ID A0A158NEK1_ATTCE Unreviewed; 118 AA.
AC A0A158NEK1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Tubulin-specific chaperone A {ECO:0000256|ARBA:ARBA00015002, ECO:0000256|RuleBase:RU364030};
GN Name=105619041 {ECO:0000313|EnsemblMetazoa:XP_012055959.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012055959.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012055959.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) 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}.
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DR EMBL; ADTU01013477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012055959.1; XM_012200569.1.
DR AlphaFoldDB; A0A158NEK1; -.
DR STRING; 12957.A0A158NEK1; -.
DR EnsemblMetazoa; XM_012200569.1; XP_012055959.1; LOC105619041.
DR GeneID; 105619041; -.
DR KEGG; acep:105619041; -.
DR InParanoid; A0A158NEK1; -.
DR OrthoDB; 2727334at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
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|RuleBase:RU364030};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205}.
FT COILED 16..43
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 118 AA; 13995 MW; D545BBC6FC01C180 CRC64;
MSDPRIRTLK IKTGVVKRLA KEKVTYEKEA AQQRERIQKL KEQDKDGYDI KKQEEVLQES
LMMVPDCQRR LVKAFEELKK ILETEQDLKE VEDYIEAEKI LQEAEEQLPK EGDILQMC
//
