ID   TBCA_BOVIN              Reviewed;         108 AA.
AC   P48427; Q32KV5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Tubulin-specific chaperone A;
DE   AltName: Full=TCP1-chaperonin cofactor A;
DE   AltName: Full=Tubulin-folding cofactor A;
DE            Short=CFA;
GN   Name=TBCA;
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 [MRNA].
RC   TISSUE=Testis;
RX   PubMed=8756698; DOI=10.1021/bi960788r;
RA   Melki R., Rommelaere H., Leguy R., Vandekerckhove J., Ampe C.;
RT   "Cofactor A is a molecular chaperone required for beta-tubulin folding:
RT   functional and structural characterization.";
RL   Biochemistry 35:10422-10435(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 3-77 AND 87-106.
RC   TISSUE=Testis;
RX   PubMed=7910827; DOI=10.1083/jcb.125.5.989;
RA   Gao Y., Melki R., Walden P.D., Lewis S.A., Ampe C., Rommelaere H.,
RA   Vandekerckhove J., Cowan N.J.;
RT   "A novel cochaperonin that modulates the ATPase activity of cytoplasmic
RT   chaperonin.";
RL   J. Cell Biol. 125:989-996(1994).
CC   -!- FUNCTION: Tubulin-folding protein; involved in the early 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, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Widely expressed, but is most abundant in the
CC       testis.
CC   -!- SIMILARITY: Belongs to the TBCA family. {ECO:0000305}.
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DR   EMBL; X97224; CAA65861.1; -; mRNA.
DR   EMBL; BC109909; AAI09910.1; -; mRNA.
DR   RefSeq; NP_786997.1; NM_175803.3.
DR   AlphaFoldDB; P48427; -.
DR   SMR; P48427; -.
DR   STRING; 9913.ENSBTAP00000004227; -.
DR   PaxDb; P48427; -.
DR   PeptideAtlas; P48427; -.
DR   PRIDE; P48427; -.
DR   Ensembl; ENSBTAT00000004227; ENSBTAP00000004227; ENSBTAG00000003263.
DR   GeneID; 327683; -.
DR   KEGG; bta:327683; -.
DR   CTD; 6902; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003263; -.
DR   VGNC; VGNC:35648; TBCA.
DR   eggNOG; KOG3470; Eukaryota.
DR   GeneTree; ENSGT00390000009710; -.
DR   HOGENOM; CLU_130569_1_0_1; -.
DR   InParanoid; P48427; -.
DR   OMA; IMMVPDS; -.
DR   OrthoDB; 1471374at2759; -.
DR   TreeFam; TF313971; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000003263; Expressed in oocyte and 109 other tissues.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0048487; F:beta-tubulin binding; IEA:InterPro.
DR   GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR   InterPro; IPR004226; TBCA.
DR   InterPro; IPR036126; TBCA_sf.
DR   PANTHER; PTHR21500; PTHR21500; 1.
DR   Pfam; PF02970; TBCA; 1.
DR   SUPFAM; SSF46988; SSF46988; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Microtubule; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P80584"
FT   CHAIN           2..108
FT                   /note="Tubulin-specific chaperone A"
FT                   /id="PRO_0000080038"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P80584"
SQ   SEQUENCE   108 AA;  12707 MW;  1F148FB28A05308C CRC64;
     MADPRVRQIK IKTGVVKRLV KEKMMYEKEA KQQEEKIEKM KAEDGENYAI KKQAEILQES
     RMMIPDCQRR LEAAHTDLLQ LLESEKDLEE AEEYKEARLV LDSVKLEA