P24817 (RIP3_MOMCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribosome-inactivating protein beta-momorcharin
Short name=B-MMC
EC=3.2.2.22

Alternative name(s):
MAP 30
rRNA N-glycosidase

Gene names

Name:	MAP30
Synonyms:	RIP

Organism

Momordica charantia (Bitter gourd) (Balsam pear)

Taxonomic identifier

3673 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Momordiceae › 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)

Function	Irreversibly relaxes supercoiled DNA and catalyzes double-stranded breakage. Acts also as a ribosome inactivating protein.
Catalytic activity	Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Post-translational modification	Bound to a branched hexasaccharide.
Miscellaneous	Possesses anti-HIV and antitumoral activities. Inhibits HIV-1 integrase. Manganese or zinc required for enhancing substrate binding rather than catalysis. The oligosaccharide does not influence the fold of the polypeptide chain and probably does not play a role in the enzymatic function. Is not toxic to uninfected normal cells as it cannot enter into them.
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
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 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.5

Chain

24 – 286

263

Ribosome-inactivating protein beta-momorcharin

PRO_0000030773

Sites

Active site

93

1

By similarity

Active site

132

1

By similarity

Active site

181

1

By similarity

Active site

184

1

By similarity

Amino acid modifications

Glycosylation

74

1

N-linked (GlcNAc...)

Experimental info

Sequence conflict

23

1

G → M Ref.3

Sequence conflict

23

1

G → M Ref.4

Sequence conflict

37

1

Y → T AA sequence Ref.5

Sequence conflict

67

1

S → P AA sequence Ref.5

Sequence conflict

147

1

D → E in CAC08217. Ref.4

Sequence conflict

188

1

I → T in AAB35194. Ref.1

Sequence conflict

228

1

G → A in CAC08217. Ref.4

Secondary structure

1

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286

Helix Strand Turn

Details...

Beta strand

25 – 28

4

Helix

29 – 31

3

Helix

34 – 45

12

Beta strand

50 – 54

5

Beta strand

57 – 60

4

Beta strand

68 – 76

9

Beta strand

82 – 88

7

Turn

89 – 91

3

Beta strand

94 – 99

6

Beta strand

102 – 106

5

Helix

111 – 116

6

Beta strand

121 – 128

8

Helix

132 – 139

8

Helix

143 – 145

3

Helix

150 – 161

12

Turn

165 – 167

3

Helix

168 – 177

10

Helix

180 – 184

5

Helix

186 – 194

9

Beta strand

196 – 200

5

Helix

205 – 210

6

Turn

211 – 214

4

Helix

215 – 222

8

Turn

223 – 228

6

Beta strand

229 – 237

9

Beta strand

243 – 248

6

Helix

252 – 256

5

Helix

264 – 269

6

Turn

274 – 276

3

Turn

279 – 281

3

Sequences

	Sequence		Length	Mass (Da)
	P24817 [UniParc]. Last modified April 26, 2004. Version 2. Checksum: 6B2DF55A41D8F921	FASTA	286	32,031
	10 20 30 40 50 60 MVKCLLLSFL IIAIFIGVPT AKGDVNFDLS TATAKTYTKF IEDFRATLPF SHKVYDIPLL 70 80 90 100 110 120 YSTISDSRRF ILLNLTSYAY ETISVAIDVT NVYVVAYRTR DVSYFFKESP PEAYNILFKG 130 140 150 160 170 180 TRKITLPYTG NYENLQTAAH KIRENIDLGL PALSSAITTL FYYNAQSAPS ALLVLIQTTA 190 200 210 220 230 240 EAARFKYIER HVAKYVATNF KPNLAIISLE NQWSALSKQI FLAQNQGGKF RNPVDLIKPT 250 260 270 280 GERFQVTNVD SDVVKGNIKL LLNSRASTAD ENFITTMTLL GESVVN

References

[1]	"Anti-HIV and anti-tumor activities of recombinant MAP30 from bitter melon." Lee-Huang S., Huang P.L., Chen H.-C., Huang P.L., Bourinbaiar A., Huang H.I., Kung H.-F. Gene 161:151-156(1995) [PubMed: 7665070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Leaf.
[2]	Quanhong Y., Rihe P., Aisheng X. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Cloning rip gene and identification of its resistance to Aspergillus flavus." Wei Y.-F., Cai L.-B., Zhuang W. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE OF 23-286.
[4]	"Expression of a RIP gene from Momordica charantia in E. coli." Nguyen Huy H., Nghiem Ngoc M., Dao Huy P., Le Tran B., Nong Van H. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE OF 23-286.
[5]	"MAP 30: a new inhibitor of HIV-1 infection and replication." Lee-Huang S., Huang P.L., Nara P.L., Chen H.-C., Kung H.-F., Huang P., Huang H.I., Huang P.L. FEBS Lett. 272:12-18(1990) [PubMed: 1699801] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-67. Tissue: Seed.
[6]	"Solution structure of anti-HIV-1 and anti-tumor protein MAP30: structural insights into its multiple functions." Wang Y.-X., Neamati N., Jacob J., Palmer I., Stahl S.J., Kaufman J.D., Huang P.L., Huang P.L., Winslow H.E., Pommier Y., Wingfield P.T., Lee-Huang S., Bax A., Torchia D.A. Cell 99:433-442(1999) [PubMed: 10571185] [Abstract] Cited for: STRUCTURE BY NMR OF 24-286, DNA-BINDING.
[7]	"Three-dimensional structure of beta-momorcharin at 2.55 A resolution." Yuan Y.-R., He Y.-N., Xiong J.-P., Xia Z.-X. Acta Crystallogr. D 55:1144-1151(1999) [PubMed: 10329776] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 24-272.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S79450 Genomic DNA. Translation: AAB35194.2.
AF284811 Genomic DNA. Translation: AAG33028.1.
AY523412 mRNA. Translation: AAS17014.1.
AJ294541 Genomic DNA. Translation: CAC08217.1.

PIR

B61318.
JC4235.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CF5	X-ray	2.55	A/B	24-272	[»]
1D8V	NMR	-	A	24-286	[»]

ProteinModelPortal

P24817.

SMR

P24817. Positions 24-286.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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.

SUPFAM

SSF56371. Ribosome_inactivat_prot. 1 hit.

PROSITE

PS00275. SHIGA_RICIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RIP3_MOMCH

Accession

Primary (citable) accession number: P24817
Secondary accession number(s): Q41257, Q9FSH2, Q9FUV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	April 26, 2004
Last modified:	May 31, 2011
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program