ID   TBCA_SCHPO              Reviewed;         119 AA.
AC   Q9Y703;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Tubulin-specific chaperone A;
DE   AltName: Full=Altered polarity protein 31;
DE   AltName: Full=Tubulin-folding cofactor A;
DE            Short=CFA;
GN   Name=alp31; ORFNames=SPAC8E11.07c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10978278; DOI=10.1093/genetics/156.1.93;
RA   Radcliffe P.A., Garcia M.A., Toda T.;
RT   "The cofactor-dependent pathways for alpha- and beta-tubulins in
RT   microtubule biogenesis are functionally different in fission yeast.";
RL   Genetics 156:93-103(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Required for the maintenance of microtubule structures and
CC       cell polarity. Beta-tubulin-folding protein; may have a regulatory role
CC       in the tubulin-folding pathway. {ECO:0000269|PubMed:10978278}.
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.
CC   -!- SIMILARITY: Belongs to the TBCA family. {ECO:0000305}.
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DR   EMBL; AB029481; BAA82293.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB40194.1; -; Genomic_DNA.
DR   PIR; T43514; T43514.
DR   RefSeq; NP_594162.1; NM_001019586.2.
DR   AlphaFoldDB; Q9Y703; -.
DR   SMR; Q9Y703; -.
DR   BioGRID; 279764; 78.
DR   STRING; 4896.SPAC8E11.07c.1; -.
DR   iPTMnet; Q9Y703; -.
DR   MaxQB; Q9Y703; -.
DR   PaxDb; Q9Y703; -.
DR   EnsemblFungi; SPAC8E11.07c.1; SPAC8E11.07c.1:pep; SPAC8E11.07c.
DR   GeneID; 2543341; -.
DR   KEGG; spo:SPAC8E11.07c; -.
DR   PomBase; SPAC8E11.07c; alp31.
DR   VEuPathDB; FungiDB:SPAC8E11.07c; -.
DR   eggNOG; KOG3470; Eukaryota.
DR   HOGENOM; CLU_2051002_0_0_1; -.
DR   InParanoid; Q9Y703; -.
DR   OMA; HQKFVLK; -.
DR   PhylomeDB; Q9Y703; -.
DR   PRO; PR:Q9Y703; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0048487; F:beta-tubulin binding; IEA:InterPro.
DR   GO; GO:0044183; F:protein folding chaperone; IGI:PomBase.
DR   GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IGI:PomBase.
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   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT   CHAIN           1..119
FT                   /note="Tubulin-specific chaperone A"
FT                   /id="PRO_0000080044"
SQ   SEQUENCE   119 AA;  13531 MW;  C1068D30FD34CAC0 CRC64;
     MSNTVRSLVI KTNVVKRIIK DVELAHIDIN EAEKRVQSKI DNGEDSAEIE HQKFVLKKHL
     EALPDALVRL RNATNDLESI SSDSAYEGTP ELEQANEYLE KAKEVIEKEQ TNFPTNGYH