Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Abrin-a

Gene
N/A
Organism
Abrus precatorius (Indian licorice) (Glycine abrus)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei164By similarity1

GO - Molecular functioni

  • galactose binding Source: UniProtKB
  • rRNA N-glycosylase activity Source: UniProtKB

GO - Biological processi

  • defense response Source: UniProtKB-KW
  • negative regulation of translation Source: UniProtKB
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi200N → P: 46-fold less potent protein synthesis inhibition. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000307291 – 251Abrin-a A chainAdd BLAST251
PeptideiPRO_0000030730252 – 261Linker peptide1 Publication10
ChainiPRO_0000030731262 – 528Abrin-a B chainAdd BLAST267

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid1
Disulfide bondi247 ↔ 269Interchain (between A and B chains)
Disulfide bondi286 ↔ 305
Disulfide bondi329 ↔ 346
Glycosylationi361N-linked (GlcNAc...)1
Glycosylationi401N-linked (GlcNAc...)1
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

1528
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi14 – 28Combined sources15
Beta strandi36 – 38Combined sources3
Helixi47 – 49Combined sources3
Beta strandi50 – 69Combined sources20
Turni70 – 72Combined sources3
Beta strandi75 – 79Combined sources5
Beta strandi81 – 86Combined sources6
Helixi94 – 97Combined sources4
Beta strandi102 – 106Combined sources5
Helixi115 – 119Combined sources5
Beta strandi120 – 122Combined sources3
Turni124 – 126Combined sources3
Helixi131 – 142Combined sources12
Helixi148 – 167Combined sources20
Helixi169 – 180Combined sources12
Helixi189 – 196Combined sources8
Helixi198 – 207Combined sources10
Beta strandi209 – 220Combined sources12
Beta strandi226 – 231Combined sources6
Helixi235 – 239Combined sources5
Helixi282 – 284Combined sources3
Beta strandi286 – 289Combined sources4
Helixi290 – 292Combined sources3
Beta strandi299 – 303Combined sources5
Helixi311 – 313Combined sources3
Beta strandi315 – 317Combined sources3
Beta strandi321 – 325Combined sources5
Beta strandi328 – 333Combined sources6
Beta strandi340 – 344Combined sources5
Turni346 – 348Combined sources3
Helixi351 – 353Combined sources3
Beta strandi364 – 366Combined sources3
Turni367 – 370Combined sources4
Beta strandi371 – 374Combined sources4
Beta strandi385 – 387Combined sources3
Helixi393 – 395Combined sources3
Beta strandi398 – 401Combined sources4
Beta strandi406 – 408Combined sources3
Helixi413 – 415Combined sources3
Beta strandi417 – 421Combined sources5
Beta strandi424 – 428Combined sources5
Helixi435 – 437Combined sources3
Beta strandi439 – 441Combined sources3
Beta strandi447 – 449Combined sources3
Beta strandi452 – 463Combined sources12
Beta strandi467 – 473Combined sources7
Helixi478 – 480Combined sources3
Beta strandi490 – 492Combined sources3
Turni493 – 496Combined sources4
Beta strandi497 – 501Combined sources5
Helixi502 – 504Combined sources3
Helixi506 – 508Combined sources3
Beta strandi511 – 514Combined sources4
Helixi520 – 522Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ABRX-ray2.14A2-251[»]
B262-528[»]
ProteinModelPortaliP11140.
SMRiP11140.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11140.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini273 – 400Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST128
Repeati283 – 3251-alphaAdd BLAST43
Repeati326 – 3661-betaAdd BLAST41
Repeati369 – 4011-gammaAdd BLAST33
Domaini403 – 527Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST125
Repeati414 – 4492-alphaAdd BLAST36
Repeati453 – 4922-betaAdd BLAST40
Repeati495 – 5282-gammaAdd BLAST34

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

        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)DescriptionActionsGraphical viewLength
Sequence conflicti1Q → E in AAA32624 (PubMed:8421313).Curated1
Sequence conflicti202Missing AA sequence (Ref. 2) Curated1
Sequence conflicti298N → Y AA sequence (PubMed:1505674).Curated1
Sequence conflicti427M → L AA sequence (PubMed:1505674).Curated1
Sequence conflicti467T → P AA sequence (PubMed:1505674).Curated1
Sequence conflicti483V → L AA sequence (PubMed:1505674).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98344 mRNA. Translation: AAA32624.1.
X54872 Genomic DNA. No translation available.
PIRiS32429. TZLSA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98344 mRNA. Translation: AAA32624.1.
X54872 Genomic DNA. No translation available.
PIRiS32429. TZLSA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ABRX-ray2.14A2-251[»]
B262-528[»]
ProteinModelPortaliP11140.
SMRiP11140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-195443.

Proteomic databases

PRIDEiP11140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP11140.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 115 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.