ID   A0A2I0TSX8_LIMLA        Unreviewed;       150 AA.
AC   A0A2I0TSX8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Tubulin-specific chaperone A {ECO:0000256|ARBA:ARBA00015002, ECO:0000256|RuleBase:RU364030};
GN   ORFNames=llap_12785 {ECO:0000313|EMBL:PKU36910.1};
OS   Limosa lapponica baueri.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Charadriiformes; Scolopacidae; Limosa.
OX   NCBI_TaxID=1758121 {ECO:0000313|EMBL:PKU36910.1, ECO:0000313|Proteomes:UP000233556};
RN   [1] {ECO:0000313|Proteomes:UP000233556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lima N.C., Parody-Merino A.M., Battley P.F., Fidler A.E., Prosdocimi F.;
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000233556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lima N.C.B., Parody-Merino A.M., Battley P.F., Fidler A.E., Prosdocimi F.;
RT   "Genome sequence of the Bar-tailed Godwit (Limosa lapponica baueri).";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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; KZ507398; PKU36910.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0TSX8; -.
DR   Proteomes; UP000233556; 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|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU364030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233556}.
FT   COILED          113..146
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   150 AA;  17758 MW;  C6C57533B6A15765 CRC64;
     MNSLLSCRQP SNCSRKRLLA RIIINSDIFK LYYSNQARIY SIDLLHLVNQ INIIPWFNCR
     LAKEKVMYEK EAKQQEEKIE KMKAEACDDY GIKKQIEILQ ESRMMIPDCQ RRLEVARADL
     TQLLENEKEL EEAEEYKEAR SILESVKLEA
//