Reviewed, UniProtKB/Swiss-Prot P09989 (RIPT_TRIKI)

Names and origin

Protein names	Recommended name:     Ribosome-inactivating protein alpha-trichosanthin       Short name=Alpha-TCS     EC=3.2.2.22 Alternative name(s):     rRNA N-glycosidase
Organism	Trichosanthes kirilowii (Mongolian snake-gourd)
Taxonomic identifier	3677 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Trichosanthes

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Inactivates eukaryotic 60S ribosomal subunits.
Catalytic activity	Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Miscellaneous	Abortion-inducing protein. Inhibits HIV-1 infection and replication.
Sequence similarities	Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.

Ontologies

Keywords
Biological process	Plant defense
Domain	Signal
Molecular function	Antiviral protein Hydrolase Protein synthesis inhibitor Toxin
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW regulation of defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	rRNA N-glycosylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.3 Ref.4

Chain

24 – 270

247

Ribosome-inactivating protein alpha-trichosanthin

PRO_0000030765

Propeptide

271 – 289

19

Removed in mature form

PRO_0000030766

Sites

Active site

183

1

By similarity

Experimental info

Sequence conflict

57 – 60

4

IPLL → LPLI AA sequence Ref.4

Sequence conflict

82 – 84

3

Missing AA sequence Ref.4

Sequence conflict

87

1

I → L AA sequence Ref.4

Sequence conflict

92

1

V → VDAGLPRNAVL AA sequence Ref.4

Sequence conflict

143 – 144

2

KI → GL AA sequence Ref.4

Sequence conflict

196

1

K → S AA sequence Ref.4

Sequence conflict

215 – 216

2

WS → LWL AA sequence Ref.4

Sequence conflict

231

1

Q → T AA sequence Ref.4

Sequence conflict

234

1

S → T in AAA34206. Ref.2

Sequence conflict

246 – 266

21

Missing AA sequence Ref.4

Sequence conflict

247

1

T → M in AAA34206. Ref.2

Secondary structure

1

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289

Helix Strand Turn

Details...

Beta strand

25 – 29

5

Helix

34 – 47

14

Beta strand

50 – 54

5

Beta strand

57 – 60

4

Helix

66 – 69

4

Beta strand

70 – 76

7

Beta strand

82 – 88

7

Turn

89 – 91

3

Beta strand

94 – 99

6

Beta strand

102 – 105

4

Helix

109 – 114

6

Turn

115 – 117

3

Beta strand

123 – 127

5

Helix

134 – 141

8

Helix

145 – 147

3

Helix

152 – 163

12

Turn

167 – 169

3

Helix

170 – 180

11

Helix

182 – 186

5

Helix

188 – 195

8

Helix

206 – 226

21

Turn

227 – 230

4

Beta strand

231 – 239

9

Beta strand

245 – 250

6

Helix

254 – 258

5

Helix

266 – 268

3

Sequences

	Sequence		Length	Mass (Da)
	P09989-1 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: 5CE09BB630575BB9	FASTA	289	31,676
	10 20 30 40 50 60 MIRFLVLSLL ILTLFLTTPA VEGDVSFRLS GATSSSYGVF ISNLRKALPN ERKLYDIPLL 70 80 90 100 110 120 RSSLPGSQRY ALIHLTNYAD ETISVAIDVT NVYIMGYRAG DTSYFFNEAS ATEAAKYVFK 130 140 150 160 170 180 DAMRKVTLPY SGNYERLQTA AGKIRENIPL GLPALDSAIT TLFYYNANSA ASALMVLIQS 190 200 210 220 230 240 TSEAARYKFI EQQIGKRVDK TFLPSLAIIS LENSWSALSK QIQIASTNNG QFESPVVLIN 250 260 270 280 AQNQRVTITN VDAGVVTSNI ALLLNRNNMA AMDDDVPMTQ SFGCGSYAI

References

[1]	"Cloning of trichosanthin cDNA and its expression in Escherichia coli." Shaw P.C., Yung M.H., Zhu R.H., Ho W.K.K., Ng T.B., Yeung H.W. Gene 97:267-272(1991) [PubMed: 1999291] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Maximowicz.
[2]	"Isolation and DNA sequence of a gene encoding alpha-trichosanthin, a type I ribosome-inactivating protein." Chow T., Feldman R.A., Lovett M., Piatak M. J. Biol. Chem. 265:8670-8674(1990) [PubMed: 2341400] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Maximowicz. Tissue: Leaf.
[3]	"Primary amino acid sequence of alpha-trichosanthin and molecular models for abrin A-chain and alpha-trichosanthin." Collins E.J., Robertus J.D., Lopresti M., Stone K.L., Williams K.R., Wu P., Hwang K., Piatak M. J. Biol. Chem. 265:8665-8669(1990) [PubMed: 2341399] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-270. Strain: Maximowicz. Tissue: Tuberous root.
[4]	"Scientific evaluation of Tian Hua Fen (THF): history, chemistry and application." Wang Y., Qian R.Q., Gu Z.W., Jin S.W., Zhang L.Q., Xia Z.X., Tian G.Y., Ni C.Z. Pure Appl. Chem. 58:789-798(1986) Cited for: PROTEIN SEQUENCE OF 24-270. Tissue: Tuberous root.
[5]	"Structure of trichosanthin at 1.88-A resolution." Zhou F., Fu Z., Chen M., Lin Y., Pan K. Proteins 19:4-13(1994) [PubMed: 8066085] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS).
[6]	"Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins." Huang Q., Liu S., Tang Y., Jin S., Wang Y. Biochem. J. 309:285-298(1995) [PubMed: 7619070] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34858 mRNA. Translation: AAA34207.1.
J05434 Genomic DNA. Translation: AAA34206.1.

PIR

RLTZT. JT0566.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GIS	X-ray	1.70	A	24-270	[»]
1GIU	X-ray	1.80	A	24-270	[»]
1J4G	X-ray	2.00	A/B/C/D	24-270	[»]
1MRJ	X-ray	1.60	A	24-270	[»]
1MRK	X-ray	1.60	A	24-270	[»]
1NLI	X-ray	1.93	A	24-270	[»]
1QD2	X-ray	1.86	A	24-270	[»]
1TCS	X-ray	1.70	A	24-270	[»]
2JDL	X-ray	2.20	A/B	25-270	[»]
2JJR	X-ray	2.30	A	24-270	[»]
2VS6	X-ray	2.40	A/B	24-270	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.2.2.22. 273574.

Family and domain databases

InterPro

IPR001574. Ribosome_inactivat_prot.
IPR017988. Ribosome_inactivat_prot_CS.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
[Graphical view]

Gene3D

G3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit.
G3DSA:4.10.470.10. Ribosome_inactivat_prot_sub2. 1 hit.

Pfam

PF00161. RIP. 1 hit.
[Graphical view]

PRINTS

PR00396. SHIGARICIN.

PROSITE

PS00275. SHIGA_RICIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00173. Adenine.
DB00131. Adenosine monophosphate.

Entry information

Entry name

RIPT_TRIKI

Accession

Primary (citable) accession number: P09989

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1990
Last modified:	February 9, 2010
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)