ID   TBCC_BOVIN              Reviewed;         345 AA.
AC   Q3SZE9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tubulin-specific chaperone C;
DE   AltName: Full=Tubulin-folding cofactor C;
DE            Short=CFC;
GN   Name=TBCC;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Tubulin-folding protein; involved in the final step of the
CC       tubulin folding pathway. {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}. Note=Detected
CC       predominantly in the photoreceptor connecting cilium. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TBCC family. {ECO:0000305}.
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DR   EMBL; BC102901; AAI02902.1; -; mRNA.
DR   RefSeq; NP_001069177.1; NM_001075709.2.
DR   AlphaFoldDB; Q3SZE9; -.
DR   SMR; Q3SZE9; -.
DR   STRING; 9913.ENSBTAP00000001245; -.
DR   PaxDb; Q3SZE9; -.
DR   PRIDE; Q3SZE9; -.
DR   Ensembl; ENSBTAT00000001245; ENSBTAP00000001245; ENSBTAG00000000940.
DR   GeneID; 515354; -.
DR   KEGG; bta:515354; -.
DR   CTD; 6903; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000940; -.
DR   VGNC; VGNC:35650; TBCC.
DR   eggNOG; KOG2512; Eukaryota.
DR   GeneTree; ENSGT00940000162058; -.
DR   HOGENOM; CLU_032612_2_1_1; -.
DR   InParanoid; Q3SZE9; -.
DR   OMA; CQQLRLH; -.
DR   OrthoDB; 1618114at2759; -.
DR   TreeFam; TF105832; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000000940; Expressed in pharyngeal tonsil and 106 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR   Gene3D; 1.20.58.1250; -; 1.
DR   Gene3D; 2.160.20.70; -; 1.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR006599; CARP_motif.
DR   InterPro; IPR027684; TBCC.
DR   InterPro; IPR031925; TBCC_N.
DR   InterPro; IPR038397; TBCC_N_sf.
DR   InterPro; IPR012945; Tubulin-bd_cofactor_C_dom.
DR   PANTHER; PTHR15139; PTHR15139; 1.
DR   Pfam; PF07986; TBCC; 1.
DR   Pfam; PF16752; TBCC_N; 1.
DR   SMART; SM00673; CARP; 2.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..345
FT                   /note="Tubulin-specific chaperone C"
FT                   /id="PRO_0000285106"
FT   DOMAIN          170..322
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15814"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15814"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15814"
SQ   SEQUENCE   345 AA;  38903 MW;  AC953C5E29D45158 CRC64;
     METGGLSAAA LANGDLGSQR ERTLVPERLQ KREHERQLEV ERRKQKRQDQ EVEEEKSDFF
     AAAFARERSA VEELLESGES VERLEEAAAR LQGLQKLIND SVLFLAAYDL RQAQEVLARL
     QAALAKRRQE LQPKKRFAFK TRKKDAASAT QVASAPDAPA AEGSLTSPPP LKEEGDFDSS
     WICGFSNLQS QVLEKRAEEL HQQDVLLTQL RNCTIKLYGN PNTLRLTKAQ GCTLLCGPVS
     TSVFLEDCSD CVLAVACQQL RVHTTKDTRI FLQVTSRAIM EDCTGIQFAP YTWSYPGIDK
     DFEGSGLDKN KNNWNDVDDF NWLARDVASP NWNVLPEEER RIQWD