TCTP_DROME
ID TCTP_DROME Reviewed; 172 AA.
AC Q9VGS2; Q49UC2; Q95TW0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Translationally-controlled tumor protein homolog;
DE Short=TCTP;
GN Name=Tctp; ORFNames=CG4800;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP SEQUENCE REVISION.
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-58 AND THR-61, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Involved in calcium binding and microtubule stabilization.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9VGS2; Q9VND8: Rheb; NbExp=3; IntAct=EBI-100452, EBI-4372932;
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; AE014297; AAF54603.1; -; Genomic_DNA.
DR EMBL; AY058482; AAZ67515.1; -; mRNA.
DR RefSeq; NP_001303431.1; NM_001316502.1.
DR RefSeq; NP_650048.1; NM_141791.3.
DR AlphaFoldDB; Q9VGS2; -.
DR SMR; Q9VGS2; -.
DR BioGRID; 66475; 49.
DR DIP; DIP-18951N; -.
DR IntAct; Q9VGS2; 7.
DR STRING; 7227.FBpp0081820; -.
DR iPTMnet; Q9VGS2; -.
DR PaxDb; Q9VGS2; -.
DR DNASU; 41341; -.
DR EnsemblMetazoa; FBtr0082344; FBpp0081820; FBgn0037874.
DR EnsemblMetazoa; FBtr0347181; FBpp0312492; FBgn0037874.
DR GeneID; 41341; -.
DR KEGG; dme:Dmel_CG4800; -.
DR CTD; 41341; -.
DR FlyBase; FBgn0037874; Tctp.
DR VEuPathDB; VectorBase:FBgn0037874; -.
DR eggNOG; KOG1727; Eukaryota.
DR GeneTree; ENSGT00390000006051; -.
DR HOGENOM; CLU_095877_0_1_1; -.
DR InParanoid; Q9VGS2; -.
DR OMA; IVYEADC; -.
DR OrthoDB; 1439384at2759; -.
DR PhylomeDB; Q9VGS2; -.
DR SignaLink; Q9VGS2; -.
DR BioGRID-ORCS; 41341; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Tctp; fly.
DR GenomeRNAi; 41341; -.
DR PRO; PR:Q9VGS2; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037874; Expressed in capitellum (Drosophila) and 25 other tissues.
DR ExpressionAtlas; Q9VGS2; baseline and differential.
DR Genevisible; Q9VGS2; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:FlyBase.
DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:FlyBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:FlyBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:FlyBase.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:FlyBase.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
DR GO; GO:0033129; P:positive regulation of histone phosphorylation; IDA:FlyBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IMP:FlyBase.
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 Calcium; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..172
FT /note="Translationally-controlled tumor protein homolog"
FT /id="PRO_0000211283"
FT DOMAIN 1..172
FT /note="TCTP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01133"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 91
FT /note="K -> N (in Ref. 3; AAZ67515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 19637 MW; 8EA92FE8D37FC979 CRC64;
MKIYKDIITG DEMFADTYKM KLVDDVIYEV YGKLITRQGD DIKLEGANAS AEEADEGTDI
TSESGVDVVL NHRLTECFAF GDKKSYTLYL KDYMKKVLAK LEEKSPDQVD IFKTNMNKAM
KDILGRFKEL QFFTGESMDC DGMVALVEYR EINGDSVPVL MFFKHGLEEE KC
