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P11140

- ABRA_ABRPR

UniProt

P11140 - ABRA_ABRPR

Protein

Abrin-a

Gene
N/A
Organism
Abrus precatorius (Indian licorice) (Glycine abrus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei164 – 1641By similarity

    GO - Molecular functioni

    1. galactose binding Source: UniProtKB
    2. rRNA N-glycosylase activity Source: UniProtKB

    GO - Biological processi

    1. defense response Source: UniProtKB-KW
    2. metabolic process Source: GOC
    3. negative regulation of translation Source: UniProtKB
    4. positive regulation of endocytosis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein synthesis inhibitor, Toxin

    Keywords - Biological processi

    Plant defense

    Keywords - Ligandi

    Lectin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Abrin-a
    Cleaved into the following 3 chains:
    Alternative name(s):
    rRNA N-glycosidase
    OrganismiAbrus precatorius (Indian licorice) (Glycine abrus)
    Taxonomic identifieri3816 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeAbreaeAbrus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi200 – 2001N → P: 46-fold less potent protein synthesis inhibition. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 251251Abrin-a A chainPRO_0000030729Add
    BLAST
    Peptidei252 – 26110Linker peptide1 PublicationPRO_0000030730
    Chaini262 – 528267Abrin-a B chainPRO_0000030731Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11Pyrrolidone carboxylic acid
    Disulfide bondi247 ↔ 269Interchain (between A and B chains)
    Disulfide bondi286 ↔ 305
    Disulfide bondi329 ↔ 346
    Glycosylationi361 – 3611N-linked (GlcNAc...)
    Glycosylationi401 – 4011N-linked (GlcNAc...)
    Disulfide bondi417 ↔ 430
    Disulfide bondi456 ↔ 473

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    PRIDEiP11140.

    Interactioni

    Subunit structurei

    Disulfide-linked dimer of A and B chains.

    Protein-protein interaction databases

    MINTiMINT-195443.

    Structurei

    Secondary structure

    1
    528
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Helixi14 – 2815
    Beta strandi36 – 383
    Helixi47 – 493
    Beta strandi50 – 6920
    Turni70 – 723
    Beta strandi75 – 795
    Beta strandi81 – 866
    Helixi94 – 974
    Beta strandi102 – 1065
    Helixi115 – 1195
    Beta strandi120 – 1223
    Turni124 – 1263
    Helixi131 – 14212
    Helixi148 – 16720
    Helixi169 – 18012
    Helixi189 – 1968
    Helixi198 – 20710
    Beta strandi209 – 22012
    Beta strandi226 – 2316
    Helixi235 – 2395
    Helixi282 – 2843
    Beta strandi286 – 2894
    Helixi290 – 2923
    Beta strandi299 – 3035
    Helixi311 – 3133
    Beta strandi315 – 3173
    Beta strandi321 – 3255
    Beta strandi328 – 3336
    Beta strandi340 – 3445
    Turni346 – 3483
    Helixi351 – 3533
    Beta strandi364 – 3663
    Turni367 – 3704
    Beta strandi371 – 3744
    Beta strandi385 – 3873
    Helixi393 – 3953
    Beta strandi398 – 4014
    Beta strandi406 – 4083
    Helixi413 – 4153
    Beta strandi417 – 4215
    Beta strandi424 – 4285
    Helixi435 – 4373
    Beta strandi439 – 4413
    Beta strandi447 – 4493
    Beta strandi452 – 46312
    Beta strandi467 – 4737
    Helixi478 – 4803
    Beta strandi490 – 4923
    Turni493 – 4964
    Beta strandi497 – 5015
    Helixi502 – 5043
    Helixi506 – 5083
    Beta strandi511 – 5144
    Helixi520 – 5223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ABRX-ray2.14A2-251[»]
    B262-528[»]
    ProteinModelPortaliP11140.
    SMRiP11140. Positions 1-251, 262-528.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11140.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini273 – 400128Ricin B-type lectin 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati283 – 325431-alphaAdd
    BLAST
    Repeati326 – 366411-betaAdd
    BLAST
    Repeati369 – 401331-gammaAdd
    BLAST
    Domaini403 – 527125Ricin B-type lectin 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati414 – 449362-alphaAdd
    BLAST
    Repeati453 – 492402-betaAdd
    BLAST
    Repeati495 – 528342-gammaAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    In the N-terminal section; belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.Curated
    Contains 2 ricin B-type lectin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di3.40.420.10. 1 hit.
    4.10.470.10. 1 hit.
    InterProiIPR001574. 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]
    PfamiPF00652. Ricin_B_lectin. 2 hits.
    PF00161. RIP. 1 hit.
    [Graphical view]
    PRINTSiPR00396. SHIGARICIN.
    SMARTiSM00458. RICIN. 2 hits.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 2 hits.
    SSF56371. SSF56371. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 2 hits.
    PS00275. SHIGA_RICIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11140-1 [UniParc]FASTAAdd to Basket

    « Hide

    QDRPIKFSTE GATSQSYKQF IEALRERLRG GLIHDIPVLP DPTTLQERNR    50
    YITVELSNSD TESIEVGIDV TNAYVVAYRA GTQSYFLRDA PSSASDYLFT 100
    GTDQHSLPFY GTYGDLERWA HQSRQQIPLG LQALTHGISF FRSGGNDNEE 150
    KARTLIVIIQ MVAEAARFRY ISNRVRVSIQ TGTAFQPDAA MISLENNWDN 200
    LSRGVQESVQ DTFPNQVTLT NIRNEPVIVD SLSHPTVAVL ALMLFVCNPP 250
    NANQSPLLIR SIVEKSKICS SRYEPTVRIG GRDGMCVDVY DNGYHNGNRI 300
    IMWKCKDRLE ENQLWTLKSD KTIRSNGKCL TTYGYAPGSY VMIYDCTSAV 350
    AEATYWEIWD NGTIINPKSA LVLSAESSSM GGTLTVQTNE YLMRQGWRTG 400
    NNTSPFVTSI SGYSDLCMQA QGSNVWMADC DSNKKEQQWA LYTDGSIRSV 450
    QNTNNCLTSK DHKQGSTILL MGCSNGWASQ RWVFKNDGSI YSLYDDMVMD 500
    VKGSDPSLKQ IILWPYTGKP NQIWLTLF 528
    Length:528
    Mass (Da):59,244
    Last modified:June 1, 1994 - v2
    Checksum:iA1F76BECD5B9A827
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11Q → E in AAA32624. (PubMed:8421313)Curated
    Sequence conflicti202 – 2021Missing AA sequence 1 PublicationCurated
    Sequence conflicti298 – 2981N → Y AA sequence (PubMed:1505674)Curated
    Sequence conflicti427 – 4271M → L AA sequence (PubMed:1505674)Curated
    Sequence conflicti467 – 4671T → P AA sequence (PubMed:1505674)Curated
    Sequence conflicti483 – 4831V → L AA sequence (PubMed:1505674)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M98344 mRNA. Translation: AAA32624.1.
    X54872 Genomic DNA. No translation available.
    PIRiS32429. TZLSA.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M98344 mRNA. Translation: AAA32624.1 .
    X54872 Genomic DNA. No translation available.
    PIRi S32429. TZLSA.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ABR X-ray 2.14 A 2-251 [» ]
    B 262-528 [» ]
    ProteinModelPortali P11140.
    SMRi P11140. Positions 1-251, 262-528.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-195443.

    Proteomic databases

    PRIDEi P11140.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P11140.

    Family and domain databases

    Gene3Di 3.40.420.10. 1 hit.
    4.10.470.10. 1 hit.
    InterProi IPR001574. 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 ]
    Pfami PF00652. Ricin_B_lectin. 2 hits.
    PF00161. RIP. 1 hit.
    [Graphical view ]
    PRINTSi PR00396. SHIGARICIN.
    SMARTi SM00458. RICIN. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 2 hits.
    SSF56371. SSF56371. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 2 hits.
    PS00275. SHIGA_RICIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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)

    Entry informationi

    Entry nameiABRA_ABRPR
    AccessioniPrimary (citable) accession number: P11140
    Secondary accession number(s): P28589
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3