ID   TBCA_CHICK              Reviewed;         108 AA.
AC   P80585;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-108, AND ACETYLATION AT ALA-2.
RC   TISSUE=Reticulocyte;
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).
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   -!- SIMILARITY: Belongs to the TBCA family. {ECO:0000305}.
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DR   AlphaFoldDB; P80585; -.
DR   SMR; P80585; -.
DR   STRING; 9031.ENSGALP00000006933; -.
DR   iPTMnet; P80585; -.
DR   PaxDb; P80585; -.
DR   VEuPathDB; HostDB:geneid_416367; -.
DR   eggNOG; KOG3470; Eukaryota.
DR   InParanoid; P80585; -.
DR   PhylomeDB; P80585; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
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:0000269|PubMed:8756698"
FT   CHAIN           2..108
FT                   /note="Tubulin-specific chaperone A"
FT                   /id="PRO_0000080042"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:8756698"
SQ   SEQUENCE   108 AA;  12679 MW;  9BD153063466847D CRC64;
     MADPRLRQIK IKTGVVKRLA KEKVMYEKEA KQQEEKIEKM KAEACDDYGI KKQAEILQES
     RMMIPDCQRR LEIAHADLTQ LLENEKELEE AEEYKEARSI LESVKLEA