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P11140

- ABRA_ABRPR

UniProt

P11140 - ABRA_ABRPR

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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

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
Complete GO annotation...

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
QDRPIKFSTE GATSQSYKQF IEALRERLRG GLIHDIPVLP DPTTLQERNR
60 70 80 90 100
YITVELSNSD TESIEVGIDV TNAYVVAYRA GTQSYFLRDA PSSASDYLFT
110 120 130 140 150
GTDQHSLPFY GTYGDLERWA HQSRQQIPLG LQALTHGISF FRSGGNDNEE
160 170 180 190 200
KARTLIVIIQ MVAEAARFRY ISNRVRVSIQ TGTAFQPDAA MISLENNWDN
210 220 230 240 250
LSRGVQESVQ DTFPNQVTLT NIRNEPVIVD SLSHPTVAVL ALMLFVCNPP
260 270 280 290 300
NANQSPLLIR SIVEKSKICS SRYEPTVRIG GRDGMCVDVY DNGYHNGNRI
310 320 330 340 350
IMWKCKDRLE ENQLWTLKSD KTIRSNGKCL TTYGYAPGSY VMIYDCTSAV
360 370 380 390 400
AEATYWEIWD NGTIINPKSA LVLSAESSSM GGTLTVQTNE YLMRQGWRTG
410 420 430 440 450
NNTSPFVTSI SGYSDLCMQA QGSNVWMADC DSNKKEQQWA LYTDGSIRSV
460 470 480 490 500
QNTNNCLTSK DHKQGSTILL MGCSNGWASQ RWVFKNDGSI YSLYDDMVMD
510 520
VKGSDPSLKQ IILWPYTGKP NQIWLTLF
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