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Protein

Agglutinin

Gene
N/A
Organism
Ricinus communis (Castor bean)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741Carbohydrate; via amide nitrogenBy similarity
Active sitei200 – 2001By similarity
Binding sitei312 – 3121Carbohydrate; via carbonyl oxygen
Binding sitei337 – 3371Carbohydrate
Binding sitei342 – 3421Carbohydrate
Binding sitei348 – 3481Carbohydrate
Binding sitei381 – 3811Carbohydrate
Binding sitei397 – 3971Carbohydrate
Binding sitei437 – 4371Carbohydrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi104 – 1052AMPBy similarity
Nucleotide bindingi145 – 1473AMPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein synthesis inhibitor, Toxin

Keywords - Biological processi

Plant defense

Keywords - Ligandi

Lectin, Nucleotide-binding

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Agglutinin
Alternative name(s):
RCA
Cleaved into the following 2 chains:
Alternative name(s):
rRNA N-glycosidase
OrganismiRicinus communis (Castor bean)
Taxonomic identifieri3988 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 290266Agglutinin A chainPRO_0000030726Add
BLAST
Propeptidei291 – 30212Linker peptide2 PublicationsPRO_0000030727Add
BLAST
Chaini303 – 564262Agglutinin B chain1 PublicationPRO_0000030728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...)Sequence analysis
Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence analysis
Disulfide bondi282 ↔ 306Interchain (between A and B chains)PROSITE-ProRule annotation1 Publication
Disulfide bondi322 ↔ 341PROSITE-ProRule annotation1 Publication
Disulfide bondi365 ↔ 382PROSITE-ProRule annotation1 Publication
Glycosylationi397 – 3971N-linked (GlcNAc...)
Glycosylationi437 – 4371N-linked (GlcNAc...)
Disulfide bondi453 ↔ 466PROSITE-ProRule annotation1 Publication
Disulfide bondi492 ↔ 509PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP06750.

Structurei

Secondary structure

1
564
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 365Combined sources
Helixi42 – 5615Combined sources
Beta strandi66 – 683Combined sources
Helixi77 – 793Combined sources
Beta strandi80 – 878Combined sources
Beta strandi93 – 997Combined sources
Turni100 – 1023Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi111 – 1166Combined sources
Helixi122 – 1276Combined sources
Helixi128 – 1303Combined sources
Beta strandi137 – 1437Combined sources
Helixi147 – 1548Combined sources
Helixi157 – 1593Combined sources
Helixi164 – 17613Combined sources
Helixi177 – 1793Combined sources
Helixi184 – 20320Combined sources
Helixi205 – 21713Combined sources
Helixi225 – 24218Combined sources
Beta strandi245 – 25612Combined sources
Beta strandi262 – 2687Combined sources
Helixi269 – 2713Combined sources
Turni272 – 2743Combined sources
Helixi318 – 3203Combined sources
Beta strandi321 – 3255Combined sources
Helixi326 – 3283Combined sources
Beta strandi335 – 3406Combined sources
Helixi347 – 3493Combined sources
Beta strandi364 – 3696Combined sources
Beta strandi376 – 3816Combined sources
Turni382 – 3843Combined sources
Helixi387 – 3893Combined sources
Beta strandi398 – 4025Combined sources
Turni403 – 4064Combined sources
Beta strandi407 – 4104Combined sources
Beta strandi421 – 4244Combined sources
Helixi429 – 4313Combined sources
Beta strandi442 – 4476Combined sources
Helixi449 – 4513Combined sources
Beta strandi452 – 4576Combined sources
Beta strandi460 – 4656Combined sources
Helixi471 – 4733Combined sources
Beta strandi475 – 4773Combined sources
Beta strandi481 – 4855Combined sources
Beta strandi491 – 4944Combined sources
Beta strandi505 – 5095Combined sources
Turni529 – 5313Combined sources
Beta strandi534 – 5374Combined sources
Helixi538 – 5403Combined sources
Beta strandi547 – 5504Combined sources
Helixi556 – 5583Combined sources
Beta strandi561 – 5633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZOX-ray2.63A/C25-286[»]
B/D303-564[»]
ProteinModelPortaliP06750.
SMRiP06750. Positions 27-286, 303-564.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06750.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini309 – 436128Ricin B-type lectin 1PROSITE-ProRule annotationAdd
BLAST
Repeati319 – 361431-alphaAdd
BLAST
Repeati362 – 402411-betaAdd
BLAST
Repeati405 – 437331-gammaAdd
BLAST
Domaini439 – 563125Ricin B-type lectin 2PROSITE-ProRule annotationAdd
BLAST
Repeati450 – 485362-alphaAdd
BLAST
Repeati489 – 528402-betaAdd
BLAST
Repeati531 – 558282-gammaAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 343Carbohydrate binding
Regioni164 – 1696Carbohydrate bindingBy similarity
Regioni218 – 2203Carbohydrate bindingBy similarity
Regioni324 – 3285Carbohydrate binding
Regioni536 – 5394Carbohydrate bindingBy similarity
Regioni553 – 5575Carbohydrate bindingBy similarity

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, 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.

P06750-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYAVATWLCF GSTSGWSFTL EDNNIFPKQY PIINFTTADA TVESYTNFIR
60 70 80 90 100
AVRSHLTTGA DVRHEIPVLP NRVGLPISQR FILVELSNHA ELSVTLALDV
110 120 130 140 150
TNAYVVGCRA GNSAYFFHPD NQEDAEAITH LFTDVQNSFT FAFGGNYDRL
160 170 180 190 200
EQLGGLRENI ELGTGPLEDA ISALYYYSTC GTQIPTLARS FMVCIQMISE
210 220 230 240 250
AARFQYIEGE MRTRIRYNRR SAPDPSVITL ENSWGRLSTA IQESNQGAFA
260 270 280 290 300
SPIQLQRRNG SKFNVYDVSI LIPIIALMVY RCAPPPSSQF SLLIRPVVPN
310 320 330 340 350
FNADVCMDPE PIVRIVGRNG LCVDVTGEEF FDGNPIQLWP CKSNTDWNQL
360 370 380 390 400
WTLRKDSTIR SNGKCLTISK SSPRQQVVIY NCSTATVGAT RWQIWDNRTI
410 420 430 440 450
INPRSGLVLA ATSGNSGTKL TVQTNIYAVS QGWLPTNNTQ PFVTTIVGLY
460 470 480 490 500
GMCLQANSGK VWLEDCTSEK AEQQWALYAD GSIRPQQNRD NCLTTDANIK
510 520 530 540 550
GTVVKILSCG PASSGQRWMF KNDGTILNLY NGLVLDVRRS DPSLKQIIVH
560
PFHGNLNQIW LPLF
Length:564
Mass (Da):62,851
Last modified:January 1, 1988 - v1
Checksum:iD455F2A72F609759
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti331 – 3311F → T AA sequence (Ref. 2) Curated
Sequence conflicti362 – 3621N → D AA sequence (Ref. 2) Curated
Sequence conflicti374 – 3741R → G AA sequence (Ref. 2) Curated
Sequence conflicti404 – 4041R → T AA sequence (Ref. 2) Curated
Sequence conflicti552 – 5521F → V AA sequence (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12089 mRNA. Translation: AAA33869.1.
S40368 mRNA. Translation: AAB22584.1.
PIRiA24261. RLCSAG.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

RCA

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12089 mRNA. Translation: AAA33869.1.
S40368 mRNA. Translation: AAB22584.1.
PIRiA24261. RLCSAG.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZOX-ray2.63A/C25-286[»]
B/D303-564[»]
ProteinModelPortaliP06750.
SMRiP06750. Positions 27-286, 303-564.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

PTM databases

UniCarbKBiP06750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP06750.

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_RICCO
AccessioniPrimary (citable) accession number: P06750
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: October 14, 2015
This is version 116 of the entry and version 1 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.