TBCA_RABIT
ID TBCA_RABIT Reviewed; 108 AA.
AC P80584;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 86.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P80584; -.
DR SMR; P80584; -.
DR STRING; 9986.ENSOCUP00000022954; -.
DR iPTMnet; P80584; -.
DR PRIDE; P80584; -.
DR eggNOG; KOG3470; Eukaryota.
DR InParanoid; P80584; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:InterPro.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:InterPro.
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_0000080041"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:8756698"
SQ SEQUENCE 108 AA; 12684 MW; 2901815ABC6CE767 CRC64;
MADPRVRQIK IKTGVVKRLV KEKVMYEKEA KQQEEKIEKM RAEDGENYAI KKQAEILQES
RMMIPDCQRR LEAACTDLQQ ILESEKDLEE AEEYKEARLV LDSVKLEA