ID   TBCE_PONAB              Reviewed;         527 AA.
AC   Q5RBD9;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Tubulin-specific chaperone E;
DE   AltName: Full=Tubulin-folding cofactor E;
GN   Name=TBCE;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Tubulin-folding protein; involved in the second step of the
CC       tubulin folding pathway and in the regulation of tubulin heterodimer
CC       dissociation. Required for correct organization of microtubule
CC       cytoskeleton and mitotic splindle, and maintenance of the neuronal
CC       microtubule network. {ECO:0000250|UniProtKB:Q15813}.
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. Cofactors B and E
CC       can form a heterodimer which binds to alpha-tubulin and enhances their
CC       ability to dissociate tubulin heterodimers (By similarity). Interacts
CC       with TBCD (By similarity). {ECO:0000250|UniProtKB:Q15813,
CC       ECO:0000250|UniProtKB:Q8CIV8}.
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; CR858712; CAH90921.1; -; mRNA.
DR   RefSeq; NP_001125526.1; NM_001132054.1.
DR   AlphaFoldDB; Q5RBD9; -.
DR   SMR; Q5RBD9; -.
DR   STRING; 9601.ENSPPYP00000000096; -.
DR   GeneID; 100172438; -.
DR   KEGG; pon:100172438; -.
DR   CTD; 6905; -.
DR   eggNOG; KOG3207; Eukaryota.
DR   InParanoid; Q5RBD9; -.
DR   OrthoDB; 249920at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
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   Acetylation; Chaperone; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q15813"
FT   CHAIN           2..527
FT                   /note="Tubulin-specific chaperone E"
FT                   /id="PRO_0000083540"
FT   DOMAIN          27..71
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT   REPEAT          154..175
FT                   /note="LRR 1"
FT   REPEAT          180..200
FT                   /note="LRR 2"
FT   REPEAT          205..226
FT                   /note="LRR 3"
FT   REPEAT          230..252
FT                   /note="LRR 4"
FT   REPEAT          253..274
FT                   /note="LRR 5"
FT   REPEAT          278..299
FT                   /note="LRR 6"
FT   REPEAT          308..329
FT                   /note="LRR 7"
FT   DOMAIN          342..384
FT                   /note="LRRCT"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15813"
FT   MOD_RES         463
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15813"
FT   MOD_RES         495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15813"
SQ   SEQUENCE   527 AA;  59231 MW;  94F6025DDC759779 CRC64;
     MSDTLTADVI GQRVEVNGEH ATVRFAGVVP PVAGPWLGVE WDNPERGKHD GSHEGTVYFQ
     CRHPTGGSFI RPNKVNFGTD FLTAIKNRYV LEDGPEEDRK EQIVTIGNKP VETIGFDSIM
     KQQSQLSKLQ EVSLRNCAVS CAGEKGGVAE GCPNIRKVDL SKNLLSSWDE VIHIADQLRH
     LEVLNVSENK LKFPSGSVLT GTLSALKVLV LNQTGITWAE VLRCAMGCPG LEELYLESNN
     IFISERPTDV LQTVKLLDLS SNQLIDENQL YLIAHLPRLE QLILSDIGIS SLHFPDAGIG
     CKTSLFPSLK YLVVNDNQIS QWSFFNELDK LPSLRALSCL RNPLTKEDKE AETARLLIIA
     SIGQLKTLNK CEILPEERRR AELDYRKAFG NEWKQAGGHK DPDKNRLSEE FLTAHPRYQF
     LCLKYGAPEE WELKTQQPLM LKNQLLTLKI KYPHQLDQKV LEKQLPGSMT IQKVKGLLSR
     LLKVPVSDLL LSYESPQKPG VEIELENDLK SLQFYSVENG DCLLVRW