Q06077 · ABRB_ABRPR

Function

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.
    EC:3.2.2.22 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

152750100150200250300350400450500
TypeIDPosition(s)Description
Active site163

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functioncarbohydrate binding
Molecular FunctionrRNA N-glycosylase activity
Molecular Functiontoxin activity
Biological Processdefense response
Biological Processnegative regulation of translation

Keywords

Names & Taxonomy

Protein names

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Abreae > Abrus

Accessions

  • Primary accession
    Q06077
  • Secondary accessions
    • P81374

Proteomes

PTM/Processing

Features

Showing features for modified residue, chain, glycosylation, disulfide bond, peptide.

TypeIDPosition(s)Description
Modified residue1Pyrrolidone carboxylic acid
ChainPRO_00000307321-250Abrin-b A chain
Glycosylation110N-linked (GlcNAc...) asparagine
Disulfide bond246↔268Interchain (between A and B chains)
PeptidePRO_0000030733251-260Linker peptide
ChainPRO_0000030734261-527Abrin-b B chain
Disulfide bond285↔304
Disulfide bond328↔345
Glycosylation360N-linked (GlcNAc...) asparagine
Glycosylation400N-linked (GlcNAc...) asparagine
Disulfide bond416↔429
Disulfide bond455↔472

Keywords

Interaction

Subunit

Disulfide-linked dimer of A and B chains.

Structure

Family & Domains

Features

Showing features for domain, repeat.

TypeIDPosition(s)Description
Domain272-399Ricin B-type lectin 1
Repeat282-3241-alpha
Repeat325-3651-beta
Repeat368-4001-gamma
Domain402-526Ricin B-type lectin 2
Repeat413-4482-alpha
Repeat452-4912-beta
Repeat494-5272-gamma

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.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    527
  • Mass (Da)
    59,115
  • Last updated
    1996-11-01 v1
  • Checksum
    3253AE490CE9494A
QDQVIKFTTEGATSQSYKQFIEALRQRLTGGLIHGIPVLPDPTTLQERNRYISVELSNSDTESIEAGIDVSNAYVVAYRAGNRSYFLRDAPTSASRYLFTGTQQYSLRFNGSYIDLERLARQTRQQIPLGLQALRHAISFLQSGTDDQEIARTLIVIIQMASEAARYRFISYRVGVSIRTNTAFQPDAAMISLENNWDNLSGGVQQSVQDTFPNAVTLRSVNNQPVIVDSLTHQSVAVLALMLFVCNPPNANQSPLLIRSIVEKSKICSSRYEPTVRIGGRNGMCVDVYDDGYHNGNRIIAWKCKDRLEENQLWTLKSDKTIRSNGKCLTTEGYAPGNYVMIYDCTSAVAEATYWEIWDNGTIINPKSALVLSAESSSMGGTLTVQTNEYLMRQGWRTGNNTSPFVTSISGYSDLCMQAQGSNVWLAYCDNNKKEQQWALYTDGSIRSVQNTNNCLTSKDHKQGSPIVLMACSNGWASQRWLFRNDGSIYNLHDDMVMDVKRSDPSLKEIILHPYHGKPNQIWLTLF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict282in Ref. 2; AA sequence
Sequence conflict291in Ref. 2; AA sequence
Sequence conflict350-351in Ref. 2; AA sequence
Sequence conflict378in Ref. 2; AA sequence
Sequence conflict426in Ref. 2; AA sequence
Sequence conflict428in Ref. 2; AA sequence
Sequence conflict431in Ref. 2; AA sequence
Sequence conflict484in Ref. 2; AA sequence
Sequence conflict491in Ref. 2; AA sequence
Sequence conflict493in Ref. 2; AA sequence
Sequence conflict502in Ref. 2; AA sequence
Sequence conflict509in Ref. 2; AA sequence
Sequence conflict513in Ref. 2; AA sequence
Sequence conflict516in Ref. 2; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M98345
EMBL· GenBank· DDBJ
AAA32625.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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