[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/13.22.8019; PubMed=2999712 [NCBI, ExPASy, EBI, Israel, Japan] Halling K.C., Halling A.C., Murray E.E., Ladin B.F., Houston L.L., Weaver R.F.; "Genomic cloning and characterization of a ricin gene from Ricinus communis."; Nucleic Acids Res. 13:8019-8033(1985).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00040667; PubMed=1371405 [NCBI, ExPASy, EBI, Israel, Japan] Tregear J.W., Roberts L.M.; "The lectin gene family of Ricinus communis: cloning of a functional ricin gene and three lectin pseudogenes."; Plant Mol. Biol. 18:515-525(1992).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 12-576. PubMed=3838723 [NCBI, ExPASy, EBI, Israel, Japan] Lamb A., Roberts L.M., Lord J.M.; "Nucleotide sequence of cloned cDNA coding for preproricin."; Eur. J. Biochem. 148:265-270(1985).
[4]	PROTEIN SEQUENCE OF 36-302. Yoshitake S., Funatsu G., Funatsu M.; "Isolation and sequences of peptic peptides, and the complete sequence of Ile chain of ricin-D."; Agric. Biol. Chem. 42:1267-1274(1978).
[5]	PROTEIN SEQUENCE OF 315-576. AGRICOLA=IND80011393 Funatsu G., Kimura M., Funatsu M.; "Primary structure of Ala chain of ricin D."; Agric. Biol. Chem. 43:2221-2224(1979).
[6]	GLYCOSYLATION AT ASN-45 AND ASN-271, AND PARTIAL PROTEIN SEQUENCE. PubMed=1368517 [NCBI, ExPASy, EBI, Israel, Japan] Kimura Y., Kusuoku H., Tada M., Takagi S., Funatsu G.; "Structural analyses of sugar chains from ricin A-chain variant."; Agric. Biol. Chem. 54:157-162(1990).
[7]	REVIEW. DOI=10.1016/S0041-0101(01)00158-1; PubMed=11595634 [NCBI, ExPASy, EBI, Israel, Japan] Olsnes S., Kozlov J.V.; "Ricin."; Toxicon 39:1723-1728(2001).
[8]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). PubMed=3558397 [NCBI, ExPASy, EBI, Israel, Japan] Monfort W., Villafranca J.E., Monzingo A.F., Ernst S.R., Katzin B., Rutenber E., Xuong N.H., Hamlin R., Robertus J.D.; "The three-dimensional structure of ricin at 2.8 A."; J. Biol. Chem. 262:5398-5403(1987).
[9]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF A-CHAIN. DOI=10.1002/prot.340100309; PubMed=1881881 [NCBI, ExPASy, EBI, Israel, Japan] Katzin B.J., Collins E.J., Robertus J.D.; "Structure of ricin A-chain at 2.5 A."; Proteins 10:251-259(1991).
[10]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF B-CHAIN. DOI=10.1002/prot.340100310; PubMed=1881882 [NCBI, ExPASy, EBI, Israel, Japan] Rutenber E., Robertus J.D.; "Structure of ricin B-chain at 2.5-A resolution."; Proteins 10:260-269(1991).
[11]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF A-CHAIN. DOI=10.1006/jmbi.1994.1739; PubMed=7990130 [NCBI, ExPASy, EBI, Israel, Japan] Weston S.A., Tucker A.D., Thatcher D.R., Derbyshire D.J., Pauptit R.A.; "X-ray structure of recombinant ricin A-chain at 1.8-A resolution."; J. Mol. Biol. 244:410-422(1994).
[12]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT HIS-215. DOI=10.1021/bi960880n; PubMed=8780513 [NCBI, ExPASy, EBI, Israel, Japan] Day P.J., Ernst S.R., Frankel A.E., Monzingo A.F., Pascal J.M., Molina-Svinth M.C., Robertus J.D.; "Structure and activity of an active site substitution of ricin A chain."; Biochemistry 35:11098-11103(1996).
[13]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF A-CHAIN. DOI=10.1006/jmbi.1996.0865; PubMed=9086280 [NCBI, ExPASy, EBI, Israel, Japan] Yan X., Hollis T., Svinth M., Day P., Monzingo A.F., Milne G.W., Robertus J.D.; "Structure-based identification of a ricin inhibitor."; J. Mol. Biol. 266:1043-1049(1997).
[14]	MUTAGENESIS. DOI=10.1093/protein/5.8.775; PubMed=1287657 [NCBI, ExPASy, EBI, Israel, Japan] Kin Y., Robertus J.D.; "Analysis of several key active site residues of ricin A chain by mutagenesis and X-ray crystallography."; Protein Eng. 5:775-779(1992).
[15]	MUTAGENESIS OF ARG-83; LEU-109; ASP-110; VAL-111 AND ASN-132. DOI=10.1038/nbt800; PubMed=12627168 [NCBI, ExPASy, EBI, Israel, Japan] Smallshaw J.E., Ghetie V., Rizo J., Fulmer J.R., Trahan L.L., Ghetie M.-A., Vitetta E.S.; "Genetic engineering of an immunotoxin to eliminate pulmonary vascular leak in mice."; Nat. Biotechnol. 21:387-391(2003).

Comments

FUNCTION: Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).
CATALYTIC ACTIVITY: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
SUBUNIT: Disulfide-linked dimer of A and B chains.
DOMAIN: The B chain is composed of two domains, each domain consists of 3 homologous subdomains (alpha, beta, gamma).
BIOTECHNOLOGY: A deglycosylated A chain may be linked to monoclonal antibodies to produce immunotoxins exploited in cancer treatment. However, a point mutation should be introduced to eliminate vascular leak syndrome, a side effect resulting from endothelial damage.
SIMILARITY: In the N-terminal section; belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.
SIMILARITY: Contains 2 ricin B-type lectin domains.
SEQUENCE CAUTION:
- Sequence=Ref.4; Type=Miscellaneous discrepancy; Note=High number of conflicts with the sequence translated from DNA
- Sequence=Ref.5; Type=Miscellaneous discrepancy; Note=High number of conflicts with the sequence translated from DNA
WEB RESOURCE: Name=Protein Spotlight; Note=Baneful beans - Issue 31 of February 2003; URL="http://www.expasy.org/spotlight/back_issues/sptlt031.shtml";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X03179; CAA26939.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52908; CAA37095.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02388; CAA26230.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24041; RLCSD.

3D structure databases

PDB

1APG; X-ray; 3.00 A; A=36-302.	[ExPASy / RCSB / EBI]
1BR5; X-ray; 2.50 A; A=36-302.	[ExPASy / RCSB / EBI]
1BR6; X-ray; 2.30 A; A=36-302.	[ExPASy / RCSB / EBI]
1FMP; X-ray; 2.80 A; A=36-302.	[ExPASy / RCSB / EBI]
1IFS; X-ray; 2.00 A; A=38-298.	[ExPASy / RCSB / EBI]
1IFT; X-ray; 1.80 A; A=38-298.	[ExPASy / RCSB / EBI]
1IFU; X-ray; 2.40 A; A=38-298.	[ExPASy / RCSB / EBI]
1IL3; X-ray; 2.80 A; A=36-302.	[ExPASy / RCSB / EBI]
1IL4; X-ray; 2.60 A; A=36-302.	[ExPASy / RCSB / EBI]
1IL5; X-ray; 2.80 A; A/B=36-302.	[ExPASy / RCSB / EBI]
1IL9; X-ray; 3.10 A; A=36-302.	[ExPASy / RCSB / EBI]
1J1M; X-ray; 1.50 A; A=36-302.	[ExPASy / RCSB / EBI]
1OBS; X-ray; 2.20 A; A=36-302.	[ExPASy / RCSB / EBI]
1OBT; X-ray; 2.80 A; A=36-302.	[ExPASy / RCSB / EBI]
1RTC; X-ray; 2.30 A; A=36-302.	[ExPASy / RCSB / EBI]
1UQ4; X-ray; 1.90 A; A=40-302.	[ExPASy / RCSB / EBI]
1UQ5; X-ray; 1.40 A; A=40-302.	[ExPASy / RCSB / EBI]
1ZAM; X-ray; 2.40 A; A=36-302.	[ExPASy / RCSB / EBI]
1ZB0; X-ray; 1.80 A; A=36-302.	[ExPASy / RCSB / EBI]
1ZB2; X-ray; 2.09 A; A=36-302.	[ExPASy / RCSB / EBI]
2AAI; X-ray; 2.50 A; A=36-302, B=315-576.	[ExPASy / RCSB / EBI]
2P8N; X-ray; 1.94 A; A=36-302.	[ExPASy / RCSB / EBI]
2PJN; X-ray; 2.40 A; A=36-302.	[ExPASy / RCSB / EBI]
2PJO; X-ray; 1.80 A; A=36-302.	[ExPASy / RCSB / EBI]
2R2X; X-ray; 2.40 A; A=36-302.	[ExPASy / RCSB / EBI]
2R3D; X-ray; 2.09 A; A=36-302.	[ExPASy / RCSB / EBI]
2VC3; X-ray; 1.60 A; A=36-302.	[ExPASy / RCSB / EBI]
2VC4; X-ray; 1.39 A; A=36-302.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1APG; -.
1BR5; -.
1BR6; -.
1FMP; -.
1IFS; -.
1IFT; -.
1IFU; -.
1IL3; -.
1IL4; -.
1IL5; -.
1IL9; -.
1J1M; -.
1OBS; -.
1OBT; -.
1RTC; -.
1UQ4; -.
1UQ5; -.
1ZAM; -.
1ZB0; -.
1ZB2; -.
2AAI; -.
2P8N; -.
2PJN; -.
2PJO; -.
2R2X; -.
2R3D; -.
2VC3; -.
2VC4; -.

ModBase

P02879.

PTM databases

GlycoSuiteDB

P02879; -.

Ontologies

GO:0000166;	Molecular function: nucleotide binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030598;	Molecular function: rRNA N-glycosylase activity (inferred from electronic annotation from InterPro).
GO:0005529;	Molecular function: sugar binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006952;	Biological process: defense response (inferred from electronic annotation from UniProtKB-KW).
GO:0017148;	Biological process: negative regulation of translation (inferred from electronic annotation from InterPro).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001574; Ribosome_inactivat_prot.
IPR000772; Ricin_B_lectin.
Graphical view of domain structure.

Pfam

PF00652; Ricin_B_lectin; 2.
PF00161; RIP; 1.
Pfam graphical view of domain structure.

PRINTS

PR00396; SHIGARICIN.

SMART

SM00458; RICIN; 2.
SMART graphical view of domain structure.

PROSITE

PS50231; RICIN_B_LECTIN; 2.
PS00275; SHIGA_RICIN; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P02879.

Other

DrugBank

DB00173; Adenine.
DB00131; Adenosine monophosphate.

LinkHub

P02879; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Lectin; Nucleotide-binding; Plant defense; Protein synthesis inhibitor; Repeat; Signal; Toxin.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 35`	`35`
`CHAIN`	`36 302`	`267`	`Ricin A chain.`	`PRO_0000030741`
`PEPTIDE`	`303 314`	`12`	`Linker peptide.`	`PRO_0000030742`
`CHAIN`	`315 576`	`262`	`Ricin B chain.`	`PRO_0000030743`
`DOMAIN`	`321 448`	`128`	`Ricin B-type lectin 1.`
`REPEAT`	`331 373`	`43`	`1-alpha.`
`REPEAT`	`374 414`	`41`	`1-beta.`
`REPEAT`	`417 449`	`33`	`1-gamma.`
`DOMAIN`	`451 575`	`125`	`Ricin B-type lectin 2.`
`REPEAT`	`462 497`	`36`	`2-alpha.`
`REPEAT`	`501 540`	`40`	`2-beta.`
`REPEAT`	`543 570`	`28`	`2-gamma.`
`NP_BIND`	`115 116`	`2`	`AMP.`
`NP_BIND`	`156 158`	`3`	`AMP.`
`REGION`	`43 45`	`3`	`Carbohydrate binding (By similarity).`
`REGION`	`176 181`	`6`	`Carbohydrate binding.`
`REGION`	`230 232`	`3`	`Carbohydrate binding.`
`REGION`	`336 340`	`5`	`Carbohydrate binding.`
`REGION`	`548 551`	`4`	`Carbohydrate binding.`
`REGION`	`565 569`	`5`	`Carbohydrate binding.`
`ACT_SITE`	`212 212`
`BINDING`	`50 50`		`Carbohydrate; via amide nitrogen.`
`BINDING`	`85 85`		`Carbohydrate; via amide nitrogen.`
`BINDING`	`324 324`		`Carbohydrate; via carbonyl oxygen (By similarity).`
`BINDING`	`349 349`		`Carbohydrate.`
`BINDING`	`354 354`		`Carbohydrate.`
`BINDING`	`360 360`		`Carbohydrate.`
`BINDING`	`409 409`		`Carbohydrate (By similarity).`
`BINDING`	`449 449`		`Carbohydrate (By similarity).`
`CARBOHYD`	`45 45`		`N-linked (GlcNAc...) [GlycoSuiteDB].`	`CAR_000080`
`CARBOHYD`	`271 271`		`N-linked (GlcNAc...); partial [GlycoSuiteDB].`	`CAR_000081`
`CARBOHYD`	`409 409`		`N-linked (GlcNAc...).`
`CARBOHYD`	`449 449`		`N-linked (GlcNAc...).`
`DISULFID`	`294 318`		`Interchain (between A and B chains).`
`DISULFID`	`334 353`
`DISULFID`	`377 394`
`DISULFID`	`465 478`
`DISULFID`	`504 521`
`MUTAGEN`	`83 83`		`R->A: No effect on the toxic activity but suppresses the vascular leak syndrome.`
`MUTAGEN`	`109 109`		`L->A,M: No effect on the toxic activity or the vascular leak syndrome.`
`MUTAGEN`	`110 110`		`D->A,E,N: Suppresses the toxic activity.`
`MUTAGEN`	`111 111`		`V->A,M: No effect on the toxic activity or the vascular leak syndrome.`
`MUTAGEN`	`132 132`		`N->A: No effect on the toxic activity but Suppresses the vascular leak syndrome.`
`CONFLICT`	`76 76`		`E -> D (in Ref. 3; CAA26230).`
`CONFLICT`	`551 551`		`A -> R (in Ref. 3; CAA26230).`
`STRAND`	`43 48`	`6`
`HELIX`	`53 67`	`15`
`STRAND`	`77 79`	`3`
`HELIX`	`88 90`	`3`
`STRAND`	`91 98`	`8`
`STRAND`	`104 110`	`7`
`TURN`	`111 113`	`3`
`STRAND`	`116 121`	`6`
`STRAND`	`124 127`	`4`
`HELIX`	`133 139`	`7`
`STRAND`	`147 151`	`5`
`HELIX`	`158 165`	`8`
`HELIX`	`169 171`	`3`
`HELIX`	`176 188`	`13`
`HELIX`	`189 191`	`3`
`HELIX`	`196 215`	`20`
`HELIX`	`217 228`	`12`
`HELIX`	`237 255`	`19`
`STRAND`	`260 268`	`9`
`STRAND`	`274 279`	`6`
`HELIX`	`280 283`	`4`
`TURN`	`284 286`	`3`
`HELIX`	`330 332`	`3`
`STRAND`	`334 337`	`4`
`HELIX`	`338 340`	`3`
`STRAND`	`347 351`	`5`
`HELIX`	`359 361`	`3`
`STRAND`	`363 365`	`3`
`STRAND`	`369 373`	`5`
`STRAND`	`376 381`	`6`
`STRAND`	`388 393`	`6`
`TURN`	`394 396`	`3`
`HELIX`	`399 401`	`3`
`STRAND`	`412 414`	`3`
`TURN`	`415 418`	`4`
`STRAND`	`419 422`	`4`
`STRAND`	`433 436`	`4`
`HELIX`	`441 443`	`3`
`STRAND`	`454 459`	`6`
`HELIX`	`461 463`	`3`
`STRAND`	`465 469`	`5`
`STRAND`	`472 476`	`5`
`STRAND`	`487 489`	`3`
`STRAND`	`495 497`	`3`
`STRAND`	`503 507`	`5`
`STRAND`	`516 521`	`6`
`TURN`	`541 543`	`3`
`STRAND`	`546 549`	`4`
`HELIX`	`550 552`	`3`
`HELIX`	`554 556`	`3`
`STRAND`	`559 562`	`4`
`HELIX`	`568 570`	`3`
`STRAND`	`573 575`	`3`

Sequence information

Length: 576 AA [This is the length of the unprocessed precursor]

Molecular weight: 64091 Da [This is the MW of the unprocessed precursor]

CRC64: C14C4B77A8B5470D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKPGGNTIVI WMYAVATWLC FGSTSGWSFT LEDNNIFPKQ YPIINFTTAG ATVQSYTNFI 

        70         80         90        100        110        120 
RAVRGRLTTG ADVRHEIPVL PNRVGLPINQ RFILVELSNH AELSVTLALD VTNAYVVGYR 

       130        140        150        160        170        180 
AGNSAYFFHP DNQEDAEAIT HLFTDVQNRY TFAFGGNYDR LEQLAGNLRE NIELGNGPLE 

       190        200        210        220        230        240 
EAISALYYYS TGGTQLPTLA RSFIICIQMI SEAARFQYIE GEMRTRIRYN RRSAPDPSVI 

       250        260        270        280        290        300 
TLENSWGRLS TAIQESNQGA FASPIQLQRR NGSKFSVYDV SILIPIIALM VYRCAPPPSS 

       310        320        330        340        350        360 
QFSLLIRPVV PNFNADVCMD PEPIVRIVGR NGLCVDVRDG RFHNGNAIQL WPCKSNTDAN 

       370        380        390        400        410        420 
QLWTLKRDNT IRSNGKCLTT YGYSPGVYVM IYDCNTAATD ATRWQIWDNG TIINPRSSLV 

       430        440        450        460        470        480 
LAATSGNSGT TLTVQTNIYA VSQGWLPTNN TQPFVTTIVG LYGLCLQANS GQVWIEDCSS 

       490        500        510        520        530        540 
EKAEQQWALY ADGSIRPQQN RDNCLTSDSN IRETVVKILS CGPASSGQRW MFKNDGTILN 

       550        560        570 
LYSGLVLDVR ASDPSLKQII LYPLHGDPNQ IWLPLF

P02879 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools

ExPASy Home page

Site Map

Search ExPASy

Contact us

Swiss-Prot

Hosted by

Mirror sites: