ID   TBCE_XENLA              Reviewed;         522 AA.
AC   Q5U508;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Tubulin-specific chaperone E;
DE   AltName: Full=Tubulin-folding cofactor E;
GN   Name=tbce;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Tubulin-folding protein; involved in the second step of the
CC       tubulin folding pathway.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TBCE family. {ECO:0000305}.
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DR   EMBL; BC084879; AAH84879.1; -; mRNA.
DR   RefSeq; NP_001088530.1; NM_001095061.1.
DR   RefSeq; XP_018117527.1; XM_018262038.1.
DR   AlphaFoldDB; Q5U508; -.
DR   MaxQB; Q5U508; -.
DR   DNASU; 495403; -.
DR   GeneID; 495403; -.
DR   KEGG; xla:495403; -.
DR   CTD; 495403; -.
DR   Xenbase; XB-GENE-865843; tbce.L.
DR   OMA; KKYALDW; -.
DR   OrthoDB; 249920at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 495403; Expressed in zone of skin and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0043014; F:alpha-tubulin binding; IEA:InterPro.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; ISS:UniProtKB.
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; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR044079; Ubl_TBCE.
DR   PANTHER; PTHR15140; PTHR15140; 1.
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   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
KW   Reference proteome; Repeat.
FT   CHAIN           1..522
FT                   /note="Tubulin-specific chaperone E"
FT                   /id="PRO_0000083543"
FT   DOMAIN          27..71
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT   REPEAT          149..170
FT                   /note="LRR 1"
FT   REPEAT          175..196
FT                   /note="LRR 2"
FT   REPEAT          201..222
FT                   /note="LRR 3"
FT   REPEAT          226..248
FT                   /note="LRR 4"
FT   REPEAT          249..270
FT                   /note="LRR 5"
FT   REPEAT          274..295
FT                   /note="LRR 6"
FT   REPEAT          303..324
FT                   /note="LRR 7"
FT   DOMAIN          337..379
FT                   /note="LRRCT"
SQ   SEQUENCE   522 AA;  58788 MW;  AB9F2D9658D5B105 CRC64;
     MNANVPSDAN CRRIICDGEY ATVRYVGNVP PTPGLWLGVE WDNHLRGKHN GTHEGTKYFT
     CSHPTGGSFI RLKKANFGVD FLAALRKRYG LKSEQNEELV IGKKTVELVG FESIQEEQSK
     LNKLKDVSLR ECAVSNAGEK GQICHSCPNI MTADLSKNLF SSWESLAHIS SQLENLTSLD
     LSENKLNPSS NPSSLATSFC NLKVLSLNRT GMKWNEILQC ASMWPALEEL HLVSNDISLL
     EQPVNNLQNL TILDISNNKI VDGNQLHTIA FLPRLKQVIV SNNIISSISF PDVDFGHTAM
     FISLTSLAVN GNNISEWCVI NELHKLLHLE SLNCHGNPLM DLDKNPETVR QLIIAKIENL
     KFLNKTEIFP TERRGAELDY RKMFGNEWLK AGGSQNEEFN KPSRDFLQDH PRYSALIKKY
     GAPDEGELKQ QQPFALKNQL LTLTIQCPEK PDKKPIQKKL PDSMTVQKVK GLLYRLLKVP
     GSDLKLSYQS SKMEGKEIEL ENDLKPLQFY SVENGDCLLV RW