ID   TBCC_YEAST              Reviewed;         268 AA.
AC   P46670; D6W3D0; Q08973;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2002, sequence version 2.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Tubulin-specific chaperone C;
DE   AltName: Full=Chromosome instability protein 2;
DE   AltName: Full=Tubulin-folding cofactor C;
GN   Name=CIN2; OrderedLocusNames=YPL241C; ORFNames=P1043;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Stearns T., Kwon D., Shin K.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Tubulin-folding protein; involved in the early step of the
CC       tubulin folding pathway.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- MISCELLANEOUS: Present with 1630 molecules/cell.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U34961; AAA78272.1; -; Genomic_DNA.
DR   EMBL; Z73597; CAA97962.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11196.1; -; Genomic_DNA.
DR   PIR; S65270; S65270.
DR   RefSeq; NP_015083.1; NM_001184055.1.
DR   PDB; 5CYA; X-ray; 2.00 A; A/B=1-268.
DR   PDBsum; 5CYA; -.
DR   AlphaFoldDB; P46670; -.
DR   SMR; P46670; -.
DR   BioGRID; 35922; 262.
DR   DIP; DIP-3960N; -.
DR   IntAct; P46670; 1.
DR   STRING; 4932.YPL241C; -.
DR   MaxQB; P46670; -.
DR   PaxDb; 4932-YPL241C; -.
DR   PeptideAtlas; P46670; -.
DR   EnsemblFungi; YPL241C_mRNA; YPL241C; YPL241C.
DR   GeneID; 855835; -.
DR   KEGG; sce:YPL241C; -.
DR   AGR; SGD:S000006162; -.
DR   SGD; S000006162; CIN2.
DR   VEuPathDB; FungiDB:YPL241C; -.
DR   eggNOG; ENOG502S4TX; Eukaryota.
DR   HOGENOM; CLU_095426_0_0_1; -.
DR   InParanoid; P46670; -.
DR   OMA; RIVMERC; -.
DR   OrthoDB; 2035334at2759; -.
DR   BioCyc; YEAST:G3O-34127-MONOMER; -.
DR   BioGRID-ORCS; 855835; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P46670; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P46670; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR   GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt.
DR   GO; GO:0036094; F:small molecule binding; EXP:DisProt.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IGI:SGD.
DR   GO; GO:0007021; P:tubulin complex assembly; IMP:SGD.
DR   DisProt; DP00778; -.
DR   Gene3D; 2.160.20.70; -; 1.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR027684; TBCC.
DR   PANTHER; PTHR15139; TUBULIN FOLDING COFACTOR C; 1.
DR   PANTHER; PTHR15139:SF0; TUBULIN-SPECIFIC CHAPERONE C; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm; Cytoskeleton; Microtubule;
KW   Reference proteome.
FT   CHAIN           1..268
FT                   /note="Tubulin-specific chaperone C"
FT                   /id="PRO_0000089762"
FT   DOMAIN          98..255
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT   CONFLICT        66
FT                   /note="E -> Y (in Ref. 1; AAA78272)"
FT                   /evidence="ECO:0000305"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          107..110
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          116..122
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          124..127
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          136..148
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          157..170
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          172..177
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          184..192
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          194..199
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          208..214
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          216..221
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   HELIX           222..227
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          228..232
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   STRAND          248..251
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   HELIX           256..258
FT                   /evidence="ECO:0007829|PDB:5CYA"
FT   HELIX           260..267
FT                   /evidence="ECO:0007829|PDB:5CYA"
SQ   SEQUENCE   268 AA;  30709 MW;  CE9F2DB6B76997A8 CRC64;
     MDFTAKIKEL ERELSETSDY KTLQKKTISL RSELNTLSHS LTSYEKEHFS NDIENVLKSI
     NAKLSESKGK KRLFSFKQKN SSSAVHKNVE RTELANAPAY TTTLKKHYVL EKGDSAFENL
     EFCTVTSTTD YSGNSALSGS LCFRNITKCV INLQRIFFQT GSIFITDCTD SIIFLRSPSD
     KDFQIRLRDL KNCKILIEKL SPSIDCKQVV IIENCHKCIF NASTRDHLII QDFSNPFQSE
     ETEDNSAFAF EDFDICNKDT MQLFRAYL
//