TSP36_TAESA
ID TSP36_TAESA Reviewed; 314 AA.
AC Q7YZT0; O77442;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Small heat shock protein p36;
DE Short=Tsp36;
DE AltName: Full=R-Tso2;
OS Taenia saginata (Beef tapeworm) (Cysticercus bovis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=6206;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ABSENCE OF SPECIFIC ANTIBODIES IN INFECTED
RP ANIMALS, AND DEVELOPMENTAL STAGE.
RC TISSUE=Larva;
RX PubMed=9610643; DOI=10.1007/s004360050422;
RA Benitez L., Harrison L.J.S., Parkhouse R.M.E., Garate T.;
RT "Sequence and preliminary characterisation of a Taenia saginata oncosphere
RT gene homologue of the small heat-shock protein family.";
RL Parasitol. Res. 84:423-425(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF CYS-147, MASS
RP SPECTROMETRY, AND SUBUNIT.
RX PubMed=15326597; DOI=10.1002/prot.20220;
RA Kappe G., Aquilina J.A., Wunderink L., Kamps B., Robinson C.V., Garate T.,
RA Boelens W.C., de Jong W.W.;
RT "Tsp36, a tapeworm small heat-shock protein with a duplicated alpha-
RT crystallin domain, forms dimers and tetramers with good chaperone-like
RT activity.";
RL Proteins 57:109-117(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=16165157; DOI=10.1016/j.jmb.2005.08.025;
RA Stamler R., Kappe G., Boelens W.C., Slingsby C.;
RT "Wrapping the alpha-crystallin domain fold in a chaperone assembly.";
RL J. Mol. Biol. 353:68-79(2005).
CC -!- FUNCTION: Has chaperone activity towards unfolded proteins (in vitro).
CC {ECO:0000269|PubMed:15326597}.
CC -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000269|PubMed:15326597,
CC ECO:0000269|PubMed:16165157}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Detected in larvae. May be expressed in the
CC oncospere. {ECO:0000269|PubMed:9610643}.
CC -!- MASS SPECTROMETRY: Mass=35441; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15326597};
CC -!- MISCELLANEOUS: Not precipitated by antisera from cattle infected with
CC T.saginata, suggesting that the protein is not accessible to the host
CC immune system.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; Y12513; CAA73114.1; -; mRNA.
DR EMBL; AJ551179; CAD80255.1; -; Genomic_DNA.
DR PDB; 2BOL; X-ray; 2.50 A; A/B=1-314.
DR PDBsum; 2BOL; -.
DR AlphaFoldDB; Q7YZT0; -.
DR SMR; Q7YZT0; -.
DR PRIDE; Q7YZT0; -.
DR EvolutionaryTrace; Q7YZT0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.790; -; 2.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR45640; PTHR45640; 2.
DR Pfam; PF00011; HSP20; 2.
DR SUPFAM; SSF49764; SSF49764; 2.
DR PROSITE; PS01031; SHSP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..314
FT /note="Small heat shock protein p36"
FT /id="PRO_0000291951"
FT DOMAIN 95..200
FT /note="sHSP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT DOMAIN 216..314
FT /note="sHSP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT MUTAGEN 147
FT /note="C->R: Abolishes formation of tetramers. No effect on
FT dimerization."
FT /evidence="ECO:0000269|PubMed:15326597"
FT CONFLICT 18..20
FT /note="SLI -> TEF (in Ref. 1; CAA73114)"
FT /evidence="ECO:0000305"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:2BOL"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:2BOL"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:2BOL"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:2BOL"
FT HELIX 63..78
FT /evidence="ECO:0007829|PDB:2BOL"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2BOL"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:2BOL"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:2BOL"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 177..189
FT /evidence="ECO:0007829|PDB:2BOL"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:2BOL"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:2BOL"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 250..265
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:2BOL"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:2BOL"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:2BOL"
SQ SEQUENCE 314 AA; 35572 MW; 53005A1147D42D4D CRC64;
MSIFPTRDSR DLSSRRRSLI DWEFPQMALV PLDQVFDWAE RSRQSLHDDI VNMHRNLFSL
EPFTAMDNAF ESVMKEMSAI QPREFHPELE YTQPGELDFL KDAYEVGKDG RLHFKVYFNV
KNFKAEEITI KADKNKLVVR AQKSVACGDA AMSESVGRSI PLPPSVDRNH IQATITTDDV
LVIEAPVNEP NYKAIKLSPE KGLAIQPSEV QERQLAVKNK EGLEIVTAED GSKKIHLELK
VDPHFAPKDV KVWAKGNKVY VHGVTGKEEK TENASHSEHR EFYKAFVTPE VVDASKTQAE
IVDGLMVVEA PLFK
