TBCE_BOVIN
ID TBCE_BOVIN Reviewed; 528 AA.
AC Q32KS0; Q0V8R2;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Tubulin-specific chaperone E;
DE AltName: Full=Tubulin-folding cofactor E;
GN Name=TBCE;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BT026156; ABG66995.1; -; mRNA.
DR EMBL; BC109955; AAI09956.1; -; mRNA.
DR RefSeq; NP_001033121.1; NM_001038032.2.
DR RefSeq; XP_005226263.1; XM_005226206.3.
DR RefSeq; XP_015316413.1; XM_015460927.1.
DR AlphaFoldDB; Q32KS0; -.
DR SMR; Q32KS0; -.
DR STRING; 9913.ENSBTAP00000018249; -.
DR PaxDb; Q32KS0; -.
DR PRIDE; Q32KS0; -.
DR Ensembl; ENSBTAT00000018249; ENSBTAP00000018249; ENSBTAG00000013735.
DR GeneID; 505066; -.
DR KEGG; bta:505066; -.
DR CTD; 6905; -.
DR VEuPathDB; HostDB:ENSBTAG00000013735; -.
DR VGNC; VGNC:35653; TBCE.
DR eggNOG; KOG3207; Eukaryota.
DR GeneTree; ENSGT00530000063405; -.
DR HOGENOM; CLU_017716_5_0_1; -.
DR InParanoid; Q32KS0; -.
DR OMA; KKYALDW; -.
DR OrthoDB; 249920at2759; -.
DR TreeFam; TF313455; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000013735; Expressed in oocyte and 106 other tissues.
DR ExpressionAtlas; Q32KS0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0048589; P:developmental growth; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; IEA:Ensembl.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
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; IPR001611; Leu-rich_rpt.
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.
DR PROSITE; PS51450; LRR; 5.
PE 2: Evidence at transcript level;
KW Acetylation; Chaperone; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..528
FT /note="Tubulin-specific chaperone E"
FT /id="PRO_0000083537"
FT DOMAIN 27..71
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REPEAT 152..176
FT /note="LRR 1"
FT REPEAT 178..206
FT /note="LRR 2"
FT REPEAT 207..229
FT /note="LRR 3"
FT REPEAT 231..253
FT /note="LRR 4"
FT REPEAT 254..274
FT /note="LRR 5"
FT REPEAT 279..300
FT /note="LRR 6"
FT REPEAT 309..330
FT /note="LRR 7"
FT DOMAIN 343..385
FT /note="LRRCT"
FT MOD_RES 464
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15813"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15813"
FT CONFLICT 243
FT /note="I -> V (in Ref. 1; ABG66995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 59327 MW; 494FCF1A4F3A1C86 CRC64;
MNSTSTSDVI GRRVEVNGEH ATVRFSGLVP PVAGLWLGVE WDNPERGKHD GSHEGTVYFK
CRHPTAGSFI RPHKVNFGVD FLTAIKNRYV LEDEPKEEET EQIVIIGNKP VETIGFDSVI
KQQSQLSKLQ DVSLRNCAVN GAGDKGEIAK ACPNIRSIDL SKNLLSSWEE VIDIADQLKH
LEVLNLSENK LTSPSSSPSP TGTFPTLKVL VLNRTGVTWA EVLRCASGWP VLEKLYLESN
NIIISERPTD VLQTVKLLDL SSNQLIDENQ LFLIAYLPRL EQLILSDIGI SSIHFPDAGI
GCKTSMFPSL QYLVLNDNQI AQWSFMNELD KLQSLHALSC TRNPLTEGSK DAQTTRQFII
ARIGQLRTLN KCAIEPEERR GAELDYRKAF GNEWKKAGGH QDPEKNRPNE EFLAAHPRYQ
ALCLKYGAPE DGELKTQQPF LLKNQLLTLK IKYPNQHDQK VIEKQLPDSM TVQKVKGLLS
RLLKVPVSEL LLSYESPKMP GKEVELENDL QPLRFYSVEN GDCLLVRW
