TCTP_PLAKN
ID TCTP_PLAKN Reviewed; 171 AA.
AC P84152;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Translationally-controlled tumor protein homolog;
DE Short=TCTP;
GN Name=TCTP;
OS Plasmodium knowlesi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5850;
RN [1] {ECO:0000312|PDB:1TXJ}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RA Walker J.R., Vedadi M., Sharma S., Houston S., Lew J., Amani M., Wasney G.,
RA Skarina T., Bray J., Hui R.;
RT "Crystal structure and biophysical characterization of translationally
RT controlled tumour-associated protein (TCTP) from Plasmodium knowlesi.";
RL Submitted (JUL-2004) to the PDB data bank.
CC -!- FUNCTION: Involved in calcium binding and microtubule stabilization.
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 PDB; 1TXJ; X-ray; 2.00 A; A=1-171.
DR PDBsum; 1TXJ; -.
DR AlphaFoldDB; P84152; -.
DR SMR; P84152; -.
DR VEuPathDB; PlasmoDB:PKA1H_100027700; -.
DR VEuPathDB; PlasmoDB:PKNH_1022600; -.
DR VEuPathDB; PlasmoDB:PKNOH_S07460700; -.
DR eggNOG; KOG1727; Eukaryota.
DR EvolutionaryTrace; P84152; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; PS51797; TCTP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm.
FT CHAIN 1..171
FT /note="Translationally-controlled tumor protein homolog"
FT /id="PRO_0000211292"
FT DOMAIN 1..171
FT /note="TCTP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01133"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1TXJ"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1TXJ"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1TXJ"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1TXJ"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1TXJ"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1TXJ"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1TXJ"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1TXJ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1TXJ"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:1TXJ"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1TXJ"
FT HELIX 84..105
FT /evidence="ECO:0007829|PDB:1TXJ"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1TXJ"
FT HELIX 110..126
FT /evidence="ECO:0007829|PDB:1TXJ"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1TXJ"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1TXJ"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1TXJ"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1TXJ"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1TXJ"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1TXJ"
SQ SEQUENCE 171 AA; 19854 MW; 319D5FA986F5825D CRC64;
MKVYKDVFTN DEVCSDSYNQ EDPFGIADFR EIAFEVKSNK RIKGNDDYGI ADNSEEAVDG
MGADVEQVID IVDSFQLTST SLSKKEYSVY IKNYMQKILK YLEEKKPDRV DVFKTKAQPL
IKHILTNFDD FEFYMGESLD MDAGLTYSYY KGEEVTPRFV YISDGLYEEK F