TBCE_RAT
ID TBCE_RAT Reviewed; 524 AA.
AC Q5FVQ9;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Tubulin-specific chaperone E;
DE AltName: Full=Tubulin-folding cofactor E;
GN Name=Tbce;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
CC -!- FUNCTION: Tubulin-folding protein; involved in the second step of the
CC tubulin folding pathway and in the regulation of tubulin heterodimer
CC dissociation. Required for correct organization of microtubule
CC cytoskeleton and mitotic splindle, and maintenance of the neuronal
CC microtubule network. {ECO:0000250|UniProtKB:Q15813}.
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. Cofactors B and E
CC can form a heterodimer which binds to alpha-tubulin and enhances their
CC ability to dissociate tubulin heterodimers (By similarity). Interacts
CC with TBCD (By similarity). {ECO:0000250|UniProtKB:Q15813,
CC ECO:0000250|UniProtKB:Q8CIV8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TBCE family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC089833; AAH89833.1; -; mRNA.
DR RefSeq; NP_001012161.1; NM_001012161.1.
DR AlphaFoldDB; Q5FVQ9; -.
DR SMR; Q5FVQ9; -.
DR IntAct; Q5FVQ9; 1.
DR STRING; 10116.ENSRNOP00000042689; -.
DR iPTMnet; Q5FVQ9; -.
DR PhosphoSitePlus; Q5FVQ9; -.
DR jPOST; Q5FVQ9; -.
DR PaxDb; Q5FVQ9; -.
DR PRIDE; Q5FVQ9; -.
DR Ensembl; ENSRNOT00000040743; ENSRNOP00000042689; ENSRNOG00000029667.
DR GeneID; 361255; -.
DR KEGG; rno:361255; -.
DR UCSC; RGD:1305533; rat.
DR CTD; 6905; -.
DR RGD; 1305533; Tbce.
DR eggNOG; KOG3207; Eukaryota.
DR GeneTree; ENSGT00530000063405; -.
DR HOGENOM; CLU_017716_5_0_1; -.
DR InParanoid; Q5FVQ9; -.
DR OrthoDB; 249920at2759; -.
DR PhylomeDB; Q5FVQ9; -.
DR TreeFam; TF313455; -.
DR PRO; PR:Q5FVQ9; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000029667; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q5FVQ9; baseline and differential.
DR Genevisible; Q5FVQ9; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0014889; P:muscle atrophy; ISO:RGD.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; ISO:RGD.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; ISS:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR CDD; cd17044; Ubl_TBCE; 1.
DR Gene3D; 2.30.30.190; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044994; TBCE.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044079; Ubl_TBCE.
DR PANTHER; PTHR15140; PTHR15140; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chaperone; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15813"
FT CHAIN 2..524
FT /note="Tubulin-specific chaperone E"
FT /id="PRO_0000083541"
FT DOMAIN 27..71
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REPEAT 154..175
FT /note="LRR 1"
FT REPEAT 180..201
FT /note="LRR 2"
FT REPEAT 206..227
FT /note="LRR 3"
FT REPEAT 231..253
FT /note="LRR 4"
FT REPEAT 254..273
FT /note="LRR 5"
FT REPEAT 279..300
FT /note="LRR 6"
FT REPEAT 309..330
FT /note="LRR 7"
FT DOMAIN 343..381
FT /note="LRRCT"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q15813"
FT MOD_RES 460
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15813"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15813"
SQ SEQUENCE 524 AA; 59043 MW; 865358549B0B9404 CRC64;
MSDILPLDVI GRRVEVNGEY ATVRFCGAVP PVAGLWLGVE WDNPERGKHD GSHEGTMYFK
CRHPTGGSFV RPNIVNFGED FLTALKKRYV LTDGPDDDEK SCSLKVGSKQ VQTIGFEHIT
KKQSQLRSLQ DISLWKCAVS CAGERGRIAE ACPNIRVVDL SKNLLSTWDE VILIAEQLKD
LEALDLSENK LQFPSDSPTL TRTFSTLKTL VLNKTGITWT EVLHCAPSWP VLQELYLKSN
GISISERPVN ALQNLRLLDL SSNPSIDESQ LCLIAYLPRL EHLLLSDIGL SSIHFPDAEI
GCKTSMFPAL TYLIVNDNQI SEWSFINELD KLQSLQALSC ARNPLTKGDK AEEIIIAKIG
QLKTLNRCQI LPEERRGAEL DYRKAFGKEW RKAGGHPDPD RNRPSAEFLS AHPRYQLLCC
KYGAPEDEEL KTQQPFMLKN QLLTLKIKCS NQPEQQILEK QLPDSMTIQK VKGLLSRLLK
VPVSELLLSY ESSKMPGREI ELENDLQPLQ FYSVENGDCL LVRW
