ID TBCC_DICDI Reviewed; 420 AA.
AC Q54PY1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=Tubulin-specific chaperone C;
DE AltName: Full=Tubulin-folding cofactor C;
DE Short=CFC;
GN Name=tbcc; ORFNames=DDB_G0284313;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Tubulin-folding protein; involved in the final step of the
CC tubulin folding pathway. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the TBCC family. {ECO:0000305}.
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DR EMBL; AAFI02000064; EAL65345.1; -; Genomic_DNA.
DR RefSeq; XP_638664.1; XM_633572.1.
DR AlphaFoldDB; Q54PY1; -.
DR SMR; Q54PY1; -.
DR STRING; 44689.Q54PY1; -.
DR PaxDb; 44689-DDB0266636; -.
DR EnsemblProtists; EAL65345; EAL65345; DDB_G0284313.
DR GeneID; 8624493; -.
DR KEGG; ddi:DDB_G0284313; -.
DR dictyBase; DDB_G0284313; tbcC.
DR eggNOG; KOG2512; Eukaryota.
DR HOGENOM; CLU_654579_0_0_1; -.
DR InParanoid; Q54PY1; -.
DR OMA; CKIRANS; -.
DR PhylomeDB; Q54PY1; -.
DR PRO; PR:Q54PY1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR027684; TBCC.
DR InterPro; IPR031925; TBCC_N.
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 PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE 3: Inferred from homology;
KW Coiled coil; Reference proteome.
FT CHAIN 1..420
FT /note="Tubulin-specific chaperone C"
FT /id="PRO_0000337256"
FT DOMAIN 216..366
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 31..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..142
FT /evidence="ECO:0000255"
FT COMPBIAS 31..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 48767 MW; 3E5A747CED21CEA0 CRC64;
MSNNNNNNNN NNDEENSKLD IVKKQFQEKE KQRLQSKLEK REISNKEQID QSSSNIASET
LLLINNLSDD IENRLNEISN NTNENKAEDL KESYNQMEES LSEINSITTM SSHILTSYDV
KSILENIDNL RKQIDKSKEK YMPKQKLSLT RKKTKTTTVS TKTTSSKEDT NETFNNNNNN
NNDNDNTDNN NNKISTEPIF NLINIKGFKN KELFYPPKKE EEIGNQDINN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNSN SINDLFISDL TDCTVILDMK VLTALKINNL VNCKIRANSP
IDGSIFIDNC INSIFSLVSR QIRIHYCTDC QFNIFVKSNP IIEGSKQIKF SSYLQNLKQQ
QQQQQQQEQE KVLSSFDNKR FKEYSFDLES NNIDSDKWKL VNDFDWIQQK QSPNWSLVEY
//
