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Protein

Agglutinin-1

Gene

AAG

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 (By similarity). Less toxic than abrin-a.By similarity1 Publication
The B chain is a galactose-specific lectin that facilitates the binding to the cell membrane that precedes endocytosis.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei183 – 1831By similarity

GO - Molecular functioni

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

GO - Biological processi

  • defense response Source: UniProtKB-KW
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • negative regulation of translation Source: UniProtKB
  • positive regulation of apoptotic process in other organism Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein synthesis inhibitor, Toxin

Keywords - Biological processi

Plant defense

Keywords - Ligandi

Lectin

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Agglutinin-1
Alternative name(s):
Agglutinin I
Cleaved into the following 2 chains:
Alternative name(s):
AAG-A
Alternative name(s):
AAG-B
Gene namesi
Name:AAGImported
OrganismiAbrus precatorius (Indian licorice) (Glycine abrus)
Taxonomic identifieri3816 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeAbreaeAbrus

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi219 – 2191P → N: 7-fold more potent in protein synthesis inhibition in vitro. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 278258Agglutinin-1 chain APRO_0000248489Add
BLAST
Propeptidei279 – 2802Linker peptide1 PublicationPRO_0000248490
Chaini281 – 547267Agglutinin-1 chain BPRO_0000248491Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acidBy similarity
Disulfide bondi266 ↔ 288Interchain (between A and B chains)PROSITE-ProRule annotationBy similarity
Disulfide bondi305 ↔ 324PROSITE-ProRule annotationBy similarity
Disulfide bondi348 ↔ 365PROSITE-ProRule annotationBy similarity
Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence analysis
Glycosylationi420 – 4201N-linked (GlcNAc...)Sequence analysis
Disulfide bondi436 ↔ 449PROSITE-ProRule annotationBy similarity
Disulfide bondi475 ↔ 492PROSITE-ProRule annotationBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Heterotetramer of two A and two B chains.1 Publication

Structurei

Secondary structure

1
547
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 273Combined sources
Helixi28 – 303Combined sources
Helixi33 – 4715Combined sources
Beta strandi48 – 525Combined sources
Beta strandi55 – 584Combined sources
Helixi61 – 633Combined sources
Helixi66 – 683Combined sources
Beta strandi69 – 7810Combined sources
Beta strandi81 – 888Combined sources
Turni89 – 913Combined sources
Beta strandi94 – 996Combined sources
Beta strandi102 – 1054Combined sources
Helixi111 – 1166Combined sources
Beta strandi121 – 1255Combined sources
Helixi132 – 1398Combined sources
Helixi143 – 1453Combined sources
Helixi150 – 16112Combined sources
Helixi167 – 18620Combined sources
Helixi188 – 20013Combined sources
Helixi208 – 22619Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi231 – 2399Combined sources
Beta strandi245 – 2506Combined sources
Helixi254 – 2585Combined sources
Helixi301 – 3033Combined sources
Beta strandi305 – 3084Combined sources
Helixi309 – 3113Combined sources
Beta strandi318 – 3225Combined sources
Helixi330 – 3323Combined sources
Beta strandi334 – 3363Combined sources
Beta strandi342 – 3443Combined sources
Beta strandi347 – 3526Combined sources
Beta strandi359 – 3635Combined sources
Turni365 – 3673Combined sources
Helixi370 – 3734Combined sources
Beta strandi383 – 3853Combined sources
Turni386 – 3894Combined sources
Beta strandi390 – 3934Combined sources
Beta strandi404 – 4063Combined sources
Helixi412 – 4143Combined sources
Beta strandi417 – 4204Combined sources
Beta strandi425 – 4306Combined sources
Beta strandi435 – 4406Combined sources
Beta strandi443 – 4486Combined sources
Helixi454 – 4563Combined sources
Beta strandi458 – 4603Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi474 – 4829Combined sources
Beta strandi486 – 4916Combined sources
Helixi492 – 4943Combined sources
Helixi497 – 4993Combined sources
Beta strandi509 – 5113Combined sources
Turni512 – 5154Combined sources
Beta strandi516 – 5205Combined sources
Helixi521 – 5233Combined sources
Helixi525 – 5273Combined sources
Beta strandi530 – 5334Combined sources
Helixi539 – 5413Combined sources
Beta strandi544 – 5463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q3NX-ray3.50A21-280[»]
B281-547[»]
2ZR1X-ray2.60A/C21-278[»]
B/D281-547[»]
ProteinModelPortaliQ9M6E9.
SMRiQ9M6E9. Positions 22-268, 287-547.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9M6E9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini292 – 419128Ricin B-type lectin 1PROSITE-ProRule annotationAdd
BLAST
Repeati302 – 344431-alphaSequence analysisAdd
BLAST
Repeati345 – 385411-betaSequence analysisAdd
BLAST
Repeati388 – 420331-gammaSequence analysisAdd
BLAST
Domaini422 – 546125Ricin B-type lectin 2PROSITE-ProRule annotationAdd
BLAST
Repeati433 – 468362-alphaSequence analysisAdd
BLAST
Repeati472 – 511402-betaSequence analysisAdd
BLAST
Repeati514 – 547342-gammaSequence analysisAdd
BLAST

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

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.

Q9M6E9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFETTKNKL HGNAYYQAQF QDPIKFTTGS ATPASYNQFI DALRERLTGG
60 70 80 90 100
LIYGIPVLRD PSTVEKPNQY VTVELSYSDT VSIQLGIDLT NAYVVAYRAG
110 120 130 140 150
SESFFFRNAP ASASTYLFTG TQQYSLPFDG NYDDLEKWAH QSRQRISLGL
160 170 180 190 200
EALRQGIKFL RSGASDDEEI ARTLIVIIQM VAEAARFRYV SKLVVISLSN
210 220 230 240 250
RAAFQPDPSM LSLENTWEPL SRAVQHTVQD TFPQNVTLIN VRQERVVVSS
260 270 280 290 300
LSHPSVSALA LMLFVCNPLN ATQSPLLIRS VVEQSKICSS HYEPTVRIGG
310 320 330 340 350
RDGLCVDVSD NAYNNGNPII LWKCKDQLEV NQLWTLKSDK TIRSKGKCLT
360 370 380 390 400
TYGYAPGNYV MIYDCSSAVA EATYWDIWDN GTIINPKSGL VLSAESSSMG
410 420 430 440 450
GTLTVQKNDY RMRQGWRTGN DTSPFVTSIA GFFKLCMEAH GNSMWLDVCD
460 470 480 490 500
ITKEEQQWAV YPDGSIRPVQ NTNNCLTCEE HKQGATIVMM GCSNAWASQR
510 520 530 540
WVFKSDGTIY NLYDDMVMDV KSSDPSLKQI ILWPYTGNAN QMWATLF
Length:547
Mass (Da):61,248
Last modified:October 1, 2000 - v1
Checksum:i355A325C2354A1BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190173 mRNA. Translation: AAF28309.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190173 mRNA. Translation: AAF28309.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q3NX-ray3.50A21-280[»]
B281-547[»]
2ZR1X-ray2.60A/C21-278[»]
B/D281-547[»]
ProteinModelPortaliQ9M6E9.
SMRiQ9M6E9. Positions 22-268, 287-547.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9M6E9.

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 nameiAGGL_ABRPR
AccessioniPrimary (citable) accession number: Q9M6E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2000
Last modified: October 14, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Induces cytokine production and proliferation of splenocytes and thymocytes in mice.1 Publication

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.