TBCB_BOVIN
ID TBCB_BOVIN Reviewed; 244 AA.
AC Q5E951; Q3ZCC1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Tubulin-folding cofactor B;
DE AltName: Full=Cytoskeleton-associated protein 1;
DE AltName: Full=Cytoskeleton-associated protein CKAPI;
DE AltName: Full=Tubulin-specific chaperone B;
GN Name=TBCB; Synonyms=CKAP1;
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=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to alpha-tubulin folding intermediates after their
CC interaction with cytosolic chaperonin in the pathway leading from newly
CC synthesized tubulin to properly folded heterodimer. Involved in
CC regulation of tubulin heterodimer dissociation. May function as a
CC negative regulator of axonal growth. {ECO:0000250|UniProtKB:Q99426,
CC ECO:0000250|UniProtKB:Q9D1E6}.
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. Interacts with GAN.
CC Interacts with DCTN1. {ECO:0000250|UniProtKB:Q99426,
CC ECO:0000250|UniProtKB:Q9D1E6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99426}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q99426}.
CC Note=Colocalizes with microtubules. In differentiated neurons, located
CC in the cytoplasm. In differentiating neurons, accumulates at the growth
CC cone. {ECO:0000250|UniProtKB:Q99426}.
CC -!- PTM: Ubiquitinated in the presence of GAN which targets it for
CC degradation by the proteasome. {ECO:0000250|UniProtKB:Q99426}.
CC -!- PTM: Phosphorylation by PAK1 is required for normal function.
CC {ECO:0000250|UniProtKB:Q99426}.
CC -!- SIMILARITY: Belongs to the TBCB family. {ECO:0000305}.
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DR EMBL; BT021069; AAX09086.1; -; mRNA.
DR EMBL; BC102571; AAI02572.1; -; mRNA.
DR RefSeq; NP_001014939.1; NM_001014939.1.
DR AlphaFoldDB; Q5E951; -.
DR SMR; Q5E951; -.
DR STRING; 9913.ENSBTAP00000019973; -.
DR PaxDb; Q5E951; -.
DR PeptideAtlas; Q5E951; -.
DR PRIDE; Q5E951; -.
DR Ensembl; ENSBTAT00000019973; ENSBTAP00000019973; ENSBTAG00000015004.
DR GeneID; 530447; -.
DR KEGG; bta:530447; -.
DR CTD; 1155; -.
DR VEuPathDB; HostDB:ENSBTAG00000015004; -.
DR VGNC; VGNC:35649; TBCB.
DR eggNOG; KOG3206; Eukaryota.
DR GeneTree; ENSGT00940000156119; -.
DR HOGENOM; CLU_067577_2_0_1; -.
DR InParanoid; Q5E951; -.
DR OMA; IGVKYDE; -.
DR OrthoDB; 1550378at2759; -.
DR TreeFam; TF313444; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000015004; Expressed in spermatocyte and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd01789; Ubl_TBCB; 1.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR045172; TBCB_N_Ubl.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
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; Developmental protein;
KW Differentiation; Microtubule; Neurogenesis; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..244
FT /note="Tubulin-folding cofactor B"
FT /id="PRO_0000083533"
FT DOMAIN 183..225
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q99426"
FT MOD_RES 98
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99426"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99426"
FT MOD_RES 219
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99426"
SQ SEQUENCE 244 AA; 27518 MW; D135E9DA88998927 CRC64;
MEVTGLSAPT VNVFISSSLN SFRSQKRYSR SLTVAEFKCK LQLVVGSPAS CMELELYGPD
DKFCCKLDQD DALLGSYPVD DGCRIHVIDH SGARLGEYED ISKVEKYEIS QEAYEQRQDS
IRSFLKRNKL GRFNEEERAQ QEAENSQRLI EEEAQASTIP VGSRCEVRTP GQPPRRGTVM
YVGLTDFKPG YWIGIRYDEP LGKNDGSVNG KRYFECQAKY GAFVKPSVVT VGDFPEEDYG
LDEM
