ID A0A2K5JWC1_COLAP Unreviewed; 108 AA.
AC A0A2K5JWC1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Tubulin-specific chaperone A {ECO:0000256|ARBA:ARBA00015002, ECO:0000256|RuleBase:RU364030};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000033085.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000033085.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Tubulin-folding protein; involved in the early step of the
CC tubulin folding pathway. {ECO:0000256|ARBA:ARBA00003046}.
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 {ECO:0000256|ARBA:ARBA00026055, ECO:0000256|RuleBase:RU364030}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|RuleBase:RU364030}.
CC -!- SIMILARITY: Belongs to the TBCA family. {ECO:0000256|ARBA:ARBA00006806,
CC ECO:0000256|RuleBase:RU364030}.
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 RefSeq; XP_011814605.1; XM_011959215.1.
DR AlphaFoldDB; A0A2K5JWC1; -.
DR SMR; A0A2K5JWC1; -.
DR Ensembl; ENSCANT00000056311.1; ENSCANP00000033085.1; ENSCANG00000040198.1.
DR GeneID; 105524098; -.
DR CTD; 6902; -.
DR OMA; VIQECIM; -.
DR OrthoDB; 2727334at2759; -.
DR Proteomes; UP000233080; 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:UniProtKB-UniRule.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.58.90; -; 1.
DR InterPro; IPR004226; TBCA.
DR InterPro; IPR036126; TBCA_sf.
DR PANTHER; PTHR21500; TUBULIN-SPECIFIC CHAPERONE A; 1.
DR PANTHER; PTHR21500:SF0; TUBULIN-SPECIFIC CHAPERONE A; 1.
DR Pfam; PF02970; TBCA; 1.
DR SUPFAM; SSF46988; Tubulin chaperone cofactor A; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU364030};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU364030};
KW Cytoskeleton {ECO:0000256|RuleBase:RU364030};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU364030};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080}.
FT COILED 16..43
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 108 AA; 12888 MW; C38016300829EF0F CRC64;
MAEPRVRQIK IKTGVVKRLV KEKVMYEKEA KQQEEKIEKM RAEDGENYDI KKQVEILQES
RMMIPDCQRR LEAAYLDLQQ ILECEKDLEE TEEYKEARLV LDSVKLEA
//
