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Reviewed, UniProtKB/Swiss-Prot Q9M6E9 (AGGL_ABRPR)

Last modified May 26, 2009. Version 47. 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 · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Agglutinin-1
Alternative name(s):
    Agglutinin I
Cleaved into the following 2 chains:
    1- Recommended name:
            Agglutinin-1 chain A
              EC=3.2.2.22
        Alternative name(s):
            AAG-A
    2- Recommended name:
            Agglutinin-1 chain B
        Alternative name(s):
            AAG-B
Gene names
Name: AAG
OrganismAbrus precatorius (Indian licorice) (Crab's eye)
Taxonomic identifier3816 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Abreae › Abrus

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Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA By similarity. Less toxic than abrin-a. Ref.1 UniProtKB P28590

The B chain is a galactose-specific lectin that facilitates the binding to the cell membrane that precedes endocytosis By similarity. UniProtKB P28590

Catalytic activity

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. UniProtKB P11140

Subunit structure

Heterotetramer of two A and two B chains. Ref.3

Domain

The B chain is composed of two domains, each domain consists of 3 homologous subdomains (alpha, beta, gamma).

Miscellaneous

Induces cytokine production and proliferation of splenocytes and thymocytes in mice. Ref.2

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.1
Chain21 – 278258Agglutinin-1 chain A Ref.1
PRO_0000248489
Propeptide279 – 2802Linker peptide Ref.1
PRO_0000248490
Chain281 – 547267Agglutinin-1 chain B Ref.1
PRO_0000248491

Regions

Domain292 – 419128Ricin B-type lectin 1
Repeat302 – 344431-alpha
Repeat345 – 385411-beta
Repeat388 – 420331-gamma
Domain422 – 546125Ricin B-type lectin 2
Repeat433 – 468362-alpha
Repeat472 – 511402-beta
Repeat514 – 547342-gamma

Sites

Active site1831 By similarity UniProtKB P11140

Amino acid modifications

Modified residue211Pyrrolidone carboxylic acid By similarity UniProtKB P28590
Glycosylation3801N-linked (GlcNAc...) Potential UniProtKB P11140
Glycosylation4201N-linked (GlcNAc...) Potential UniProtKB P11140
Disulfide bond266 ↔ 288Interchain (between A and B chains) By similarity UniProtKB P11140
Disulfide bond305 ↔ 324 By similarity UniProtKB P11140
Disulfide bond348 ↔ 365 By similarity UniProtKB P11140
Disulfide bond436 ↔ 449 By similarity UniProtKB P11140
Disulfide bond475 ↔ 492 By similarity UniProtKB P11140

Experimental info

Mutagenesis2191P → N: 7-fold more potent in protein synthesis inhibition in vitro. Ref.1

Secondary structure

1 ........................................................................................................ 547
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9M6E9-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 355A325C2354A1BD

FASTA54761,248
        10         20         30         40         50         60 
MKFETTKNKL HGNAYYQAQF QDPIKFTTGS ATPASYNQFI DALRERLTGG LIYGIPVLRD 

        70         80         90        100        110        120 
PSTVEKPNQY VTVELSYSDT VSIQLGIDLT NAYVVAYRAG SESFFFRNAP ASASTYLFTG 

       130        140        150        160        170        180 
TQQYSLPFDG NYDDLEKWAH QSRQRISLGL EALRQGIKFL RSGASDDEEI ARTLIVIIQM 

       190        200        210        220        230        240 
VAEAARFRYV SKLVVISLSN RAAFQPDPSM LSLENTWEPL SRAVQHTVQD TFPQNVTLIN 

       250        260        270        280        290        300 
VRQERVVVSS LSHPSVSALA LMLFVCNPLN ATQSPLLIRS VVEQSKICSS HYEPTVRIGG 

       310        320        330        340        350        360 
RDGLCVDVSD NAYNNGNPII LWKCKDQLEV NQLWTLKSDK TIRSKGKCLT TYGYAPGNYV 

       370        380        390        400        410        420 
MIYDCSSAVA EATYWDIWDN GTIINPKSGL VLSAESSSMG GTLTVQKNDY RMRQGWRTGN 

       430        440        450        460        470        480 
DTSPFVTSIA GFFKLCMEAH GNSMWLDVCD ITKEEQQWAV YPDGSIRPVQ NTNNCLTCEE 

       490        500        510        520        530        540 
HKQGATIVMM GCSNAWASQR WVFKSDGTIY NLYDDMVMDV KSSDPSLKQI ILWPYTGNAN 


QMWATLF

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References

[1]"Primary structure and function analysis of the Abrus precatorius agglutinin A chain by site-directed mutagenesis. Pro(199) Of amphiphilic alpha-helix H impairs protein synthesis inhibitory activity."
Liu C.-L., Tsai C.-C., Lin S.-C., Wang L.-I., Hsu C.-I., Hwang M.-J., Lin J.-Y.
J. Biol. Chem. 275:1897-1901(2000) [PubMed: 10636890] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-278 AND 281-543, FUNCTION, MUTAGENESIS OF PRO-219.
[2]"Immunomodulatory role of native and heat denatured agglutinin from Abrus precatorius."
Tripathi S., Maiti T.K.
Int. J. Biochem. Cell Biol. 37:451-462(2005) [PubMed: 15474989] [Abstract]
Cited for: IMMUNOMODULATORY ROLE.
[3]"Structure-function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin."
Bagaria A., Surendranath K., Ramagopal U.A., Ramakumar S., Karande A.A.
J. Biol. Chem. 281:34465-34474(2006) [PubMed: 16772301] [Abstract]
Cited for: SUBUNIT, 3D-STRUCTURE MODELING.

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Cross-references

Sequence databases

AF190173 mRNA. Translation: AAF28309.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2Q3NX-ray3.50A21-280[»]
B281-547[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.

Enzyme and pathway databases

BRENDA3.2.2.22. 273549.

Family and domain databases

InterProIPR001574. Ribosome_inactivat_prot.
IPR017988. Ribosome_inactivat_prot_CS.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
IPR000772. Ricin_B_lectin.
[Graphical view]
Gene3DG3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit.
G3DSA:4.10.470.10. Ribosome_inactivat_prot_sub2. 1 hit.
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...

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Entry information

Entry nameAGGL_ABRPR
AccessionPrimary (citable) accession number: Q9M6E9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2000
Last modified: May 26, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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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 · Cross-references · Entry information · Relevant documents