ID   Q95TP0_DROME            Unreviewed;       355 AA.
AC   Q95TP0;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   02-SEP-2026, entry version 184.
DE   SubName: Full=LD34582p {ECO:0000313|EMBL:AAL13875.1};
GN   Name=Tbcc {ECO:0000313|FlyBase:FBgn0051961};
GN   Synonyms=TBCC {ECO:0000313|FlyBase:FBgn0051961};
GN   ORFNames=CG31961 {ECO:0000313|FlyBase:FBgn0051961};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AAL13875.1};
RN   [1] {ECO:0000313|EMBL:AAL13875.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Berkeley {ECO:0000313|EMBL:AAL13875.1};
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA   Chavez C., Dorsett V., Farfan D., Frise E., George R., Gonzalez M.,
RA   Guarin H., Li P., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.,
RA   Paragas V., Park S., Phouanenavong S., Wan K., Yu C., Lewis S.E.,
RA   Rubin G.M., Celniker S.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TBCC family.
CC       {ECO:0000256|ARBA:ARBA00008848}.
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DR   EMBL; AY058646; AAL13875.1; -; mRNA.
DR   RefSeq; NP_722959.1; NM_164570.2.
DR   RefSeq; NP_722960.1; NM_164571.2.
DR   AlphaFoldDB; Q95TP0; -.
DR   SMR; Q95TP0; -.
DR   IntAct; Q95TP0; 5.
DR   STRING; 7227.FBpp0077174; -.
DR   PaxDb; 7227-FBpp0077174; -.
DR   PeptideAtlas; Q95TP0; -.
DR   DNASU; 319048; -.
DR   GeneID; 319048; -.
DR   KEGG; dme:Dmel_CG31961; -.
DR   UCSC; CG31961-RA; d. melanogaster.
DR   AGR; FB:FBgn0051961; -.
DR   CTD; 6903; -.
DR   FlyBase; FBgn0051961; Tbcc.
DR   VEuPathDB; VectorBase:FBgn0051961; -.
DR   eggNOG; KOG2512; Eukaryota.
DR   HOGENOM; CLU_032612_2_1_1; -.
DR   OMA; YFQHEIT; -.
DR   OrthoDB; 194775at2759; -.
DR   BioGRID-ORCS; 319048; 0 hits in 3 CRISPR screens.
DR   Bgee; FBgn0051961; Expressed in mechanosensory neuron of leg chordotonal organ in insect leg and 162 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR   Gene3D; 2.160.20.70; -; 1.
DR   Gene3D; 1.20.58.1250; Tubulin Binding Cofactor C, N-terminal domain; 1.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR006599; CARP_motif.
DR   InterPro; IPR027684; TBCC.
DR   InterPro; IPR031925; TBCC_N.
DR   InterPro; IPR038397; TBCC_N_sf.
DR   InterPro; IPR012945; Tubulin-bd_cofactor_C_dom.
DR   PANTHER; PTHR15139; TUBULIN FOLDING COFACTOR C; 1.
DR   PANTHER; PTHR15139:SF0; TUBULIN-SPECIFIC CHAPERONE C; 1.
DR   Pfam; PF07986; TBCC; 1.
DR   Pfam; PF16752; TBCC_N; 1.
DR   SMART; SM00673; CARP; 2.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490}.
FT   DOMAIN          146..308
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
SQ   SEQUENCE   355 AA;  40522 MW;  A5ED44EA188745CD CRC64;
     MEGDAENRKD QILERLNKRN KDRQNYLDVK SELRSKETVQ NEGVDYFYQT FSQKTMDIEQ
     RLKDVQCGDG QPTDLARNFA DITVEIQDLQ RYLTASTMFL PDFKIKSCQN ILNTLTAVSD
     ETRQRLLPKK KFGFSGKKTV TKPKVPPNKD IVDAKLSKVP EKLGSNFTWT IANRTNEHIV
     LDSAKVNGQD ITISKLNHCL VELQGHPGSV QVSRASKCTL LCGPIARSFF AENLEDCTLS
     IACQQLRLHS SRSIRIYMHV TCRAIIEDCK SIEIGEYNYD YSKLEADYLA SGLNKAQNNY
     TDVADFNWLS PDVPSPNWSL LKDYPDPNWN ALRRDFIANN HNSELKQDVK DISII
//