Skip Header

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

P11140 (ABRA_ABRPR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Abrin-a

Cleaved into the following 3 chains:

  1. Abrin-a A chain
    EC=3.2.2.22
    Alternative name(s):
    rRNA N-glycosidase
  2. Linker peptide
  3. Abrin-a B chain
OrganismAbrus precatorius (Indian licorice) (Glycine abrus)
Taxonomic identifier3816 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Abreae › Abrus

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. Abrin-a is more toxic than ricin.

The B chain is a galactose-specific lectin that facilitates the binding of abrin to the cell membrane that precedes endocytosis.

Catalytic activity

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

Subunit structure

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).

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Abrin-a A chain
PRO_0000030729
Peptide252 – 26110Linker peptide
PRO_0000030730
Chain262 – 528267Abrin-a B chain
PRO_0000030731

Regions

Domain273 – 400128Ricin B-type lectin 1
Repeat283 – 325431-alpha
Repeat326 – 366411-beta
Repeat369 – 401331-gamma
Domain403 – 527125Ricin B-type lectin 2
Repeat414 – 449362-alpha
Repeat453 – 492402-beta
Repeat495 – 528342-gamma

Sites

Active site1641 By similarity

Amino acid modifications

Modified residue11Pyrrolidone carboxylic acid
Glycosylation3611N-linked (GlcNAc...)
Glycosylation4011N-linked (GlcNAc...)
Disulfide bond247 ↔ 269Interchain (between A and B chains)
Disulfide bond286 ↔ 305
Disulfide bond329 ↔ 346
Disulfide bond417 ↔ 430
Disulfide bond456 ↔ 473

Experimental info

Mutagenesis2001N → P: 46-fold less potent protein synthesis inhibition. Ref.5
Sequence conflict11Q → E in AAA32624. Ref.1
Sequence conflict2021Missing AA sequence Ref.2
Sequence conflict2981N → Y AA sequence Ref.4
Sequence conflict4271M → L AA sequence Ref.4
Sequence conflict4671T → P AA sequence Ref.4
Sequence conflict4831V → L AA sequence Ref.4

Secondary structure

1 ...................................................................................................... 528
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11140 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: A1F76BECD5B9A827

FASTA52859,244
        10         20         30         40         50         60 
QDRPIKFSTE GATSQSYKQF IEALRERLRG GLIHDIPVLP DPTTLQERNR YITVELSNSD 

        70         80         90        100        110        120 
TESIEVGIDV TNAYVVAYRA GTQSYFLRDA PSSASDYLFT GTDQHSLPFY GTYGDLERWA 

       130        140        150        160        170        180 
HQSRQQIPLG LQALTHGISF FRSGGNDNEE KARTLIVIIQ MVAEAARFRY ISNRVRVSIQ 

       190        200        210        220        230        240 
TGTAFQPDAA MISLENNWDN LSRGVQESVQ DTFPNQVTLT NIRNEPVIVD SLSHPTVAVL 

       250        260        270        280        290        300 
ALMLFVCNPP NANQSPLLIR SIVEKSKICS SRYEPTVRIG GRDGMCVDVY DNGYHNGNRI 

       310        320        330        340        350        360 
IMWKCKDRLE ENQLWTLKSD KTIRSNGKCL TTYGYAPGSY VMIYDCTSAV AEATYWEIWD 

       370        380        390        400        410        420 
NGTIINPKSA LVLSAESSSM GGTLTVQTNE YLMRQGWRTG NNTSPFVTSI SGYSDLCMQA 

       430        440        450        460        470        480 
QGSNVWMADC DSNKKEQQWA LYTDGSIRSV QNTNNCLTSK DHKQGSTILL MGCSNGWASQ 

       490        500        510        520 
RWVFKNDGSI YSLYDDMVMD VKGSDPSLKQ IILWPYTGKP NQIWLTLF

« Hide

References

[1]"Primary structure of three distinct isoabrins determined by cDNA sequencing. Conservation and significance."
Hung C.-H., Lee M.-C., Lee T.-C., Lin J.-Y.
J. Mol. Biol. 229:263-267(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The complete amino acid sequence of the A-chain of abrin-a, a toxic protein from the seeds of Abrus precatorius."
Funatsu G., Taguchi Y., Kamenosono M., Yanaka M.
Agric. Biol. Chem. 52:1095-1097(1988)
Cited for: PROTEIN SEQUENCE OF 1-251.
Tissue: Seed.
[3]"Direct molecular cloning and expression of two distinct abrin A-chains."
Evensen G., Mathiesen A., Sundan A.
J. Biol. Chem. 266:6848-6852(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251.
Tissue: Leaf.
[4]"The complete primary structure of abrin-a B chain."
Chen Y.-L., Chow L.-P., Tsugita A., Lin J.-Y.
FEBS Lett. 309:115-118(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 262-528.
[5]"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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-200.
[6]"Crystal structure of abrin-a at 2.14 A."
Tahirov T.H., Lu T.-H., Liaw Y.-C., Chen Y.-L., Lin J.-Y.
J. Mol. Biol. 250:354-367(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS).
[7]Erratum
Tahirov T.H., Lu T.-H., Liaw Y.-C., Chen Y.-L., Lin J.-Y.
J. Mol. Biol. 252:154-154(1995)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M98344 mRNA. Translation: AAA32624.1.
X54872 Genomic DNA. No translation available.
PIRTZLSA. S32429.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ABRX-ray2.14A2-251[»]
B262-528[»]
ProteinModelPortalP11140.
SMRP11140. Positions 1-251, 262-528.
ModBaseSearch...

Proteomic databases

PRIDEP11140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
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]
PfamPF00652. Ricin_B_lectin. 2 hits.
PF00161. RIP. 1 hit.
[Graphical view]
PRINTSPR00396. SHIGARICIN.
SMARTSM00458. RICIN. 2 hits.
[Graphical view]
SUPFAMSSF56371. Ribosome_inactivat_prot. 1 hit.
SSF50370. RicinB_like. 2 hits.
PROSITEPS50231. RICIN_B_LECTIN. 2 hits.
PS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11140.

Entry information

Entry nameABRA_ABRPR
AccessionPrimary (citable) accession number: P11140
Secondary accession number(s): P28589
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: June 1, 1994
Last modified: April 3, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents