TBCE_DANRE
ID TBCE_DANRE Reviewed; 521 AA.
AC Q5U378;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Tubulin-specific chaperone E;
DE AltName: Full=Tubulin-folding cofactor E;
GN Name=tbce; ORFNames=zgc:123075;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Tubulin-folding protein; involved in the second 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 {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TBCE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH85669.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC085669; AAH85669.1; ALT_INIT; mRNA.
DR RefSeq; NP_001035078.2; NM_001039989.2.
DR RefSeq; XP_005155982.1; XM_005155925.3.
DR AlphaFoldDB; Q5U378; -.
DR SMR; Q5U378; -.
DR STRING; 7955.ENSDARP00000065584; -.
DR PaxDb; Q5U378; -.
DR Ensembl; ENSDART00000160639; ENSDARP00000131097; ENSDARG00000099921.
DR Ensembl; ENSDART00000171837; ENSDARP00000132970; ENSDARG00000099921.
DR GeneID; 664760; -.
DR KEGG; dre:664760; -.
DR CTD; 6905; -.
DR ZFIN; ZDB-GENE-051030-120; tbce.
DR eggNOG; KOG3207; Eukaryota.
DR GeneTree; ENSGT00530000063405; -.
DR HOGENOM; CLU_017716_5_0_1; -.
DR InParanoid; Q5U378; -.
DR OMA; KKYALDW; -.
DR OrthoDB; 249920at2759; -.
DR PhylomeDB; Q5U378; -.
DR TreeFam; TF313455; -.
DR PRO; PR:Q5U378; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000099921; Expressed in spleen and 25 other tissues.
DR ExpressionAtlas; Q5U378; baseline and differential.
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:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; ISS:UniProtKB.
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; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044994; TBCE.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044079; Ubl_TBCE.
DR PANTHER; PTHR15140; PTHR15140; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00369; LRR_TYP; 4.
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 Chaperone; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
KW Reference proteome; Repeat.
FT CHAIN 1..521
FT /note="Tubulin-specific chaperone E"
FT /id="PRO_0000083542"
FT DOMAIN 24..68
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REPEAT 147..168
FT /note="LRR 1"
FT REPEAT 173..194
FT /note="LRR 2"
FT REPEAT 199..220
FT /note="LRR 3"
FT REPEAT 224..245
FT /note="LRR 4"
FT REPEAT 247..268
FT /note="LRR 5"
FT REPEAT 271..292
FT /note="LRR 6"
FT REPEAT 301..322
FT /note="LRR 7"
FT DOMAIN 335..377
FT /note="LRRCT"
SQ SEQUENCE 521 AA; 59043 MW; F6533A652A98685E CRC64;
MMLDEAVGRR VCCDGERGTV RYVGPVPPTA GVWLGVEWDH PERGKHDGSH DGVRYFTCRH
PTGGSFVRPQ KASFGVDYVT ALKQRYEVEI EEVTAEEMKI SSKTVVMVGF ENVKKKQSVK
NLTEVGLRRC EVSAPGPENE IRNTTPFVQS LDLSGNLLSS WEVLAAITEQ LDSLQELHLS
HNRLSISSAP SSLSSAFSHL RVLSINSCAL TWTQVLHCAP MWQQVEELYL ADNNITELLR
PEHVLQALTV LDLSNNQIAQ ETVLEISHLP RLERLNLSST SLSEIKFSDV PAGKKTTLFP
ALKELLLDDN NISEWRVVNE LEKLPSLVYL SCRRNPLLHK EKNLETARQI MIARLGQLEL
LDMRQILSDE RRGAELDYCK MFGSAWLRAG GHREAEKNNP NTDFMTEHPR YLTLIQKYGA
PDEGELREQK PFALKNQLLT ITFLCPEDLE RKPIEKKLPG SMIVQKVKGL LHRLLKLPGV
ELKLTYTCAK MADREIEIDN DLKPLQFYSV EDGDKILVRW S