TBCB_YEAST
ID TBCB_YEAST Reviewed; 254 AA.
AC P53904; D6W134;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Tubulin-specific chaperone B;
DE AltName: Full=Alpha-tubulin formation protein 1;
DE AltName: Full=Tubulin-folding cofactor B;
GN Name=ALF1; OrderedLocusNames=YNL148C; ORFNames=N1201, N1777;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9885248; DOI=10.1083/jcb.144.1.113;
RA Feierbach B., Nogales E., Downing K.H., Stearns T.;
RT "Alf1p, a CLIP-170 domain-containing protein, is functionally and
RT physically associated with alpha-tubulin.";
RL J. Cell Biol. 144:113-124(1999).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Acts to sequester alpha-tubulin from interaction with beta-
CC tubulin, raising the possibility that it plays a regulatory role in the
CC formation of the tubulin heterodimer.
CC -!- SUBUNIT: Binds to monomeric alpha-tubulin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC Note=Microtubule-associated.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TBCB family. {ECO:0000305}.
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DR EMBL; Z46843; CAA86878.1; -; Genomic_DNA.
DR EMBL; X92517; CAA63291.1; -; Genomic_DNA.
DR EMBL; Z71424; CAA96031.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10400.1; -; Genomic_DNA.
DR PIR; S55136; S55136.
DR RefSeq; NP_014251.1; NM_001182986.1.
DR AlphaFoldDB; P53904; -.
DR SMR; P53904; -.
DR BioGRID; 35680; 56.
DR DIP; DIP-901N; -.
DR STRING; 4932.YNL148C; -.
DR MaxQB; P53904; -.
DR PaxDb; P53904; -.
DR PRIDE; P53904; -.
DR EnsemblFungi; YNL148C_mRNA; YNL148C; YNL148C.
DR GeneID; 855574; -.
DR KEGG; sce:YNL148C; -.
DR SGD; S000005092; ALF1.
DR VEuPathDB; FungiDB:YNL148C; -.
DR eggNOG; KOG3206; Eukaryota.
DR HOGENOM; CLU_067577_2_0_1; -.
DR InParanoid; P53904; -.
DR OMA; WCGIEFD; -.
DR BioCyc; YEAST:G3O-33166-MON; -.
DR PRO; PR:P53904; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53904; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0043014; F:alpha-tubulin binding; IPI:SGD.
DR GO; GO:0008017; F:microtubule binding; IDA:SGD.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IDA:SGD.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT CHAIN 1..254
FT /note="Tubulin-specific chaperone B"
FT /id="PRO_0000083536"
FT DOMAIN 182..225
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 234..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 254 AA; 28354 MW; BEB01698DB3B3FCC CRC64;
MVRVVIESEL VRTEKELPNS LKLRQFKDRL YHVTGVEPED MEIVVKRQYD NKEIYSTKKG
GAYSNEDEDA NFLKGEEELI VVVTDSNAQS ISNQLATQAE GIPSMEVISE EDYLRRDQSV
LRWKMAHGYG RFNAAQQSQR AALAKQDEAY AREQLTAAIG RHCRVTVDGS APREAILRYV
GPLPLDVMGT WCGVEFPEAA GKNDGRINGV TLFGPVAPGH GSFVRPRAVE ILSKDEESAE
VEDVHDDVES DDEI
