TBCA_MOUSE
ID TBCA_MOUSE Reviewed; 108 AA.
AC P48428;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Tubulin-specific chaperone A;
DE AltName: Full=TCP1-chaperonin cofactor A;
DE AltName: Full=Tubulin-folding cofactor A;
DE Short=CFA;
GN Name=Tbca;
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 [MRNA].
RC STRAIN=Swiss Webster; TISSUE=Testis;
RX PubMed=7910827; DOI=10.1083/jcb.125.5.989;
RA Gao Y., Melki R., Walden P.D., Lewis S.A., Ampe C., Rommelaere H.,
RA Vandekerckhove J., Cowan N.J.;
RT "A novel cochaperonin that modulates the ATPase activity of cytoplasmic
RT chaperonin.";
RL J. Cell Biol. 125:989-996(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Colon, and Mammary gland;
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, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 early step of the
CC tubulin folding pathway.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Widely expressed, but is most abundant in the
CC testis.
CC -!- SIMILARITY: Belongs to the TBCA family. {ECO:0000305}.
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DR EMBL; U05333; AAA83250.1; -; mRNA.
DR EMBL; BC034267; AAH34267.1; -; mRNA.
DR EMBL; BC051475; AAH51475.1; -; mRNA.
DR EMBL; BC055749; AAH55749.1; -; mRNA.
DR CCDS; CCDS26694.1; -.
DR PIR; I48930; I48930.
DR RefSeq; NP_033347.1; NM_009321.2.
DR AlphaFoldDB; P48428; -.
DR SMR; P48428; -.
DR BioGRID; 203976; 1.
DR STRING; 10090.ENSMUSP00000038781; -.
DR iPTMnet; P48428; -.
DR PhosphoSitePlus; P48428; -.
DR REPRODUCTION-2DPAGE; P48428; -.
DR EPD; P48428; -.
DR jPOST; P48428; -.
DR PaxDb; P48428; -.
DR PeptideAtlas; P48428; -.
DR PRIDE; P48428; -.
DR ProteomicsDB; 263010; -.
DR Antibodypedia; 24499; 271 antibodies from 27 providers.
DR DNASU; 21371; -.
DR Ensembl; ENSMUST00000046644; ENSMUSP00000038781; ENSMUSG00000042043.
DR GeneID; 21371; -.
DR KEGG; mmu:21371; -.
DR UCSC; uc007rlx.1; mouse.
DR CTD; 6902; -.
DR MGI; MGI:107549; Tbca.
DR VEuPathDB; HostDB:ENSMUSG00000042043; -.
DR eggNOG; KOG3470; Eukaryota.
DR GeneTree; ENSGT00390000009710; -.
DR HOGENOM; CLU_130569_1_0_1; -.
DR InParanoid; P48428; -.
DR OMA; IMMVPDS; -.
DR OrthoDB; 1471374at2759; -.
DR PhylomeDB; P48428; -.
DR TreeFam; TF313971; -.
DR BioGRID-ORCS; 21371; 29 hits in 105 CRISPR screens.
DR ChiTaRS; Tbca; mouse.
DR PRO; PR:P48428; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P48428; protein.
DR Bgee; ENSMUSG00000042043; Expressed in floor plate of midbrain and 255 other tissues.
DR ExpressionAtlas; P48428; baseline and differential.
DR Genevisible; P48428; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:InterPro.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
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 InterPro; IPR004226; TBCA.
DR InterPro; IPR036126; TBCA_sf.
DR PANTHER; PTHR21500; PTHR21500; 1.
DR Pfam; PF02970; TBCA; 1.
DR SUPFAM; SSF46988; SSF46988; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Cytoskeleton; Microtubule;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P80584"
FT CHAIN 2..108
FT /note="Tubulin-specific chaperone A"
FT /id="PRO_0000080040"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P80584"
SQ SEQUENCE 108 AA; 12758 MW; 93D4E497F256C48E CRC64;
MADPRVRQIK IKTGVVRRLV KERVMYEKEA KQQEEKIEKM KAEDGENYAI KKQAEILQES
RMMIPDCQRR LEAAYTDLQQ ILESEKDLEE AEEYKEARVV LDSVKLEA
