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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)DescriptionActionsGraphical viewLength
Binding sitei74Carbohydrate; via amide nitrogenBy similarity1
Active sitei200By similarity1
Binding sitei312Carbohydrate; via carbonyl oxygen1
Binding sitei337Carbohydrate1
Binding sitei342Carbohydrate1
Binding sitei348Carbohydrate1
Binding sitei381Carbohydrate1
Binding sitei397Carbohydrate1
Binding sitei437Carbohydrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi104 – 105AMPBy similarity2
Nucleotide bindingi145 – 147AMPBy similarity3

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000003072625 – 290Agglutinin A chainAdd BLAST266
PropeptideiPRO_0000030727291 – 302Linker peptide2 PublicationsAdd BLAST12
ChainiPRO_0000030728303 – 564Agglutinin B chain1 PublicationAdd BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi34N-linked (GlcNAc...)Sequence analysis1
Glycosylationi259N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi282 ↔ 306Interchain (between A and B chains)PROSITE-ProRule annotation1 Publication
Disulfide bondi322 ↔ 341PROSITE-ProRule annotation1 Publication
Disulfide bondi365 ↔ 382PROSITE-ProRule annotation1 Publication
Glycosylationi397N-linked (GlcNAc...)1
Glycosylationi437N-linked (GlcNAc...)1
Disulfide bondi453 ↔ 466PROSITE-ProRule annotation1 Publication
Disulfide bondi492 ↔ 509PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP06750.

Structurei

Secondary structure

1564
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 36Combined sources5
Helixi42 – 56Combined sources15
Beta strandi66 – 68Combined sources3
Helixi77 – 79Combined sources3
Beta strandi80 – 87Combined sources8
Beta strandi93 – 99Combined sources7
Turni100 – 102Combined sources3
Beta strandi105 – 109Combined sources5
Beta strandi111 – 116Combined sources6
Helixi122 – 127Combined sources6
Helixi128 – 130Combined sources3
Beta strandi137 – 143Combined sources7
Helixi147 – 154Combined sources8
Helixi157 – 159Combined sources3
Helixi164 – 176Combined sources13
Helixi177 – 179Combined sources3
Helixi184 – 203Combined sources20
Helixi205 – 217Combined sources13
Helixi225 – 242Combined sources18
Beta strandi245 – 256Combined sources12
Beta strandi262 – 268Combined sources7
Helixi269 – 271Combined sources3
Turni272 – 274Combined sources3
Helixi318 – 320Combined sources3
Beta strandi321 – 325Combined sources5
Helixi326 – 328Combined sources3
Beta strandi335 – 340Combined sources6
Helixi347 – 349Combined sources3
Beta strandi364 – 369Combined sources6
Beta strandi376 – 381Combined sources6
Turni382 – 384Combined sources3
Helixi387 – 389Combined sources3
Beta strandi398 – 402Combined sources5
Turni403 – 406Combined sources4
Beta strandi407 – 410Combined sources4
Beta strandi421 – 424Combined sources4
Helixi429 – 431Combined sources3
Beta strandi442 – 447Combined sources6
Helixi449 – 451Combined sources3
Beta strandi452 – 457Combined sources6
Beta strandi460 – 465Combined sources6
Helixi471 – 473Combined sources3
Beta strandi475 – 477Combined sources3
Beta strandi481 – 485Combined sources5
Beta strandi491 – 494Combined sources4
Beta strandi505 – 509Combined sources5
Turni529 – 531Combined sources3
Beta strandi534 – 537Combined sources4
Helixi538 – 540Combined sources3
Beta strandi547 – 550Combined sources4
Helixi556 – 558Combined sources3
Beta strandi561 – 563Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP06750.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini309 – 436Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST128
Repeati319 – 3611-alphaAdd BLAST43
Repeati362 – 4021-betaAdd BLAST41
Repeati405 – 4371-gammaAdd BLAST33
Domaini439 – 563Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST125
Repeati450 – 4852-alphaAdd BLAST36
Repeati489 – 5282-betaAdd BLAST40
Repeati531 – 5582-gammaAdd BLAST28

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 34Carbohydrate binding3
Regioni164 – 169Carbohydrate bindingBy similarity6
Regioni218 – 220Carbohydrate bindingBy similarity3
Regioni324 – 328Carbohydrate binding5
Regioni536 – 539Carbohydrate bindingBy similarity4
Regioni553 – 557Carbohydrate bindingBy similarity5

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)DescriptionActionsGraphical viewLength
Sequence conflicti331F → T AA sequence (Ref. 2) Curated1
Sequence conflicti362N → D AA sequence (Ref. 2) Curated1
Sequence conflicti374R → G AA sequence (Ref. 2) Curated1
Sequence conflicti404R → T AA sequence (Ref. 2) Curated1
Sequence conflicti552F → V AA sequence (Ref. 2) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RZOX-ray2.63A/C25-286[»]
B/D303-564[»]
ProteinModelPortaliP06750.
SMRiP06750.
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: November 2, 2016
This is version 118 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.