TBCC_MOUSE
ID TBCC_MOUSE Reviewed; 341 AA.
AC Q8VCN9; Q3V242;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Tubulin-specific chaperone C;
DE AltName: Full=Tubulin-folding cofactor C;
DE Short=CFC;
GN Name=Tbcc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Kidney, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Detected
CC predominantly in the photoreceptor connecting cilium. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TBCC family. {ECO:0000305}.
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DR EMBL; AK132036; BAE20957.1; -; mRNA.
DR EMBL; BC019476; AAH19476.1; -; mRNA.
DR EMBL; BC083164; AAH83164.1; -; mRNA.
DR CCDS; CCDS28843.1; -.
DR RefSeq; NP_848472.2; NM_178385.3.
DR AlphaFoldDB; Q8VCN9; -.
DR SMR; Q8VCN9; -.
DR BioGRID; 215535; 2.
DR STRING; 10090.ENSMUSP00000048696; -.
DR iPTMnet; Q8VCN9; -.
DR PhosphoSitePlus; Q8VCN9; -.
DR REPRODUCTION-2DPAGE; Q8VCN9; -.
DR EPD; Q8VCN9; -.
DR MaxQB; Q8VCN9; -.
DR PaxDb; Q8VCN9; -.
DR PeptideAtlas; Q8VCN9; -.
DR PRIDE; Q8VCN9; -.
DR ProteomicsDB; 263076; -.
DR DNASU; 72726; -.
DR GeneID; 72726; -.
DR KEGG; mmu:72726; -.
DR UCSC; uc008cum.1; mouse.
DR CTD; 6903; -.
DR MGI; MGI:1919976; Tbcc.
DR eggNOG; KOG2512; Eukaryota.
DR InParanoid; Q8VCN9; -.
DR OrthoDB; 1618114at2759; -.
DR PhylomeDB; Q8VCN9; -.
DR TreeFam; TF105832; -.
DR BioGRID-ORCS; 72726; 17 hits in 74 CRISPR screens.
DR PRO; PR:Q8VCN9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VCN9; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR Gene3D; 1.20.58.1250; -; 1.
DR Gene3D; 2.160.20.70; -; 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; PTHR15139; 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 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..341
FT /note="Tubulin-specific chaperone C"
FT /id="PRO_0000285107"
FT DOMAIN 163..318
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15814"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15814"
FT CONFLICT 157
FT /note="T -> A (in Ref. 1; BAE20957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 38125 MW; D8730206F0C9F96E CRC64;
MEGVDCSMAL ADAAAGSPRD LSLVPERLQR REQERQIEVE RRKQKRQDQE VEEEKSGFFA
AAFARERAAV EELLRGEASA ERLEEAANRL QGLRKLLNDS VLFLAAYDLR QGQAALAQLQ
AVLTERRQEL QPKKRFAFKA RKKDAAGTAQ VDAAPVTSAA PSPPVTKEEE GAPGASWACG
FSNLESQDLE KRAEELHQRD VLLSDLTNCT VKLCGNPNTL RLAKARGCKV LCGPVTTSVF
LEDCRDCVLA VACQQLRVHT TKDTRVFLQV TSRAIVEDCS GIQFAPYTWS YPGIDKDFQD
SGLDRSKNNW DQVDDFNWLA RNVASPNWSI LPEEERDIQW D
