TBCA_RAT
ID TBCA_RAT Reviewed; 108 AA.
AC Q6PEC1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 53-61; 70-79 AND 99-105, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- FUNCTION: Tubulin-folding protein; involved in the early 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, cytoskeleton {ECO:0000250}.
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 EMBL; BC058155; AAH58155.1; -; mRNA.
DR RefSeq; NP_001013263.1; NM_001013245.2.
DR AlphaFoldDB; Q6PEC1; -.
DR SMR; Q6PEC1; -.
DR STRING; 10116.ENSRNOP00000067864; -.
DR iPTMnet; Q6PEC1; -.
DR PhosphoSitePlus; Q6PEC1; -.
DR jPOST; Q6PEC1; -.
DR PaxDb; Q6PEC1; -.
DR PRIDE; Q6PEC1; -.
DR Ensembl; ENSRNOT00000073688; ENSRNOP00000067864; ENSRNOG00000048342.
DR GeneID; 366995; -.
DR KEGG; rno:366995; -.
DR CTD; 6902; -.
DR RGD; 1311538; Tbca.
DR eggNOG; KOG3470; Eukaryota.
DR GeneTree; ENSGT00390000009710; -.
DR HOGENOM; CLU_130569_1_0_1; -.
DR InParanoid; Q6PEC1; -.
DR OMA; IMMVPDS; -.
DR OrthoDB; 1471374at2759; -.
DR PhylomeDB; Q6PEC1; -.
DR PRO; PR:Q6PEC1; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000048342; Expressed in ovary and 20 other tissues.
DR Genevisible; Q6PEC1; RN.
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:0000250|UniProtKB:P80584"
FT CHAIN 2..108
FT /note="Tubulin-specific chaperone A"
FT /id="PRO_0000287583"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P80584"
SQ SEQUENCE 108 AA; 12744 MW; 04116F067B5FC073 CRC64;
MADPRVRQIK IKTGVVKRLV KEKVMYEKEA KQQEEKIEKM KAEDGENYAI KKQAEILQES
RMMIPDCQRR LEAAYTDLRQ ILESEKDLEE AEEYKEARIV LDSVKLEA
