Reviewed, UniProtKB/Swiss-Prot P16094 (RIP1_MOMCH)

Names and origin

Protein names	Recommended name:     Ribosome-inactivating protein momordin I     EC=3.2.2.22 Alternative name(s):     rRNA N-glycosidase     Alpha-momorcharin       Short name=Alpha-MMC
Organism	Momordica charantia (Bitter gourd) (Balsam pear)
Taxonomic identifier	3673 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Cucurbitales › Cucurbitaceae › Momordica

Protein attributes

Sequence length	286 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)

Catalytic activity	Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence similarities	Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.

Ontologies

Keywords
Biological process	Plant defense
Domain	Signal
Molecular function	Hydrolase Protein synthesis inhibitor Toxin
PTM	Glycoprotein
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
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.2 Ref.3

Chain

24 – 269

246

Ribosome-inactivating protein momordin I

PRO_0000030770

Propeptide

270 – 286

17

Removed in mature form

PRO_0000030771

Sites

Active site

183

1

Amino acid modifications

Glycosylation

250

1

N-linked (GlcNAc...)

CAR_000082

Secondary structure

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286

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 – 162

11

Helix

167 – 180

14

Helix

182 – 186

5

Helix

188 – 196

9

Beta strand

198 – 200

3

Helix

206 – 225

20

Helix

226 – 228

3

Beta strand

231 – 239

9

Beta strand

245 – 250

6

Helix

254 – 257

4

Helix

266 – 268

3

Sequences

	Sequence		Length	Mass (Da)
	P16094-1 [UniParc]. Last modified December 1, 1992. Version 2. Checksum: E1B013ABEBC216CF	FASTA	286	31,532
	10 20 30 40 50 60 MSRFSVLSFL ILAIFLGGSI VKGDVSFRLS GADPRSYGMF IKDLRNALPF REKVYNIPLL 70 80 90 100 110 120 LPSVSGAGRY LLMHLFNYDG KTITVAVDVT NVYIMGYLAD TTSYFFNEPA AELASQYVFR 130 140 150 160 170 180 DARRKITLPY SGNYERLQIA AGKPREKIPI GLPALDSAIS TLLHYDSTAA AGALLVLIQT 190 200 210 220 230 240 TAEAARFKYI EQQIQERAYR DEVPSLATIS LENSWSGLSK QIQLAQGNNG IFRTPIVLVD 250 260 270 280 NKGNRVQITN VTSKVVTSNI QLLLNTRNIA EGDNGDVSTT HGFSSY

References

[1]	"Cloning of the cDNA of alpha-momorcharin: a ribosome inactivating protein." Ho W.K.K., Liu S.C., Shaw P.C., Yeung H.W., Ng T.B., Chan W.Y. Biochim. Biophys. Acta 1088:311-314(1991) [PubMed: 2001404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Seed.
[2]	"N-terminal sequence of some ribosome-inactivating proteins." Montecucchi P.-C., Lazzarini A.M., Barbieri L., Stirpe F., Soria M., Lappi D. Int. J. Pept. Protein Res. 33:263-267(1989) [PubMed: 2753596] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-38. Tissue: Seed.
[3]	"Trichokirin, a ribosome-inactivating protein from the seeds of Trichosanthes kirilowii Maximowicz. Purification, partial characterization and use for preparation of immunotoxins." Casellas P., Dussossoy D., Falasca A.I., Barbieri L., Guillemot J.-C., Ferrara P., Bolognesi A., Cenini P., Stirpe F. Eur. J. Biochem. 176:581-588(1988) [PubMed: 3262509] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-70. Tissue: Seed.
[4]	"The N-glycosidase mechanism of ribosome-inactivating proteins implied by crystal structures of alpha-momorcharin." Ren J., Wang Y., Dong Y., Stuart D.I. Structure 2:7-16(1994) [PubMed: 8075985] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]	"Crystal structure of momordin, a type I ribosome inactivating protein from the seeds of Momordica charantia." Husain J., Tickle I.J., Wood S.P. FEBS Lett. 342:154-158(1994) [PubMed: 8143869] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.16 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 (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X57682 mRNA. Translation: CAA40869.1.

PIR

RLPUGG. S14273.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AHA	X-ray	2.20	A	24-269	[»]
1AHB	X-ray	2.20	A	24-269	[»]
1AHC	X-ray	2.00	A	24-269	[»]
1F8Q	X-ray	2.20	A	24-286	[»]
1MOM	X-ray	2.16	A	24-269	[»]
1MRG	X-ray	1.80	A	24-286	[»]
1MRH	X-ray	2.00	A	24-286	[»]
1MRI	X-ray	2.20	A	24-286	[»]

ModBase

Search...

PTM databases

GlycoSuiteDB

P16094.

Enzyme and pathway databases

BRENDA

3.2.2.22. 273563.

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.

Entry information

Entry name

RIP1_MOMCH

Accession

Primary (citable) accession number: P16094
Secondary accession number(s): P24697

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	December 1, 1992
Last modified:	June 16, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)