TCTP_SCHPO
ID TCTP_SCHPO Reviewed; 168 AA.
AC Q10344;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Translationally-controlled tumor protein homolog;
DE Short=TCTP;
DE AltName: Full=p23fyp;
GN Name=p23fy; ORFNames=SPAC1F12.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=11473261; DOI=10.1038/90415;
RA Thaw P., Baxter N.J., Hounslow A.M., Price C., Waltho J.P., Craven C.J.;
RT "Structure of TCTP reveals unexpected relationship with guanine nucleotide-
RT free chaperones.";
RL Nat. Struct. Biol. 8:701-704(2001).
CC -!- FUNCTION: Involved in calcium binding and microtubule stabilization (By
CC similarity). May be a guanine nucleotide-free chaperone (GFC).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TCTP family. {ECO:0000255|PROSITE-
CC ProRule:PRU01133}.
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DR EMBL; CU329670; CAA93806.1; -; Genomic_DNA.
DR PIR; T38060; S67445.
DR RefSeq; NP_594328.1; NM_001019749.2.
DR PDB; 1H6Q; NMR; -; A=1-168.
DR PDB; 1H7Y; NMR; -; A=1-168.
DR PDBsum; 1H6Q; -.
DR PDBsum; 1H7Y; -.
DR AlphaFoldDB; Q10344; -.
DR BMRB; Q10344; -.
DR SMR; Q10344; -.
DR BioGRID; 278935; 7.
DR STRING; 4896.SPAC1F12.02c.1; -.
DR iPTMnet; Q10344; -.
DR MaxQB; Q10344; -.
DR PaxDb; Q10344; -.
DR PRIDE; Q10344; -.
DR EnsemblFungi; SPAC1F12.02c.1; SPAC1F12.02c.1:pep; SPAC1F12.02c.
DR GeneID; 2542475; -.
DR KEGG; spo:SPAC1F12.02c; -.
DR PomBase; SPAC1F12.02c; -.
DR VEuPathDB; FungiDB:SPAC1F12.02c; -.
DR eggNOG; KOG1727; Eukaryota.
DR HOGENOM; CLU_095877_0_0_1; -.
DR InParanoid; Q10344; -.
DR OMA; IVYEADC; -.
DR PhylomeDB; Q10344; -.
DR EvolutionaryTrace; Q10344; -.
DR PRO; PR:Q10344; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:1990624; F:guanyl nucleotide exchange factor inhibitor activity; ISO:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:PomBase.
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 3D-structure; Calcium; Chaperone; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..168
FT /note="Translationally-controlled tumor protein homolog"
FT /id="PRO_0000211310"
FT DOMAIN 1..168
FT /note="TCTP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01133"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1H6Q"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:1H6Q"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1H6Q"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1H6Q"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:1H6Q"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1H6Q"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1H6Q"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1H6Q"
FT HELIX 81..101
FT /evidence="ECO:0007829|PDB:1H6Q"
FT HELIX 106..122
FT /evidence="ECO:0007829|PDB:1H6Q"
FT TURN 123..128
FT /evidence="ECO:0007829|PDB:1H6Q"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1H6Q"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1H6Q"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1H6Q"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1H6Q"
SQ SEQUENCE 168 AA; 19049 MW; 52F749AF994C917F CRC64;
MLLYKDVISG DELVSDAYDL KEVDDIVYEA DCQMVTVKQG GDVDIGANPS AEDAEENAEE
GTETVNNLVY SFRLSPTSFD KKSYMSYIKG YMKAIKARLQ ESNPERVPVF EKNAIGFVKK
ILANFKDYDF YIGESMDPDA MVVLMNYRED GITPYMIFFK DGLVSEKF
