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Protein

Ribosome-inactivating protein SNAI

Gene

SNA-I

Organism
Sambucus nigra (European elder)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Neu5Ac(alpha2-6)Gal/GalNAc specific agglutinin (PubMed:3805045). Behaves as a type-2 ribosome-inactivating protein (PubMed:8631319). Strongly inhibits mammalian but not plant ribosomes (PubMed:8631319). 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 (Probable). 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) (Probable). Involved in plant defense against insects (By similarity).By similarityCurated2 Publications
TrSNAI: Binds Neu5Ac(alpha2-6)Gal/GalNAc but has no clear agglutination activity.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei199By similarity1

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

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome-inactivating protein SNAI1 Publication
Alternative name(s):
Agglutinin I
Cleaved into the following 4 chains:
SNAI-A chain1 Publication (EC:3.2.2.22UniRule annotation)
Alternative name(s):
rRNA N-glycosidaseUniRule annotation
SNAI-B chain1 Publication
TrSNAI1 Publication
Gene namesi
Name:SNA-I1 Publication
Synonyms:LECSNAI1 Publication, SNAI1 Publication
OrganismiSambucus nigra (European elder)
Taxonomic identifieri4202 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsDipsacalesAdoxaceaeSambucus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 281 PublicationAdd BLAST28
ChainiPRO_000043797129 – 289SNAI-A chainCuratedAdd BLAST261
PeptideiPRO_0000437972290 – 308Linker peptideBy similarityAdd BLAST19
ChainiPRO_0000437973309 – 570SNAI-B chain1 PublicationAdd BLAST262
ChainiPRO_0000437974434 – 570TrSNAI1 PublicationAdd BLAST137

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...)1 Publication1
Glycosylationi62N-linked (GlcNAc...)1 Publication1
Glycosylationi144N-linked (GlcNAc...)1 Publication1
Glycosylationi260N-linked (GlcNAc...)1 Publication1
Disulfide bondi284 ↔ 316Interchain (between A and B chains)PROSITE-ProRule annotation
Disulfide bondi332 ↔ 351PROSITE-ProRule annotation
Disulfide bondi355Interchain (between two adjacent B chains)1 Publication
Disulfide bondi373 ↔ 385PROSITE-ProRule annotation
Disulfide bondi455 ↔ 470PROSITE-ProRule annotation
Glycosylationi492N-linked (GlcNAc...)1 Publication1
Disulfide bondi496 ↔ 513PROSITE-ProRule annotation
Glycosylationi526N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

The precursor is processed in two chains, A and B, that are linked by a disulfide bond (PubMed:9541002). A small truncated form corresponding roughly to the second ricin B-type lectin domain of the B chain, TrSNAI, can also be produced (PubMed:9541002).1 Publication
Glycosylated (PubMed:8631319, PubMed:27384337). N-glycans of subunit A are (Man)2-3(Xyl)(GlcNAc)2(Fuc) at Asn-40, (GlcNAc)0-2(Man)3(Xyl)(GlcNAc)2(Fuc) or (Man)1-2(GlcNAc)2 at Asn-62, (Man)3(Xyl)(GlcNAc)2(Fuc)0-1 at Asn-144 and (GlcNAc)0-1(Man)3(Xyl)(GlcNAc)2(Fuc) at Asn-260 (PubMed:27384337). N-glycans of subunit B are (Man)3(Xyl)(GlcNAc)2(Fuc) at Asn-492 and (Man)6-9(GlcNAc)2 at Asn-526 (PubMed:27384337).2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed in bark.1 Publication

Interactioni

Subunit structurei

Tetramer of four pairs of disulfide bound A-B chains.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ41358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini319 – 439Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST121
Repeati329 – 3691-alpha1 PublicationAdd BLAST41
Repeati370 – 4051-beta1 PublicationAdd BLAST36
Repeati408 – 4401-gamma1 PublicationAdd BLAST33
Domaini441 – 566Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST126
Repeati452 – 4892-alpha1 PublicationAdd BLAST38
Repeati493 – 5312-beta1 PublicationAdd BLAST39
Repeati534 – 5672-gamma1 PublicationAdd BLAST34

Domaini

The B-chain consists of six tandemly repeated subdomains. Only subdomains 1-alpha and 2-gamma possess a functional carbohydrate-binding site.1 Publication

Sequence similaritiesi

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.

Q41358-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLVAKLLYL AVLAICGLGI HGALTHPRVT PPVYPSVSFN LTGADTYEPF
60 70 80 90 100
LRALQEKVIL GNHTAFDLPV LNPESQVSDS NRFVLVPLTN PSGDTVTLAI
110 120 130 140 150
DVVNLYVVAF SSNGKSYFFS GSTAVQRDNL FVDTTQEELN FTGNYTSLER
160 170 180 190 200
QVGFGRVYIP LGPKSLDQAI SSLRTYTLTA GDTKPLARGL LVVIQMVSEA
210 220 230 240 250
ARFRYIELRI RTSITDASEF TPDLLMLSME NNWSSMSSEI QQAQPGGIFA
260 270 280 290 300
GVVQLRDERN NSIEVTNFRR LFELTYIAVL LYGCAPVTSS SYSNNAIDAQ
310 320 330 340 350
IIKMPVFRGG EYEKVCSVVE VTRRISGWDG LCVDVRYGHY IDGNPVQLRP
360 370 380 390 400
CGNECNQLWT FRTDGTIRWL GKCLTASSSV MIYDCNTVPP EATKWVVSID
410 420 430 440 450
GTITNPHSGL VLTAPQAAEG TALSLENNIH AARQGWTVGD VEPLVTFIVG
460 470 480 490 500
YKQMCLRENG ENNFVWLEDC VLNRVQQEWA LYGDGTIRVN SNRSLCVTSE
510 520 530 540 550
DHEPSDLIVI LKCEGSGNQR WVFNTNGTIS NPNAKLLMDV AQRDVSLRKI
560 570
ILYRPTGNPN QQWITTTHPA
Length:570
Mass (Da):63,102
Last modified:November 1, 1996 - v1
Checksum:iA059E2A3E868B868
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27122 mRNA. Translation: AAC49158.1.
PIRiS62627.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27122 mRNA. Translation: AAC49158.1.
PIRiS62627.

3D structure databases

ProteinModelPortaliQ41358.
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...

Entry informationi

Entry nameiSNAIB_SAMNI
AccessioniPrimary (citable) accession number: Q41358
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2016
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 83 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.