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 27-MAR-2024, entry version 138. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; Ricin (A subunit), domain 1; 1. DR Gene3D; 4.10.470.10; Ricin (A Subunit), domain 2; 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; -; 1. DR PANTHER; PTHR33453:SF34; DUF6598 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00161; RIP; 1. DR PRINTS; PR00396; SHIGARICIN. DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 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 //