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Protein

Ribosome-inactivating protein SNAI'

Gene
N/A
Organism
Sambucus nigra (European elder)
Status
Reviewed-Annotation score: Annotation score: 4 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. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Agglutination is inhibited by Neu5Ac(alpha2,6)lactose, and N-linked glycoproteins such as fetuin and orosomucoid.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei201 – 2011By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Protein synthesis inhibitor, Toxin

Keywords - Biological processi

Plant defense

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome-inactivating protein SNAI'
Cleaved into the following 3 chains:
Alternative name(s):
rRNA N-glycosidase
OrganismiSambucus nigra (European elder)
Taxonomic identifieri4202 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsDipsacalesAdoxaceaeSambucus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 291263SNAI' A chainPRO_0000030746Add
BLAST
Peptidei292 – 30312Linker peptide1 PublicationPRO_0000030747Add
BLAST
Chaini304 – 569266SNAI' B chainPRO_0000030748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence analysis
Disulfide bondi286 ↔ 311Interchain (between A and B chains)PROSITE-ProRule annotation
Disulfide bondi328 ↔ 347PROSITE-ProRule annotation
Disulfide bondi369 ↔ 381PROSITE-ProRule annotation
Disulfide bondi451 ↔ 466PROSITE-ProRule annotation
Disulfide bondi495 ↔ 512PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Disulfide-linked dimer of A and B chains.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP93543.
SMRiP93543. Positions 309-565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini315 – 435121Ricin B-type lectin 1PROSITE-ProRule annotationAdd
BLAST
Repeati325 – 365411-alphaAdd
BLAST
Repeati366 – 401361-betaAdd
BLAST
Repeati404 – 436331-gammaAdd
BLAST
Domaini437 – 565129Ricin B-type lectin 2PROSITE-ProRule annotationAdd
BLAST
Repeati448 – 488412-alphaAdd
BLAST
Repeati492 – 530392-betaAdd
BLAST
Repeati533 – 566342-gammaAdd
BLAST

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, 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.

P93543-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVVATILYL VVLAICGLGI HGAHPTHSAP PTVYPSVSFN LTEANSNEYR
60 70 80 90 100
HFLQELRGKV ILGSHRAFDL PVLNPESKVS DSDRFVLVRL TNPSRKKVTL
110 120 130 140 150
AIDVVTFYVV AFAQNDRSYF FSGSSEVQRE NLFVDTTQED LNFKGDYTSL
160 170 180 190 200
EHQVGFGRVY IPLGPKSLAQ SISSLSTYKS SAGDNKRLAR SLLVVIQMVS
210 220 230 240 250
EAARFRYIQL RIQASITDAK EFTPDLLMLS MENKWSSMSS EIQQAQPGGA
260 270 280 290 300
FAQVVKLLDQ RNHPIDVTNF RRLFQLTSVA VLLHGCPTVT KMPAYIIKMP
310 320 330 340 350
VFNGGEDEER CSVVEEVTRR IGGRDGFCAE VKNGDEKDGT PVQLSSCGEQ
360 370 380 390 400
SNQQWTFSTD GTIQSLGKCL TTSSSVMIYN CKVVPPESTK WVVSIDGTIT
410 420 430 440 450
NPRSGLVLTA PKAAEGTLVS LEKNVHAARQ GWIVGNVEPL VTFIVGYEQM
460 470 480 490 500
CLETNPGNND VSLGDCSVKS ASKVDQKWAL YGDGTIRVNN DRSLCVTSEG
510 520 530 540 550
KSSNEPIIIL KCLGWANQRW VFNTDGTISN PDSKLVMHVD QNDVPLRKII
560
LSHPSGTSNQ QWIASTHPA
Length:569
Mass (Da):62,598
Last modified:May 1, 1997 - v1
Checksum:i82B9C889A3E1F9AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66191 mRNA. Translation: AAC49754.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66191 mRNA. Translation: AAC49754.1.

3D structure databases

ProteinModelPortaliP93543.
SMRiP93543. Positions 309-565.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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...

Publicationsi

  1. "Elderberry (Sambucus nigra) bark contains two structurally different Neu5Ac(alpha2,6)Gal/GalNAc-binding type 2 ribosome-inactivating proteins."
    van Damme E.J.M., Roy S., Barre A., Citores L., Mostafapous K., Rouge P., Van Leuven F., Girbes T., Goldstein I.J., Peumans W.J.
    Eur. J. Biochem. 245:648-655(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-38 AND 304-309, FUNCTION, SUBUNIT.
    Tissue: Bark.

Entry informationi

Entry nameiRIP1_SAMNI
AccessioniPrimary (citable) accession number: P93543
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 1, 1997
Last modified: July 6, 2016
This is version 70 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

Direct protein sequencing

Documents

  1. 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.