RIPT_TRIKI
ID RIPT_TRIKI Reviewed; 289 AA.
AC P09989;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Ribosome-inactivating protein alpha-trichosanthin;
DE Short=Alpha-TCS;
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase;
DE Flags: Precursor;
OS Trichosanthes kirilowii (Chinese snake gourd) (Chinese cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Trichosanthes.
OX NCBI_TaxID=3677;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Maximowicz;
RX PubMed=1999291; DOI=10.1016/0378-1119(91)90061-f;
RA Shaw P.C., Yung M.H., Zhu R.H., Ho W.K.K., Ng T.B., Yeung H.W.;
RT "Cloning of trichosanthin cDNA and its expression in Escherichia coli.";
RL Gene 97:267-272(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Maximowicz; TISSUE=Leaf;
RX PubMed=2341400; DOI=10.1016/s0021-9258(19)38940-9;
RA Chow T., Feldman R.A., Lovett M., Piatak M.;
RT "Isolation and DNA sequence of a gene encoding alpha-trichosanthin, a type
RT I ribosome-inactivating protein.";
RL J. Biol. Chem. 265:8670-8674(1990).
RN [3]
RP PROTEIN SEQUENCE OF 24-270.
RC STRAIN=Maximowicz; TISSUE=Tuberous root;
RX PubMed=2341399; DOI=10.1016/s0021-9258(19)38939-2;
RA Collins E.J., Robertus J.D., Lopresti M., Stone K.L., Williams K.R., Wu P.,
RA Hwang K., Piatak M.;
RT "Primary amino acid sequence of alpha-trichosanthin and molecular models
RT for abrin A-chain and alpha-trichosanthin.";
RL J. Biol. Chem. 265:8665-8669(1990).
RN [4]
RP PROTEIN SEQUENCE OF 24-270.
RC TISSUE=Tuberous root;
RA Wang Y., Qian R.Q., Gu Z.W., Jin S.W., Zhang L.Q., Xia Z.X., Tian G.Y.,
RA Ni C.Z.;
RT "Scientific evaluation of Tian Hua Fen (THF): history, chemistry and
RT application.";
RL Pure Appl. Chem. 58:789-798(1986).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS).
RX PubMed=8066085; DOI=10.1002/prot.340190103;
RA Zhou F., Fu Z., Chen M., Lin Y., Pan K.;
RT "Structure of trichosanthin at 1.88-A resolution.";
RL Proteins 19:4-13(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=7619070; DOI=10.1042/bj3090285;
RA Huang Q., Liu S., Tang Y., Jin S., Wang Y.;
RT "Studies on crystal structures, active-centre geometry and depurinating
RT mechanism of two ribosome-inactivating proteins.";
RL Biochem. J. 309:285-298(1995).
CC -!- FUNCTION: Inactivates eukaryotic 60S ribosomal subunits.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC adenosine on the 28S rRNA.; EC=3.2.2.22;
CC -!- MISCELLANEOUS: Abortion-inducing protein. Inhibits HIV-1 infection and
CC replication.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; M34858; AAA34207.1; -; mRNA.
DR EMBL; J05434; AAA34206.1; -; Genomic_DNA.
DR PIR; JT0566; RLTZT.
DR PDB; 1GIS; X-ray; 1.70 A; A=24-270.
DR PDB; 1GIU; X-ray; 1.80 A; A=24-270.
DR PDB; 1J4G; X-ray; 2.00 A; A/B/C/D=24-270.
DR PDB; 1MRJ; X-ray; 1.60 A; A=24-270.
DR PDB; 1MRK; X-ray; 1.60 A; A=24-270.
DR PDB; 1NLI; X-ray; 1.93 A; A=24-270.
DR PDB; 1QD2; X-ray; 1.86 A; A=24-270.
DR PDB; 1TCS; X-ray; 1.70 A; A=24-270.
DR PDB; 2JDL; X-ray; 2.20 A; A/B=25-270.
DR PDB; 2JJR; X-ray; 2.30 A; A=24-270.
DR PDB; 2VS6; X-ray; 2.40 A; A/B=24-270.
DR PDBsum; 1GIS; -.
DR PDBsum; 1GIU; -.
DR PDBsum; 1J4G; -.
DR PDBsum; 1MRJ; -.
DR PDBsum; 1MRK; -.
DR PDBsum; 1NLI; -.
DR PDBsum; 1QD2; -.
DR PDBsum; 1TCS; -.
DR PDBsum; 2JDL; -.
DR PDBsum; 2JJR; -.
DR PDBsum; 2VS6; -.
DR AlphaFoldDB; P09989; -.
DR SMR; P09989; -.
DR MINT; P09989; -.
DR Allergome; 2807; Tri k RIP.
DR ABCD; P09989; 4 sequenced antibodies.
DR BRENDA; 3.2.2.22; 6463.
DR EvolutionaryTrace; P09989; -.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.40.420.10; -; 1.
DR Gene3D; 4.10.470.10; -; 1.
DR InterPro; IPR036041; Ribosome-inact_prot_sf.
DR InterPro; IPR017989; Ribosome_inactivat_1/2.
DR InterPro; IPR001574; Ribosome_inactivat_prot.
DR InterPro; IPR017988; Ribosome_inactivat_prot_CS.
DR InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR PANTHER; PTHR33453; PTHR33453; 1.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SUPFAM; SSF56371; SSF56371; 1.
DR PROSITE; PS00275; SHIGA_RICIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral protein; Direct protein sequencing; Hydrolase;
KW Plant defense; Protein synthesis inhibitor; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2341399, ECO:0000269|Ref.4"
FT CHAIN 24..270
FT /note="Ribosome-inactivating protein alpha-trichosanthin"
FT /id="PRO_0000030765"
FT PROPEP 271..289
FT /note="Removed in mature form"
FT /id="PRO_0000030766"
FT ACT_SITE 183
FT /evidence="ECO:0000250"
FT CONFLICT 57..60
FT /note="IPLL -> LPLI (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..84
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="I -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="V -> VDAGLPRNAVL (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..144
FT /note="KI -> GL (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="K -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..216
FT /note="WS -> LWL (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="Q -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="S -> T (in Ref. 2; AAA34206)"
FT /evidence="ECO:0000305"
FT CONFLICT 246..266
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="T -> M (in Ref. 2; AAA34206)"
FT /evidence="ECO:0000305"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1MRJ"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:1MRJ"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1MRJ"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1MRJ"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:1MRJ"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:1MRJ"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1MRJ"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1MRJ"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1MRJ"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1MRJ"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:1MRJ"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1MRJ"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1MRJ"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:1MRJ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1MRJ"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:1MRJ"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:1MRJ"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:1MRJ"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:1MRJ"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1MRK"
FT HELIX 206..226
FT /evidence="ECO:0007829|PDB:1MRJ"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:1MRJ"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:1MRJ"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:1MRJ"
FT HELIX 254..258
FT /evidence="ECO:0007829|PDB:1MRJ"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:1MRJ"
SQ SEQUENCE 289 AA; 31676 MW; 5CE09BB630575BB9 CRC64;
MIRFLVLSLL ILTLFLTTPA VEGDVSFRLS GATSSSYGVF ISNLRKALPN ERKLYDIPLL
RSSLPGSQRY ALIHLTNYAD ETISVAIDVT NVYIMGYRAG DTSYFFNEAS ATEAAKYVFK
DAMRKVTLPY SGNYERLQTA AGKIRENIPL GLPALDSAIT TLFYYNANSA ASALMVLIQS
TSEAARYKFI EQQIGKRVDK TFLPSLAIIS LENSWSALSK QIQIASTNNG QFESPVVLIN
AQNQRVTITN VDAGVVTSNI ALLLNRNNMA AMDDDVPMTQ SFGCGSYAI
