Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P09989

- RIPT_TRIKI

UniProt

P09989 - RIPT_TRIKI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribosome-inactivating protein alpha-trichosanthin

Gene
N/A
Organism
Trichosanthes kirilowii (Chinese snake gourd) (Chinese cucumber)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Inactivates eukaryotic 60S ribosomal subunits.

Catalytic activityi

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei183 – 1831By similarity

GO - Molecular functioni

  1. rRNA N-glycosylase activity Source: UniProtKB-EC

GO - Biological processi

  1. defense response Source: UniProtKB-KW
  2. negative regulation of translation Source: UniProtKB-KW
  3. regulation of defense response to virus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antiviral protein, Hydrolase, Protein synthesis inhibitor, Toxin

Keywords - Biological processi

Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome-inactivating protein alpha-trichosanthin (EC:3.2.2.22)
Short name:
Alpha-TCS
Alternative name(s):
rRNA N-glycosidase
OrganismiTrichosanthes kirilowii (Chinese snake gourd) (Chinese cucumber)
Taxonomic identifieri3677 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeSicyoeaeTrichosanthes

Pathology & Biotechi

Protein family/group databases

Allergomei2807. Tri k RIP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23232 PublicationsAdd
BLAST
Chaini24 – 270247Ribosome-inactivating protein alpha-trichosanthinPRO_0000030765Add
BLAST
Propeptidei271 – 28919Removed in mature formPRO_0000030766Add
BLAST

Interactioni

Protein-protein interaction databases

MINTiMINT-193117.

Structurei

Secondary structure

1
289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 284
Helixi34 – 4613
Beta strandi50 – 545
Beta strandi57 – 604
Helixi66 – 694
Beta strandi70 – 767
Beta strandi82 – 887
Turni89 – 913
Beta strandi94 – 996
Beta strandi102 – 1054
Helixi109 – 1146
Turni115 – 1173
Beta strandi123 – 1275
Helixi134 – 1418
Helixi145 – 1473
Helixi152 – 16312
Helixi167 – 18014
Helixi182 – 1865
Helixi188 – 1958
Beta strandi198 – 2003
Helixi206 – 22621
Turni227 – 2304
Beta strandi231 – 2399
Beta strandi245 – 2506
Helixi254 – 2585
Turni266 – 2683

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GISX-ray1.70A24-270[»]
1GIUX-ray1.80A24-270[»]
1J4GX-ray2.00A/B/C/D24-270[»]
1MRJX-ray1.60A24-270[»]
1MRKX-ray1.60A24-270[»]
1NLIX-ray1.93A24-270[»]
1QD2X-ray1.86A24-270[»]
1TCSX-ray1.70A24-270[»]
2JDLX-ray2.20A/B25-270[»]
2JJRX-ray2.30A24-270[»]
2VS6X-ray2.40A/B24-270[»]
ProteinModelPortaliP09989.
SMRiP09989. Positions 24-270.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09989.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProiIPR001574. 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]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PRINTSiPR00396. SHIGARICIN.
SUPFAMiSSF56371. SSF56371. 1 hit.
PROSITEiPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09989-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIRFLVLSLL ILTLFLTTPA VEGDVSFRLS GATSSSYGVF ISNLRKALPN
60 70 80 90 100
ERKLYDIPLL RSSLPGSQRY ALIHLTNYAD ETISVAIDVT NVYIMGYRAG
110 120 130 140 150
DTSYFFNEAS ATEAAKYVFK DAMRKVTLPY SGNYERLQTA AGKIRENIPL
160 170 180 190 200
GLPALDSAIT TLFYYNANSA ASALMVLIQS TSEAARYKFI EQQIGKRVDK
210 220 230 240 250
TFLPSLAIIS LENSWSALSK QIQIASTNNG QFESPVVLIN AQNQRVTITN
260 270 280
VDAGVVTSNI ALLLNRNNMA AMDDDVPMTQ SFGCGSYAI
Length:289
Mass (Da):31,676
Last modified:November 1, 1990 - v2
Checksum:i5CE09BB630575BB9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 604IPLL → LPLI AA sequence 1 PublicationCurated
Sequence conflicti82 – 843Missing AA sequence 1 PublicationCurated
Sequence conflicti87 – 871I → L AA sequence 1 PublicationCurated
Sequence conflicti92 – 921V → VDAGLPRNAVL AA sequence 1 PublicationCurated
Sequence conflicti143 – 1442KI → GL AA sequence 1 PublicationCurated
Sequence conflicti196 – 1961K → S AA sequence 1 PublicationCurated
Sequence conflicti215 – 2162WS → LWL AA sequence 1 PublicationCurated
Sequence conflicti231 – 2311Q → T AA sequence 1 PublicationCurated
Sequence conflicti234 – 2341S → T in AAA34206. (PubMed:2341400)Curated
Sequence conflicti246 – 26621Missing AA sequence 1 PublicationCuratedAdd
BLAST
Sequence conflicti247 – 2471T → M in AAA34206. (PubMed:2341400)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34858 mRNA. Translation: AAA34207.1.
J05434 Genomic DNA. Translation: AAA34206.1.
PIRiJT0566. RLTZT.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34858 mRNA. Translation: AAA34207.1 .
J05434 Genomic DNA. Translation: AAA34206.1 .
PIRi JT0566. RLTZT.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P09989.
SMRi P09989. Positions 24-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-193117.

Protein family/group databases

Allergomei 2807. Tri k RIP.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P09989.

Family and domain databases

Gene3Di 3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProi 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 ]
Pfami PF00161. RIP. 1 hit.
[Graphical view ]
PRINTSi PR00396. SHIGARICIN.
SUPFAMi SSF56371. SSF56371. 1 hit.
PROSITEi PS00275. SHIGA_RICIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Entry informationi

Entry nameiRIPT_TRIKI
AccessioniPrimary (citable) accession number: P09989
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Abortion-inducing protein. Inhibits HIV-1 infection and replication.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3