TCTP_YEAST
ID TCTP_YEAST Reviewed; 167 AA.
AC P35691; D6VXN1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Translationally-controlled tumor protein homolog;
DE Short=TCTP;
DE AltName: Full=Microtubule and mitochondria-interacting protein 1;
DE AltName: Full=Translation machinery-associated protein 19;
GN Name=TMA19; Synonyms=MMI1; OrderedLocusNames=YKL056C; ORFNames=YKL312;
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=8091862; DOI=10.1002/yea.320100008;
RA Rasmussen S.W.;
RT "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and
RT TOA2 genes, an open reading frame (ORF) similar to a translationally
RT controlled tumour protein, one ORF containing motifs also found in plant
RT storage proteins and 13 ORFs with weak or no homology to known proteins.";
RL Yeast 10:S63-S68(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 1-50; 65-79 AND 112-118.
RA Klier H., Lottspeich F.;
RL Submitted (MAR-1994) to the PIR data bank.
RN [5]
RP PROTEIN SEQUENCE OF 6-17.
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=9038161; DOI=10.1074/jbc.272.9.5544;
RA Norbeck J., Blomberg A.;
RT "Metabolic and regulatory changes associated with growth of Saccharomyces
RT cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol
RT dissimilation via the dihydroxyacetone pathway.";
RL J. Biol. Chem. 272:5544-5554(1997).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16806052; DOI=10.1016/j.bbabio.2006.05.022;
RA Rinnerthaler M., Jarolim S., Heeren G., Palle E., Perju S., Klinger H.,
RA Bogengruber E., Madeo F., Braun R.J., Breitenbach-Koller L.,
RA Breitenbach M., Laun P.;
RT "MMI1 (YKL056c, TMA19), the yeast orthologue of the translationally
RT controlled tumor protein (TCTP) has apoptotic functions and interacts with
RT both microtubules and mitochondria.";
RL Biochim. Biophys. Acta 1757:631-638(2006).
RN [9]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-15, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in protein synthesis. Involved in microtubule
CC stabilization. {ECO:0000269|PubMed:16702403,
CC ECO:0000269|PubMed:16806052}.
CC -!- SUBUNIT: Interacts with the 40S and 60S ribosomal subunits. Interacts
CC with microtubules. {ECO:0000269|PubMed:16702403}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16806052}. Mitochondrion
CC {ECO:0000269|PubMed:16806052}. Note=After induction of apoptosis or
CC mild oxidative stress, reversibly translocates from the cytoplasm to
CC mitochondria, where it is associated with the outer surface.
CC {ECO:0000269|PubMed:16806052}.
CC -!- MISCELLANEOUS: Present with 27800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TCTP family. {ECO:0000255|PROSITE-
CC ProRule:PRU01133}.
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DR EMBL; X75781; CAA53416.1; -; Genomic_DNA.
DR EMBL; Z28056; CAA81893.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09101.1; -; Genomic_DNA.
DR PIR; S37878; S37878.
DR RefSeq; NP_012867.1; NM_001179622.1.
DR AlphaFoldDB; P35691; -.
DR SMR; P35691; -.
DR BioGRID; 34077; 237.
DR DIP; DIP-2116N; -.
DR IntAct; P35691; 13.
DR MINT; P35691; -.
DR STRING; 4932.YKL056C; -.
DR iPTMnet; P35691; -.
DR SWISS-2DPAGE; P35691; -.
DR MaxQB; P35691; -.
DR PaxDb; P35691; -.
DR PRIDE; P35691; -.
DR TopDownProteomics; P35691; -.
DR EnsemblFungi; YKL056C_mRNA; YKL056C; YKL056C.
DR GeneID; 853809; -.
DR KEGG; sce:YKL056C; -.
DR SGD; S000001539; TMA19.
DR VEuPathDB; FungiDB:YKL056C; -.
DR eggNOG; KOG1727; Eukaryota.
DR GeneTree; ENSGT00390000006051; -.
DR HOGENOM; CLU_095877_0_0_1; -.
DR InParanoid; P35691; -.
DR OMA; IVYEADC; -.
DR BioCyc; YEAST:G3O-31855-MON; -.
DR PRO; PR:P35691; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P35691; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:SGD.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
DR Gene3D; 2.170.150.10; -; 1.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR011323; Mss4/transl-control_tumour.
DR InterPro; IPR034737; TCTP.
DR InterPro; IPR018103; Translation_control_tumour_CS.
DR InterPro; IPR018105; Translational_control_tumour_p.
DR PANTHER; PTHR11991; PTHR11991; 1.
DR Pfam; PF00838; TCTP; 1.
DR PRINTS; PR01653; TCTPROTEIN.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS01002; TCTP_1; 1.
DR PROSITE; PS01003; TCTP_2; 1.
DR PROSITE; PS51797; TCTP_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Microtubule;
KW Mitochondrion; Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..167
FT /note="Translationally-controlled tumor protein homolog"
FT /id="PRO_0000211311"
FT DOMAIN 1..167
FT /note="TCTP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01133"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 19..20
FT /note="DA -> AD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 18741 MW; C4407A3B3B77124A CRC64;
MIIYKDIFSN DELLSDAYDA KLVDDVIYEA DCAMVNVGGD NIDIGANPSA EGGDDDVEEG
AEMVNNVVHS FRLQQTAFDK KSFLTYIKGY MKAVKAKLQE TNPEEVPKFE KGAQTYVKKV
IGSFKDWEFF TGESMDPDAM VVMLNYREDG TTPFVAIWKH GIVEEKI
