Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P06750 (AGGL_RICCO)

Last modified June 16, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Agglutinin
Alternative name(s):
    RCA
Cleaved into the following 2 chains:
    1- Recommended name:
            Agglutinin A chain
              EC=3.2.2.22
        Alternative name(s):
            rRNA N-glycosidase
    2- Recommended name:
            Agglutinin B chain
OrganismRicinus communis (Castor bean)
Taxonomic identifier3988 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus

Hide | Top

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

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

Sequence similarities

In the N-terminal section; belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.

Contains 2 ricin B-type lectin domains.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 290266Agglutinin A chain
PRO_0000030726
Propeptide291 – 30212Linker peptide Ref.2 Ref.3
PRO_0000030727
Chain303 – 564262Agglutinin B chain Ref.1
PRO_0000030728

Regions

Domain309 – 436128Ricin B-type lectin 1
Repeat319 – 361431-alpha
Repeat362 – 402411-beta
Repeat405 – 437331-gamma
Domain439 – 563125Ricin B-type lectin 2
Repeat450 – 485362-alpha
Repeat489 – 528402-beta
Repeat531 – 558282-gamma
Nucleotide binding104 – 1052AMP By similarity
Nucleotide binding145 – 1473AMP By similarity
Region32 – 343Carbohydrate binding
Region164 – 1696Carbohydrate binding By similarity
Region218 – 2203Carbohydrate binding By similarity
Region324 – 3285Carbohydrate binding
Region536 – 5394Carbohydrate binding By similarity
Region553 – 5575Carbohydrate binding By similarity

Sites

Active site2001 By similarity
Binding site741Carbohydrate; via amide nitrogen By similarity
Binding site3121Carbohydrate; via carbonyl oxygen
Binding site3371Carbohydrate
Binding site3421Carbohydrate
Binding site3481Carbohydrate
Binding site3811Carbohydrate
Binding site3971Carbohydrate
Binding site4371Carbohydrate

Amino acid modifications

Glycosylation341N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...)
Glycosylation4371N-linked (GlcNAc...)
Disulfide bond282 ↔ 306Interchain (between A and B chains)
Disulfide bond322 ↔ 341
Disulfide bond365 ↔ 382
Disulfide bond453 ↔ 466
Disulfide bond492 ↔ 509

Experimental info

Sequence conflict3311F → T AA sequence Ref.2
Sequence conflict3621N → D AA sequence Ref.2
Sequence conflict3741R → G AA sequence Ref.2
Sequence conflict4041R → T AA sequence Ref.2
Sequence conflict5521F → V AA sequence Ref.2

Secondary structure

1 ............................................................................................ 564
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P06750-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: D455F2A72F609759

FASTA56462,851
        10         20         30         40         50         60 
MYAVATWLCF GSTSGWSFTL EDNNIFPKQY PIINFTTADA TVESYTNFIR AVRSHLTTGA 

        70         80         90        100        110        120 
DVRHEIPVLP NRVGLPISQR FILVELSNHA ELSVTLALDV TNAYVVGCRA GNSAYFFHPD 

       130        140        150        160        170        180 
NQEDAEAITH LFTDVQNSFT FAFGGNYDRL EQLGGLRENI ELGTGPLEDA ISALYYYSTC 

       190        200        210        220        230        240 
GTQIPTLARS FMVCIQMISE AARFQYIEGE MRTRIRYNRR SAPDPSVITL ENSWGRLSTA 

       250        260        270        280        290        300 
IQESNQGAFA SPIQLQRRNG SKFNVYDVSI LIPIIALMVY RCAPPPSSQF SLLIRPVVPN 

       310        320        330        340        350        360 
FNADVCMDPE PIVRIVGRNG LCVDVTGEEF FDGNPIQLWP CKSNTDWNQL WTLRKDSTIR 

       370        380        390        400        410        420 
SNGKCLTISK SSPRQQVVIY NCSTATVGAT RWQIWDNRTI INPRSGLVLA ATSGNSGTKL 

       430        440        450        460        470        480 
TVQTNIYAVS QGWLPTNNTQ PFVTTIVGLY GMCLQANSGK VWLEDCTSEK AEQQWALYAD 

       490        500        510        520        530        540 
GSIRPQQNRD NCLTTDANIK GTVVKILSCG PASSGQRWMF KNDGTILNLY NGLVLDVRRS 

       550        560 
DPSLKQIIVH PFHGNLNQIW LPLF

« Hide

Hide | Top

References

[1]"The primary sequence of Ricinus communis agglutinin. Comparison with ricin."
Roberts L.M., Lamb F.I., Pappin D.J.C., Lord J.M.
J. Biol. Chem. 260:15682-15686(1985) [PubMed: 2999130] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The complete amino acid sequence of the B-chain of the Ricinus communis agglutinin isolated from large-grain castor bean seeds."
Araki T., Yoshioka Y., Funatsu G.
Biochim. Biophys. Acta 872:277-285(1986)
Cited for: PROTEIN SEQUENCE OF 303-564.
Tissue: Seed.
[3]"Purification and physicochemical properties of ricins and agglutinins from Ricinus communis."
Lin T.T.-S., Li S.S.-L.
Eur. J. Biochem. 105:453-459(1980) [PubMed: 6768555] [Abstract]
Cited for: PROTEIN SEQUENCE OF 303-337.
[4]"Structure-function investigation complex of agglutinin from Ricinus communis with galactose."
Gabdoulkhakov A.G., Savochkina Y., Konareva N., Krauspenhaar R., Stoeva S., Nikonov S.V., Voelter W., Betzel C., Mikhailov A.M.
Submitted (DEC-2003) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 25-286 AND 303-564 IN COMPLEX WITH GALACTOSE, DISULFID BONDS.

Hide | Top

Cross-references

Sequence databases

M12089 mRNA. Translation: AAA33869.1.
S40368 mRNA. Translation: AAB22584.1.
PIRRLCSAG. A24261.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1RZOX-ray2.63A/C25-286[»]
B/D303-564[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.

PTM databases

GlycoSuiteDBP06750.

Enzyme and pathway databases

BRENDA3.2.2.22. 816.

Family and domain databases

InterProIPR001574. Ribosome_inactivat_prot.
IPR017988. Ribosome_inactivat_prot_CS.
IPR017989. Ribosome_inactivat_prot_subgr.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00652. Ricin_B_lectin. 2 hits.
PF00161. RIP. 1 hit.
[Graphical view]
PRINTSPR00396. SHIGARICIN.
SMARTSM00458. RICIN. 2 hits.
[Graphical view]
PROSITEPS50231. RICIN_B_LECTIN. 2 hits.
PS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameAGGL_RICCO
AccessionPrimary (citable) accession number: P06750
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents