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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)DescriptionActionsGraphical viewLength
Active sitei183By similarity1

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)DescriptionActionsGraphical viewLength
Mutagenesisi219P → N: 7-fold more potent in protein synthesis inhibition in vitro. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000024848921 – 278Agglutinin-1 chain AAdd BLAST258
PropeptideiPRO_0000248490279 – 280Linker peptide1 Publication2
ChainiPRO_0000248491281 – 547Agglutinin-1 chain BAdd BLAST267

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21Pyrrolidone carboxylic acidBy similarity1
Disulfide bondi266 ↔ 288Interchain (between A and B chains)PROSITE-ProRule annotationBy similarity
Disulfide bondi305 ↔ 324PROSITE-ProRule annotationBy similarity
Disulfide bondi348 ↔ 365PROSITE-ProRule annotationBy similarity
Glycosylationi380N-linked (GlcNAc...)Sequence analysis1
Glycosylationi420N-linked (GlcNAc...)Sequence analysis1
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

1547
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 27Combined sources3
Helixi28 – 30Combined sources3
Helixi33 – 47Combined sources15
Beta strandi48 – 52Combined sources5
Beta strandi55 – 58Combined sources4
Helixi61 – 63Combined sources3
Helixi66 – 68Combined sources3
Beta strandi69 – 78Combined sources10
Beta strandi81 – 88Combined sources8
Turni89 – 91Combined sources3
Beta strandi94 – 99Combined sources6
Beta strandi102 – 105Combined sources4
Helixi111 – 116Combined sources6
Beta strandi121 – 125Combined sources5
Helixi132 – 139Combined sources8
Helixi143 – 145Combined sources3
Helixi150 – 161Combined sources12
Helixi167 – 186Combined sources20
Helixi188 – 200Combined sources13
Helixi208 – 226Combined sources19
Beta strandi228 – 230Combined sources3
Beta strandi231 – 239Combined sources9
Beta strandi245 – 250Combined sources6
Helixi254 – 258Combined sources5
Helixi301 – 303Combined sources3
Beta strandi305 – 308Combined sources4
Helixi309 – 311Combined sources3
Beta strandi318 – 322Combined sources5
Helixi330 – 332Combined sources3
Beta strandi334 – 336Combined sources3
Beta strandi342 – 344Combined sources3
Beta strandi347 – 352Combined sources6
Beta strandi359 – 363Combined sources5
Turni365 – 367Combined sources3
Helixi370 – 373Combined sources4
Beta strandi383 – 385Combined sources3
Turni386 – 389Combined sources4
Beta strandi390 – 393Combined sources4
Beta strandi404 – 406Combined sources3
Helixi412 – 414Combined sources3
Beta strandi417 – 420Combined sources4
Beta strandi425 – 430Combined sources6
Beta strandi435 – 440Combined sources6
Beta strandi443 – 448Combined sources6
Helixi454 – 456Combined sources3
Beta strandi458 – 460Combined sources3
Beta strandi466 – 468Combined sources3
Beta strandi474 – 482Combined sources9
Beta strandi486 – 491Combined sources6
Helixi492 – 494Combined sources3
Helixi497 – 499Combined sources3
Beta strandi509 – 511Combined sources3
Turni512 – 515Combined sources4
Beta strandi516 – 520Combined sources5
Helixi521 – 523Combined sources3
Helixi525 – 527Combined sources3
Beta strandi530 – 533Combined sources4
Helixi539 – 541Combined sources3
Beta strandi544 – 546Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9M6E9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini292 – 419Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST128
Repeati302 – 3441-alphaSequence analysisAdd BLAST43
Repeati345 – 3851-betaSequence analysisAdd BLAST41
Repeati388 – 4201-gammaSequence analysisAdd BLAST33
Domaini422 – 546Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST125
Repeati433 – 4682-alphaSequence analysisAdd BLAST36
Repeati472 – 5112-betaSequence analysisAdd BLAST40
Repeati514 – 5472-gammaSequence analysisAdd BLAST34

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Q3NX-ray3.50A21-280[»]
B281-547[»]
2ZR1X-ray2.60A/C21-278[»]
B/D281-547[»]
ProteinModelPortaliQ9M6E9.
SMRiQ9M6E9.
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: November 2, 2016
This is version 77 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.