YRGLGGELMR PAVCTLIEKL SLSKMPFKGD PIIEGWQWLI NDSLRSLPLA
SCAARQHVKE SAVSALSALC NEYYINENGE ADPALQGELV TQYISELQST EQMIRCGFSL
ALGALPRFLL KGRLQQVLEG LRKVTLITPR DVSFAESRRD ALIAIAEICQ TVGVKGEGSQ
EEYICKDNVA QIYATLLNCV TDYTTDSRGD VGGWVREAAM TSLMKVTLLL VQNEAELINA
NICKQIMCWL AQQSAEKIDK FRAHAGSVFL TLLHFDSPPV PHIPHREELE RIFPRSEAET
LNWNAASEAF PRITQLLALP AYQYYVLLGL SVSVGGLTET TGVCAPPDNA GPNAGKRLF
