TBCB_CAEEL
ID TBCB_CAEEL Reviewed; 229 AA.
AC Q20728;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Tubulin-specific chaperone B;
DE AltName: Full=Tubulin-folding cofactor B;
DE Short=CoB;
GN Name=tbcb-1 {ECO:0000312|WormBase:F53F4.3};
GN ORFNames=F53F4.3 {ECO:0000312|WormBase:F53F4.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 135-229.
RX PubMed=12221106; DOI=10.1074/jbc.m208512200;
RA Li S., Finley J., Liu Z.J., Qiu S.H., Chen H., Luan C.H., Carson M.,
RA Tsao J., Johnson D., Lin G., Zhao J., Thomas W., Nagy L.A., Sha B.,
RA DeLucas L.J., Wang B.C., Luo M.;
RT "Crystal structure of the cytoskeleton-associated protein glycine-rich
RT (CAP-Gly) domain.";
RL J. Biol. Chem. 277:48596-48601(2002).
RN [3]
RP STRUCTURE BY NMR OF 1-120.
RX PubMed=15364906; DOI=10.1074/jbc.m409422200;
RA Lytle B.L., Peterson F.C., Qiu S.H., Luo M., Zhao Q., Markley J.L.,
RA Volkman B.F.;
RT "Solution structure of a ubiquitin-like domain from tubulin-binding
RT cofactor B.";
RL J. Biol. Chem. 279:46787-46793(2004).
CC -!- FUNCTION: Binds to alpha-tubulin folding intermediates after their
CC interaction with cytosolic chaperonin in the pathway leading from newly
CC synthesized tubulin to properly folded heterodimer. {ECO:0000250}.
CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC function by capturing and stabilizing tubulin in a quasi-native
CC conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC interaction with cofactor C then causes the release of tubulin
CC polypeptides that are committed to the native state (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TBCB family. {ECO:0000305}.
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DR EMBL; Z77663; CAB01212.1; -; Genomic_DNA.
DR PIR; T22581; T22581.
DR RefSeq; NP_506367.1; NM_073966.1.
DR PDB; 1LPL; X-ray; 1.77 A; A=135-229.
DR PDB; 1T0Y; NMR; -; A=1-120.
DR PDB; 1TOV; X-ray; 1.77 A; A=132-229.
DR PDBsum; 1LPL; -.
DR PDBsum; 1T0Y; -.
DR PDBsum; 1TOV; -.
DR AlphaFoldDB; Q20728; -.
DR BMRB; Q20728; -.
DR SMR; Q20728; -.
DR BioGRID; 50924; 3.
DR STRING; 6239.F53F4.3; -.
DR EPD; Q20728; -.
DR PaxDb; Q20728; -.
DR PeptideAtlas; Q20728; -.
DR EnsemblMetazoa; F53F4.3.1; F53F4.3.1; WBGene00009987.
DR GeneID; 186176; -.
DR KEGG; cel:CELE_F53F4.3; -.
DR UCSC; F53F4.3; c. elegans.
DR CTD; 186176; -.
DR WormBase; F53F4.3; CE10958; WBGene00009987; tbcb-1.
DR eggNOG; KOG3206; Eukaryota.
DR HOGENOM; CLU_067577_1_0_1; -.
DR InParanoid; Q20728; -.
DR OMA; IGVKYDE; -.
DR OrthoDB; 1550378at2759; -.
DR PhylomeDB; Q20728; -.
DR EvolutionaryTrace; Q20728; -.
DR PRO; PR:Q20728; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00009987; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR CDD; cd01789; Ubl_TBCB; 1.
DR DisProt; DP03057; -.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR045172; TBCB_N_Ubl.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Cytoskeleton; Microtubule;
KW Reference proteome.
FT CHAIN 1..229
FT /note="Tubulin-specific chaperone B"
FT /id="PRO_0000083546"
FT DOMAIN 170..212
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:1T0Y"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1T0Y"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:1T0Y"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1T0Y"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1T0Y"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:1T0Y"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1T0Y"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:1T0Y"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1T0Y"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:1LPL"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1LPL"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:1LPL"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1LPL"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:1LPL"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:1LPL"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:1LPL"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1LPL"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1LPL"
SQ SEQUENCE 229 AA; 25441 MW; C465365DAE378A0F CRC64;
MTEVYDLEIT TNATDFPMEK KYPAGMSLND LKKKLELVVG TTVDSMRIQL FDGDDQLKGE
LTDGAKSLKD LGVRDGYRIH AVDVTGGNED FKDESMVEKY EMSDDTYGKR TDSVRAWKKK
MQEEQGSAAP MENESDKLNE EAAKNIMVGN RCEVTVGAQM ARRGEVAYVG ATKFKEGVWV
GVKYDEPVGK NDGSVAGVRY FDCDPKYGGF VRPVDVKVGD FPELSIDEI
