Q06077 · ABRB_ABRPR
- ProteinAbrin-b
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids527 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 163 | |||||
Sequence: E |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | carbohydrate binding | |
Molecular Function | rRNA N-glycosylase activity | |
Molecular Function | toxin activity | |
Biological Process | defense response | |
Biological Process | negative regulation of translation |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameAbrin-b
- Cleaved into 3 chains
Organism names
- Taxonomic lineageEukaryota > 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 accessionQ06077
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for modified residue, chain, glycosylation, disulfide bond, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000030732 | 1-250 | Abrin-b A chain | |||
Sequence: QDQVIKFTTEGATSQSYKQFIEALRQRLTGGLIHGIPVLPDPTTLQERNRYISVELSNSDTESIEAGIDVSNAYVVAYRAGNRSYFLRDAPTSASRYLFTGTQQYSLRFNGSYIDLERLARQTRQQIPLGLQALRHAISFLQSGTDDQEIARTLIVIIQMASEAARYRFISYRVGVSIRTNTAFQPDAAMISLENNWDNLSGGVQQSVQDTFPNAVTLRSVNNQPVIVDSLTHQSVAVLALMLFVCNPPN | ||||||
Glycosylation | 110 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 246↔268 | Interchain (between A and B chains) | ||||
Sequence: CNPPNANQSPLLIRSIVEKSKIC | ||||||
Peptide | PRO_0000030733 | 251-260 | Linker peptide | |||
Sequence: ANQSPLLIRS | ||||||
Chain | PRO_0000030734 | 261-527 | Abrin-b B chain | |||
Sequence: IVEKSKICSSRYEPTVRIGGRNGMCVDVYDDGYHNGNRIIAWKCKDRLEENQLWTLKSDKTIRSNGKCLTTEGYAPGNYVMIYDCTSAVAEATYWEIWDNGTIINPKSALVLSAESSSMGGTLTVQTNEYLMRQGWRTGNNTSPFVTSISGYSDLCMQAQGSNVWLAYCDNNKKEQQWALYTDGSIRSVQNTNNCLTSKDHKQGSPIVLMACSNGWASQRWLFRNDGSIYNLHDDMVMDVKRSDPSLKEIILHPYHGKPNQIWLTLF | ||||||
Disulfide bond | 285↔304 | |||||
Sequence: CVDVYDDGYHNGNRIIAWKC | ||||||
Disulfide bond | 328↔345 | |||||
Sequence: CLTTEGYAPGNYVMIYDC | ||||||
Glycosylation | 360 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 400 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 416↔429 | |||||
Sequence: CMQAQGSNVWLAYC | ||||||
Disulfide bond | 455↔472 | |||||
Sequence: CLTSKDHKQGSPIVLMAC |
Keywords
- PTM
Interaction
Subunit
Disulfide-linked dimer of A and B chains.
Structure
Family & Domains
Features
Showing features for domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 272-399 | Ricin B-type lectin 1 | ||||
Sequence: YEPTVRIGGRNGMCVDVYDDGYHNGNRIIAWKCKDRLEENQLWTLKSDKTIRSNGKCLTTEGYAPGNYVMIYDCTSAVAEATYWEIWDNGTIINPKSALVLSAESSSMGGTLTVQTNEYLMRQGWRTG | ||||||
Repeat | 282-324 | 1-alpha | ||||
Sequence: NGMCVDVYDDGYHNGNRIIAWKCKDRLEENQLWTLKSDKTIRS | ||||||
Repeat | 325-365 | 1-beta | ||||
Sequence: NGKCLTTEGYAPGNYVMIYDCTSAVAEATYWEIWDNGTIIN | ||||||
Repeat | 368-400 | 1-gamma | ||||
Sequence: SALVLSAESSSMGGTLTVQTNEYLMRQGWRTGN | ||||||
Domain | 402-526 | Ricin B-type lectin 2 | ||||
Sequence: TSPFVTSISGYSDLCMQAQGSNVWLAYCDNNKKEQQWALYTDGSIRSVQNTNNCLTSKDHKQGSPIVLMACSNGWASQRWLFRNDGSIYNLHDDMVMDVKRSDPSLKEIILHPYHGKPNQIWLTL | ||||||
Repeat | 413-448 | 2-alpha | ||||
Sequence: SDLCMQAQGSNVWLAYCDNNKKEQQWALYTDGSIRS | ||||||
Repeat | 452-491 | 2-beta | ||||
Sequence: TNNCLTSKDHKQGSPIVLMACSNGWASQRWLFRNDGSIYN | ||||||
Repeat | 494-527 | 2-gamma | ||||
Sequence: DDMVMDVKRSDPSLKEIILHPYHGKPNQIWLTLF |
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
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length527
- Mass (Da)59,115
- Last updated1996-11-01 v1
- Checksum3253AE490CE9494A
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 282 | in Ref. 2; AA sequence | ||||
Sequence: N → D | ||||||
Sequence conflict | 291 | in Ref. 2; AA sequence | ||||
Sequence: D → N | ||||||
Sequence conflict | 350-351 | in Ref. 2; AA sequence | ||||
Sequence: AE → PQ | ||||||
Sequence conflict | 378 | in Ref. 2; AA sequence | ||||
Sequence: S → N | ||||||
Sequence conflict | 426 | in Ref. 2; AA sequence | ||||
Sequence: L → M | ||||||
Sequence conflict | 428 | in Ref. 2; AA sequence | ||||
Sequence: Y → D | ||||||
Sequence conflict | 431 | in Ref. 2; AA sequence | ||||
Sequence: N → S | ||||||
Sequence conflict | 484 | in Ref. 2; AA sequence | ||||
Sequence: R → K | ||||||
Sequence conflict | 491 | in Ref. 2; AA sequence | ||||
Sequence: N → S | ||||||
Sequence conflict | 493 | in Ref. 2; AA sequence | ||||
Sequence: H → Y | ||||||
Sequence conflict | 502 | in Ref. 2; AA sequence | ||||
Sequence: R → G | ||||||
Sequence conflict | 509 | in Ref. 2; AA sequence | ||||
Sequence: E → Q | ||||||
Sequence conflict | 513 | in Ref. 2; AA sequence | ||||
Sequence: H → W | ||||||
Sequence conflict | 516 | in Ref. 2; AA sequence | ||||
Sequence: H → T |
Keywords
- Technical term